1ID CRU4_ARATH Reviewed; 472 AA. 2AC P15455; Q3E711; Q56Z11; Q9FFH7; 3DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. 4DT 20-JUN-2002, sequence version 2. 5DT 16-MAY-2012, entry version 95. 6DE RecName: Full=12S seed storage protein CRU4; 7DE AltName: Full=Cruciferin 4; 8DE Short=AtCRU4; 9DE AltName: Full=Cruciferin A1; 10DE AltName: Full=Legumin-type globulin storage protein CRU4; 11DE Contains: 12DE RecName: Full=12S seed storage protein CRU4 alpha chain; 13DE AltName: Full=12S seed storage protein CRU4 acidic chain; 14DE Contains: 15DE RecName: Full=12S seed storage protein CRU4 beta chain; 16DE AltName: Full=12S seed storage protein CRU4 basic chain; 17DE Flags: Precursor; 18GN Name=CRU4; Synonyms=CRA1; OrderedLocusNames=At5g44120; 19GN ORFNames=MLN1.4; 20OS Arabidopsis thaliana (Mouse-ear cress). 21OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; 22OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 23OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. 24OX NCBI_TaxID=3702; 25RN [1] 26RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE. 27RC STRAIN=cv. Columbia, and cv. Landsberg erecta; 28RX AGRICOLA=IND91035197; DOI=10.1007/BF00019521; 29RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; 30RT "Molecular cloning, genome organization, expression and evolution of 31RT 12S seed storage protein genes of Arabidopsis thaliana."; 32RL Plant Mol. Biol. 11:805-820(1988). 33RN [2] 34RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 35RC STRAIN=cv. Columbia; 36RX MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215; 37RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., 38RA Miyajima N., Tabata S.; 39RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence 40RT features of the 1.6 Mb regions covered by twenty physically assigned 41RT P1 clones."; 42RL DNA Res. 4:215-230(1997). 43RN [3] 44RP GENOME REANNOTATION. 45RC STRAIN=cv. Columbia; 46RG The Arabidopsis Information Resource (TAIR); 47RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 48RN [4] 49RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 50RC STRAIN=cv. Columbia; 51RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; 52RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., 53RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., 54RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., 55RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., 56RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., 57RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., 58RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., 59RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., 60RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., 61RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., 62RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., 63RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; 64RT "Empirical analysis of transcriptional activity in the Arabidopsis 65RT genome."; 66RL Science 302:842-846(2003). 67RN [5] 68RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 69RC STRAIN=cv. Columbia; 70RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.; 71RT "Arabidopsis ORF clones."; 72RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 73RN [6] 74RP PROTEIN SEQUENCE OF 126-134, AND PROTEOLYSIS. 75RX PubMed=14688293; DOI=10.1105/tpc.016378; 76RA Gruis D., Schulze J., Jung R.; 77RT "Storage protein accumulation in the absence of the vacuolar 78RT processing enzyme family of cysteine proteases."; 79RL Plant Cell 16:270-290(2004). 80RN [7] 81RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-472 (ISOFORM 1/2). 82RC STRAIN=cv. Columbia; 83RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., 84RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., 85RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., 86RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., 87RA Hayashizaki Y., Shinozaki K.; 88RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; 89RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. 90RN [8] 91RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472 (ISOFORM 1/2). 92RC STRAIN=cv. Columbia; TISSUE=Green siliques; 93RX MEDLINE=94108489; PubMed=8281187; 94RX DOI=10.1046/j.1365-313X.1993.04061051.x; 95RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., 96RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., 97RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., 98RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., 99RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., 100RA Bardet C., Tremousaygue D., Lescure B.; 101RT "An inventory of 1152 expressed sequence tags obtained by partial 102RT sequencing of cDNAs from Arabidopsis thaliana."; 103RL Plant J. 4:1051-1061(1993). 104RN [9] 105RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY. 106RX PubMed=12417707; DOI=10.1105/tpc.005009; 107RA Gruis D.F., Selinger D.A., Curran J.M., Jung R.; 108RT "Redundant proteolytic mechanisms process seed storage proteins in the 109RT absence of seed-type members of the vacuolar processing enzyme family 110RT of cysteine proteases."; 111RL Plant Cell 14:2863-2882(2002). 112RN [10] 113RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-115; 114RP TYR-312 AND SER-314. 115RX PubMed=17313365; DOI=10.1042/BJ20061569; 116RA Wan L., Ross A.R., Yang J., Hegedus D.D., Kermode A.R.; 117RT "Phosphorylation of the 12 S globulin cruciferin in wild-type and 118RT abi1-1 mutant Arabidopsis thaliana (thale cress) seeds."; 119RL Biochem. J. 404:247-256(2007). 120RN [11] 121RP PROTEOLYSIS, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. 122RX PubMed=17562289; 123RA Li Q., Wang B.-C., Xu Y., Zhu Y.-X.; 124RT "Systematic studies of 12S seed storage protein accumulation and 125RT degradation patterns during Arabidopsis seed maturation and early 126RT seedling germination stages."; 127RL J. Biochem. Mol. Biol. 40:373-381(2007). 128RN [12] 129RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION. 130RX PubMed=18768909; DOI=10.1104/pp.108.124594; 131RA Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B., 132RA Jeannette E.; 133RT "Protein tyrosine kinases and protein tyrosine phosphatases are 134RT involved in abscisic acid-dependent processes in Arabidopsis seeds and 135RT suspension cells."; 136RL Plant Physiol. 148:1668-1680(2008). 137RN [13] 138RP UBIQUITINATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS 139RP SPECTROMETRY. 140RX PubMed=19292762; DOI=10.1111/j.1365-313X.2009.03862.x; 141RA Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., 142RA Vierstra R.D.; 143RT "Tandem affinity purification and mass spectrometric analysis of 144RT ubiquitylated proteins in Arabidopsis."; 145RL Plant J. 59:344-358(2009). 146CC -!- FUNCTION: Seed storage protein. 147CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a 148CC basic chain derived from a single precursor and linked by a 149CC disulfide bond. 150CC -!- SUBCELLULAR LOCATION: Protein storage vacuole (Probable). 151CC -!- ALTERNATIVE PRODUCTS: 152CC Event=Alternative splicing; Named isoforms=2; 153CC Name=1; 154CC IsoId=P15455-1; Sequence=Displayed; 155CC Name=2; 156CC IsoId=P15455-2; Sequence=VSP_026066; 157CC Note=No experimental confirmation available; 158CC -!- TISSUE SPECIFICITY: Accumulates in seeds 8 days after anthesis. 159CC -!- DEVELOPMENTAL STAGE: Detected in siliques at nucleotide level from 160CC 6 days post anthesis (dpa) to 17 dpa. First observed in siliques 161CC at protein level 15 dpa and accumulates progressively as native 162CC isoforms or proteolytic fragments during the last week of seed 163CC maturation/desiccation. Present in dry seeds, essentially in 164CC cotyledons and hypocotyls, but disappears during their germination 165CC (at protein level). 166CC -!- PTM: Ubiquitinated. 167CC -!- PTM: Phosphorylated in seeds on some Tyr residues in response to 168CC abscisic acid (ABA). 169CC -!- PTM: Proteolytically processed during seed maturation at a 170CC conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to 171CC produce two mature polypeptides referred to as alpha and beta 172CC subunits that are joined together by a disulfide bond. 173CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 174CC family. 175CC ----------------------------------------------------------------------- 176CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 177CC Distributed under the Creative Commons Attribution-NoDerivs License 178CC ----------------------------------------------------------------------- 179DR EMBL; M37247; AAA32777.1; -; Genomic_DNA. 180DR EMBL; X14312; CAA32493.1; -; Genomic_DNA. 181DR EMBL; AB005239; BAB10979.1; -; Genomic_DNA. 182DR EMBL; CP002688; AED95062.1; -; Genomic_DNA. 183DR EMBL; CP002688; AED95064.1; -; Genomic_DNA. 184DR EMBL; AY070730; AAL50071.1; -; mRNA. 185DR EMBL; BT029491; ABL66748.1; -; mRNA. 186DR EMBL; AK221158; BAD95189.1; -; mRNA. 187DR EMBL; Z17590; CAA79005.1; -; mRNA. 188DR IPI; IPI00533916; -. 189DR IPI; IPI00542873; -. 190DR PIR; S08509; S08509. 191DR RefSeq; NP_199225.1; NM_123779.4. 192DR RefSeq; NP_851128.1; NM_180797.1. 193DR UniGene; At.20540; -. 194DR UniGene; At.74770; -. 195DR ProteinModelPortal; P15455; -. 196DR SMR; P15455; 30-459. 197DR STRING; P15455; -. 198DR PRIDE; P15455; -. 199DR EnsemblPlants; AT5G44120; AT5G44120; AT5G44120. 200DR GeneID; 834435; -. 201DR GenomeReviews; BA000015_GR; AT5G44120. 202DR KEGG; ath:AT5G44120; -. 203DR TAIR; At5g44120; -. 204DR eggNOG; NOG261521; -. 205DR HOGENOM; HOG000217279; -. 206DR InParanoid; P15455; -. 207DR OMA; ANAQINT; -. 208DR PhylomeDB; P15455; -. 209DR ProtClustDB; CLSN2679899; -. 210DR ArrayExpress; P15455; -. 211DR Genevestigator; P15455; -. 212DR GO; GO:0000326; C:protein storage vacuole; IEA:UniProtKB-SubCell. 213DR GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB. 214DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IDA:UniProtKB. 215DR GO; GO:0010431; P:seed maturation; IDA:UniProtKB. 216DR Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2. 217DR InterPro; IPR022379; 11S_seedstore_CS. 218DR InterPro; IPR006044; 11S_seedstore_pln. 219DR InterPro; IPR006045; Cupin_1. 220DR InterPro; IPR011051; Cupin_RmlC_type. 221DR InterPro; IPR014710; RmlC-like_jellyroll. 222DR Pfam; PF00190; Cupin_1; 2. 223DR PRINTS; PR00439; 11SGLOBULIN. 224DR SMART; SM00835; Cupin_1; 2. 225DR SUPFAM; SSF51182; RmlC_like_cupin; 1. 226DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. 227PE 1: Evidence at protein level; 228KW Alternative splicing; Complete proteome; Direct protein sequencing; 229KW Disulfide bond; Phosphoprotein; Reference proteome; 230KW Seed storage protein; Signal; Storage protein; Ubl conjugation; 231KW Vacuole. 232FT SIGNAL 1 24 By similarity. 233FT CHAIN 25 282 12S seed storage protein CRU4 alpha chain 234FT (By similarity). 235FT /FTId=PRO_0000031999. 236FT CHAIN 283 472 12S seed storage protein CRU4 beta chain 237FT (By similarity). 238FT /FTId=PRO_0000032000. 239FT MOD_RES 52 52 Phosphoserine (By similarity). 240FT MOD_RES 77 77 Phosphotyrosine (By similarity). 241FT MOD_RES 96 96 Phosphoserine (By similarity). 242FT MOD_RES 115 115 Phosphothreonine. 243FT MOD_RES 312 312 Phosphotyrosine. 244FT MOD_RES 314 314 Phosphoserine. 245FT MOD_RES 408 408 Phosphothreonine (By similarity). 246FT MOD_RES 433 433 Phosphothreonine (By similarity). 247FT MOD_RES 450 450 Phosphothreonine (By similarity). 248FT DISULFID 36 69 By similarity. 249FT DISULFID 112 289 Interchain (between alpha and beta 250FT chains) (Potential). 251FT VAR_SEQ 1 104 Missing (in isoform 2). 252FT /FTId=VSP_026066. 253FT CONFLICT 167 167 E -> Q (in Ref. 1; AAA32777/CAA32493). 254FT CONFLICT 356 356 V -> E (in Ref. 1; AAA32777/CAA32493). 255SQ SEQUENCE 472 AA; 52595 MW; 700B468E4D251994 CRC64; 256 MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW 257 DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS 258 EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH 259 QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN 260 QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP 261 SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE 262 AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR 263 TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA 264// 265ID 5HT1D_TAKRU Reviewed; 379 AA. 266AC P79748; 267DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 268DT 01-MAY-1997, sequence version 1. 269DT 16-MAY-2012, entry version 78. 270DE RecName: Full=5-hydroxytryptamine receptor 1D; 271DE Short=5-HT-1D; 272DE Short=5-HT1D; 273DE Short=5HT1D; 274DE AltName: Full=F1D; 275DE AltName: Full=Serotonin receptor 1D; 276GN Name=htr1d; 277OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 278OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 279OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 280OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 281OC Tetradontoidea; Tetraodontidae; Takifugu. 282OX NCBI_TaxID=31033; 283RN [1] 284RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 285RC TISSUE=Testis; 286RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; 287RA Yamaguchi F., Brenner S.; 288RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes 289RT from the Japanese puffer fish, Fugu rubripes."; 290RL Gene 191:219-223(1997). 291CC -!- FUNCTION: This is one of the several different receptors for 5- 292CC hydroxytryptamine (serotonin), a biogenic hormone that functions 293CC as a neurotransmitter, a hormone, and a mitogen. The activity of 294CC this receptor is mediated by G proteins that inhibit adenylate 295CC cyclase activity (By similarity). 296CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 297CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 298CC ----------------------------------------------------------------------- 299CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 300CC Distributed under the Creative Commons Attribution-NoDerivs License 301CC ----------------------------------------------------------------------- 302DR EMBL; X83865; CAA58745.1; -; Genomic_DNA. 303DR ProteinModelPortal; P79748; -. 304DR SMR; P79748; 121-152. 305DR eggNOG; NOG249628; -. 306DR InParanoid; P79748; -. 307DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 308DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 309DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 310DR InterPro; IPR000505; 5HT1D_rcpt. 311DR InterPro; IPR002231; 5HT_rcpt. 312DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 313DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 314DR Pfam; PF00001; 7tm_1; 1. 315DR PRINTS; PR00514; 5HT1DRECEPTR. 316DR PRINTS; PR01101; 5HTRECEPTOR. 317DR PRINTS; PR00237; GPCRRHODOPSN. 318DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 319DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 320PE 3: Inferred from homology; 321KW Cell membrane; Complete proteome; Disulfide bond; 322KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; 323KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. 324FT CHAIN 1 379 5-hydroxytryptamine receptor 1D. 325FT /FTId=PRO_0000068932. 326FT TOPO_DOM 1 36 Extracellular (By similarity). 327FT TRANSMEM 37 60 Helical; Name=1; (By similarity). 328FT TOPO_DOM 61 73 Cytoplasmic (By similarity). 329FT TRANSMEM 74 96 Helical; Name=2; (By similarity). 330FT TOPO_DOM 97 106 Extracellular (By similarity). 331FT TRANSMEM 107 132 Helical; Name=3; (By similarity). 332FT TOPO_DOM 133 152 Cytoplasmic (By similarity). 333FT TRANSMEM 153 174 Helical; Name=4; (By similarity). 334FT TOPO_DOM 175 192 Extracellular (By similarity). 335FT TRANSMEM 193 216 Helical; Name=5; (By similarity). 336FT TOPO_DOM 217 307 Cytoplasmic (By similarity). 337FT TRANSMEM 308 331 Helical; Name=6; (By similarity). 338FT TOPO_DOM 332 339 Extracellular (By similarity). 339FT TRANSMEM 340 364 Helical; Name=7; (By similarity). 340FT TOPO_DOM 365 379 Cytoplasmic (By similarity). 341FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). 342FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). 343FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). 344FT DISULFID 109 186 By similarity. 345SQ SEQUENCE 379 AA; 42302 MW; 99B6E2C0379EBC78 CRC64; 346 MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT 347 IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC 348 TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH 349 EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA 350 QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR 351 ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY 352 TVFNDEFKQA FQKLIKFRR 353// 354ID ACH2_DROME Reviewed; 576 AA. 355AC P17644; Q0KI18; Q9VC73; 356DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. 357DT 01-AUG-1990, sequence version 1. 358DT 18-APR-2012, entry version 123. 359DE RecName: Full=Acetylcholine receptor subunit alpha-like 2; 360DE Flags: Precursor; 361GN Name=nAcRalpha-96Ab; Synonyms=Acr96Ab, AcrE, sad; ORFNames=CG6844; 362OS Drosophila melanogaster (Fruit fly). 363OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 364OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; 365OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. 366OX NCBI_TaxID=7227; 367RN [1] 368RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND 369RP DEVELOPMENTAL STAGE. 370RC TISSUE=Head; 371RX MEDLINE=90353591; PubMed=2117557; DOI=10.1016/0014-5793(90)81170-S; 372RA Jonas P., Baumann A., Merz B., Gundelfinger E.D.; 373RT "Structure and developmental expression of the D alpha 2 gene encoding 374RT a novel nicotinic acetylcholine receptor protein of Drosophila 375RT melanogaster."; 376RL FEBS Lett. 269:264-268(1990). 377RN [2] 378RP NUCLEOTIDE SEQUENCE [MRNA]. 379RX MEDLINE=90360975; PubMed=1697262; 380RA Sawruk E., Schloss P., Betz H., Schmitt B.; 381RT "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, a 382RT novel developmentally regulated alpha-subunit."; 383RL EMBO J. 9:2671-2677(1990). 384RN [3] 385RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL 386RP STAGE. 387RC TISSUE=Head; 388RX MEDLINE=90301489; PubMed=2114015; DOI=10.1093/nar/18.12.3640; 389RA Baumann A., Jonas P., Gundelfinger E.D.; 390RT "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila 391RT nicotinic acetylcholine receptors."; 392RL Nucleic Acids Res. 18:3640-3640(1990). 393RN [4] 394RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 395RC STRAIN=Berkeley; 396RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; 397RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., 398RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., 399RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., 400RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., 401RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., 402RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 403RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., 404RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., 405RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., 406RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., 407RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., 408RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., 409RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., 410RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., 411RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., 412RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., 413RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., 414RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., 415RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., 416RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., 417RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., 418RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., 419RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., 420RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., 421RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., 422RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., 423RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., 424RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., 425RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., 426RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., 427RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., 428RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., 429RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., 430RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., 431RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., 432RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; 433RT "The genome sequence of Drosophila melanogaster."; 434RL Science 287:2185-2195(2000). 435RN [5] 436RP GENOME REANNOTATION. 437RC STRAIN=Berkeley; 438RX MEDLINE=22426069; PubMed=12537572; 439RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., 440RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., 441RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., 442RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., 443RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., 444RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., 445RA Lewis S.E.; 446RT "Annotation of the Drosophila melanogaster euchromatic genome: a 447RT systematic review."; 448RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). 449RN [6] 450RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 451RC STRAIN=Berkeley; TISSUE=Head; 452RX MEDLINE=22426066; PubMed=12537569; 453RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., 454RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., 455RA Rubin G.M., Celniker S.E.; 456RT "A Drosophila full-length cDNA resource."; 457RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). 458CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an 459CC extensive change in conformation that affects all subunits and 460CC leads to opening of an ion-conducting channel across the plasma 461CC membrane. 462CC -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell 463CC membrane; Multi-pass membrane protein. Cell membrane; Multi-pass 464CC membrane protein. 465CC -!- TISSUE SPECIFICITY: CNS in embryos. 466CC -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages. 467CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) 468CC family. Acetylcholine receptor (TC 1.A.9.1) subfamily. 469CC ----------------------------------------------------------------------- 470CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 471CC Distributed under the Creative Commons Attribution-NoDerivs License 472CC ----------------------------------------------------------------------- 473DR EMBL; X52274; CAA36517.1; -; mRNA. 474DR EMBL; X53583; CAA37652.1; -; mRNA. 475DR EMBL; AE014297; AAF56302.2; -; Genomic_DNA. 476DR EMBL; AY058446; AAL13675.1; -; mRNA. 477DR PIR; S11679; ACFFA2. 478DR RefSeq; NP_524482.1; NM_079758.2. 479DR RefSeq; NP_733001.1; NM_170146.1. 480DR UniGene; Dm.2363; -. 481DR ProteinModelPortal; P17644; -. 482DR SMR; P17644; 42-547. 483DR DIP; DIP-22674N; -. 484DR IntAct; P17644; 1. 485DR MINT; MINT-888559; -. 486DR STRING; P17644; -. 487DR PRIDE; P17644; -. 488DR EnsemblMetazoa; FBtr0084639; FBpp0084023; FBgn0000039. 489DR EnsemblMetazoa; FBtr0084640; FBpp0084024; FBgn0000039. 490DR GeneID; 42919; -. 491DR KEGG; dme:Dmel_CG6844; -. 492DR CTD; 42919; -. 493DR FlyBase; FBgn0000039; nAcRalpha-96Ab. 494DR eggNOG; NOG290206; -. 495DR GeneTree; ENSGT00630000089708; -. 496DR InParanoid; P17644; -. 497DR KO; K05312; -. 498DR OMA; LELCHPP; -. 499DR OrthoDB; EOG4W6MB5; -. 500DR PhylomeDB; P17644; -. 501DR NextBio; 831266; -. 502DR ArrayExpress; P17644; -. 503DR Bgee; P17644; -. 504DR GermOnline; CG6844; Drosophila melanogaster. 505DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. 506DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 507DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 508DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. 509DR GO; GO:0004889; F:acetylcholine-activated cation-selective channel activity; IEA:InterPro. 510DR GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW. 511DR Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1. 512DR InterPro; IPR006202; Neur_chan_lig-bd. 513DR InterPro; IPR006201; Neur_channel. 514DR InterPro; IPR006029; Neurotrans-gated_channel_TM. 515DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. 516DR InterPro; IPR002394; Nicotinic_acetylcholine_rcpt. 517DR PANTHER; PTHR18945; Neur_channel; 1. 518DR Pfam; PF02931; Neur_chan_LBD; 1. 519DR Pfam; PF02932; Neur_chan_memb; 1. 520DR PRINTS; PR00254; NICOTINICR. 521DR PRINTS; PR00252; NRIONCHANNEL. 522DR SUPFAM; SSF90112; Neu_channel_TM; 1. 523DR SUPFAM; SSF63712; Neur_chan_LBD; 1. 524DR TIGRFAMs; TIGR00860; LIC; 1. 525DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. 526PE 2: Evidence at transcript level; 527KW Cell junction; Cell membrane; Complete proteome; Disulfide bond; 528KW Glycoprotein; Ion transport; Ionic channel; Ligand-gated ion channel; 529KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; 530KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport. 531FT SIGNAL 1 21 Probable. 532FT CHAIN 22 576 Acetylcholine receptor subunit alpha-like 533FT 2. 534FT /FTId=PRO_0000000300. 535FT TOPO_DOM 22 261 Extracellular (Potential). 536FT TRANSMEM 262 285 Helical; (Potential). 537FT TRANSMEM 293 311 Helical; (Potential). 538FT TRANSMEM 327 346 Helical; (Potential). 539FT TOPO_DOM 347 526 Cytoplasmic (Potential). 540FT TRANSMEM 527 545 Helical; (Potential). 541FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). 542FT CARBOHYD 254 254 N-linked (GlcNAc...) (Potential). 543FT CARBOHYD 570 570 N-linked (GlcNAc...) (Potential). 544FT DISULFID 169 183 By similarity. 545FT DISULFID 243 244 Associated with receptor activation (By 546FT similarity). 547SQ SEQUENCE 576 AA; 65506 MW; 97D6A46CADC3F42F CRC64; 548 MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI 549 RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY 550 VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ 551 QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY 552 YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL 553 LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP 554 WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD 555 SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV 556 AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT 557 FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN 558// 559ID ACTB1_TAKRU Reviewed; 375 AA. 560AC P68142; P53484; 561DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. 562DT 25-OCT-2004, sequence version 1. 563DT 16-MAY-2012, entry version 49. 564DE RecName: Full=Actin, cytoplasmic 1; 565DE AltName: Full=Beta-actin A; 566DE Contains: 567DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed; 568GN Name=actba; 569OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 570OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 571OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 572OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 573OC Tetradontoidea; Tetraodontidae; Takifugu. 574OX NCBI_TaxID=31033; 575RN [1] 576RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 577RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 578RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 579RT "Isolation, characterization and evolution of nine pufferfish (Fugu 580RT rubripes) actin genes."; 581RL J. Mol. Biol. 259:655-665(1996). 582CC -!- FUNCTION: Actins are highly conserved proteins that are involved 583CC in various types of cell motility and are ubiquitously expressed 584CC in all eukaryotic cells. 585CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 586CC structural filament (F-actin) in the form of a two-stranded helix. 587CC Each actin can bind to 4 others. 588CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 589CC -!- TISSUE SPECIFICITY: Widely distributed. Not expressed in skeletal 590CC muscle. 591CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to 592CC form methionine sulfoxide promotes actin filament 593CC depolymerization. Methionine sulfoxide is produced 594CC stereospecifically, but it is not known whether the (S)-S-oxide or 595CC the (R)-S-oxide is produced (By similarity). 596CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 597CC alpha, beta and gamma have been identified. The alpha actins are 598CC found in muscle tissues and are a major constituent of the 599CC contractile apparatus. The beta and gamma actins coexist in most 600CC cell types as components of the cytoskeleton and as mediators of 601CC internal cell motility. 602CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins 603CC in Fugu rubripes. 604CC -!- SIMILARITY: Belongs to the actin family. 605CC ----------------------------------------------------------------------- 606CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 607CC Distributed under the Creative Commons Attribution-NoDerivs License 608CC ----------------------------------------------------------------------- 609DR EMBL; U37499; AAC59889.1; -; Genomic_DNA. 610DR PIR; S71124; S71124. 611DR ProteinModelPortal; P68142; -. 612DR SMR; P68142; 2-375. 613DR Ensembl; ENSTRUT00000013141; ENSTRUP00000013080; ENSTRUG00000005447. 614DR eggNOG; COG5277; -. 615DR GeneTree; ENSGT00630000089629; -. 616DR InParanoid; P68142; -. 617DR OMA; IKNLMER; -. 618DR OrthoDB; EOG41JZC9; -. 619DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 620DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 621DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 622DR InterPro; IPR004000; Actin-like. 623DR InterPro; IPR020902; Actin/actin-like_CS. 624DR InterPro; IPR004001; Actin_CS. 625DR PANTHER; PTHR11937; Actin_like; 1. 626DR Pfam; PF00022; Actin; 1. 627DR PRINTS; PR00190; ACTIN. 628DR SMART; SM00268; ACTIN; 1. 629DR PROSITE; PS00406; ACTINS_1; 1. 630DR PROSITE; PS00432; ACTINS_2; 1. 631DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 632PE 2: Evidence at transcript level; 633KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 634KW Methylation; Nucleotide-binding; Oxidation; Reference proteome. 635FT CHAIN 1 375 Actin, cytoplasmic 1. 636FT /FTId=PRO_0000367094. 637FT INIT_MET 1 1 Removed; alternate (By similarity). 638FT CHAIN 2 375 Actin, cytoplasmic 1, N-terminally 639FT processed. 640FT /FTId=PRO_0000000809. 641FT MOD_RES 1 1 N-acetylmethionine; in Actin, cytoplasmic 642FT 1; alternate (By similarity). 643FT MOD_RES 2 2 N-acetylglutamate; in Actin, cytoplasmic 644FT 1, N-terminally processed (By 645FT similarity). 646FT MOD_RES 44 44 Methionine sulfoxide (By similarity). 647FT MOD_RES 73 73 Tele-methylhistidine (By similarity). 648SQ SEQUENCE 375 AA; 41767 MW; 9C505616D33E9495 CRC64; 649 MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 650 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 651 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 652 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY 653 ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS 654 GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 655 EYDESGPSIV HRKCF 656// 657ID ACTB2_TAKRU Reviewed; 375 AA. 658AC P53485; 659DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 660DT 01-OCT-1996, sequence version 1. 661DT 16-MAY-2012, entry version 69. 662DE RecName: Full=Actin, cytoplasmic 2; 663DE AltName: Full=Beta-actin B; 664DE Contains: 665DE RecName: Full=Actin, cytoplasmic 2, N-terminally processed; 666GN Name=actbb; 667OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 668OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 669OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 670OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 671OC Tetradontoidea; Tetraodontidae; Takifugu. 672OX NCBI_TaxID=31033; 673RN [1] 674RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 675RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 676RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 677RT "Isolation, characterization and evolution of nine pufferfish (Fugu 678RT rubripes) actin genes."; 679RL J. Mol. Biol. 259:655-665(1996). 680CC -!- FUNCTION: Actins are highly conserved proteins that are involved 681CC in various types of cell motility and are ubiquitously expressed 682CC in all eukaryotic cells. 683CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 684CC structural filament (F-actin) in the form of a two-stranded helix. 685CC Each actin can bind to 4 others. 686CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 687CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to 688CC form methionine sulfoxide promotes actin filament 689CC depolymerization. Methionine sulfoxide is produced 690CC stereospecifically, but it is not known whether the (S)-S-oxide or 691CC the (R)-S-oxide is produced (By similarity). 692CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 693CC alpha, beta and gamma have been identified. The alpha actins are 694CC found in muscle tissues and are a major constituent of the 695CC contractile apparatus. The beta and gamma actins coexist in most 696CC cell types as components of the cytoskeleton and as mediators of 697CC internal cell motility. 698CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins 699CC in Fugu rubripes. 700CC -!- SIMILARITY: Belongs to the actin family. 701CC ----------------------------------------------------------------------- 702CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 703CC Distributed under the Creative Commons Attribution-NoDerivs License 704CC ----------------------------------------------------------------------- 705DR EMBL; U38848; AAC59890.1; -; Genomic_DNA. 706DR PIR; S71125; S71125. 707DR ProteinModelPortal; P53485; -. 708DR SMR; P53485; 2-375. 709DR eggNOG; COG5277; -. 710DR InParanoid; P53485; -. 711DR OrthoDB; EOG41JZC9; -. 712DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 713DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 714DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 715DR InterPro; IPR004000; Actin-like. 716DR InterPro; IPR020902; Actin/actin-like_CS. 717DR InterPro; IPR004001; Actin_CS. 718DR Pfam; PF00022; Actin; 1. 719DR PRINTS; PR00190; ACTIN. 720DR SMART; SM00268; ACTIN; 1. 721DR PROSITE; PS00406; ACTINS_1; 1. 722DR PROSITE; PS00432; ACTINS_2; 1. 723DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 724PE 3: Inferred from homology; 725KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 726KW Methylation; Nucleotide-binding; Oxidation; Reference proteome. 727FT CHAIN 1 375 Actin, cytoplasmic 2. 728FT /FTId=PRO_0000367095. 729FT INIT_MET 1 1 Removed; alternate (By similarity). 730FT CHAIN 2 375 Actin, cytoplasmic 2, N-terminally 731FT processed. 732FT /FTId=PRO_0000000811. 733FT MOD_RES 1 1 N-acetylmethionine; in Actin, cytoplasmic 734FT 2; alternate (By similarity). 735FT MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic 736FT 2, N-terminally processed (By 737FT similarity). 738FT MOD_RES 44 44 Methionine sulfoxide (By similarity). 739FT MOD_RES 73 73 Tele-methylhistidine (By similarity). 740SQ SEQUENCE 375 AA; 41767 MW; 1AE990BC0AED0D1C CRC64; 741 MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 742 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 743 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 744 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY 745 ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 746 GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 747 EYDESGPSIV HRKCF 748// 749ID ACTB3_TAKRU Reviewed; 375 AA. 750AC P53486; 751DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 752DT 01-OCT-1996, sequence version 1. 753DT 16-MAY-2012, entry version 71. 754DE RecName: Full=Actin, cytoplasmic 3; 755DE AltName: Full=Beta-actin C; 756DE Contains: 757DE RecName: Full=Actin, cytoplasmic 3, N-terminally processed; 758GN Name=actbc; 759OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 760OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 761OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 762OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 763OC Tetradontoidea; Tetraodontidae; Takifugu. 764OX NCBI_TaxID=31033; 765RN [1] 766RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 767RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 768RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 769RT "Isolation, characterization and evolution of nine pufferfish (Fugu 770RT rubripes) actin genes."; 771RL J. Mol. Biol. 259:655-665(1996). 772CC -!- FUNCTION: Actins are highly conserved proteins that are involved 773CC in various types of cell motility and are ubiquitously expressed 774CC in all eukaryotic cells. 775CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 776CC structural filament (F-actin) in the form of a two-stranded helix. 777CC Each actin can bind to 4 others. 778CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 779CC -!- TISSUE SPECIFICITY: Predominantly expressed in gills, kidney and 780CC skin. 781CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to 782CC form methionine sulfoxide promotes actin filament 783CC depolymerization. Methionine sulfoxide is produced 784CC stereospecifically, but it is not known whether the (S)-S-oxide or 785CC the (R)-S-oxide is produced (By similarity). 786CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 787CC alpha, beta and gamma have been identified. The alpha actins are 788CC found in muscle tissues and are a major constituent of the 789CC contractile apparatus. The beta and gamma actins coexist in most 790CC cell types as components of the cytoskeleton and as mediators of 791CC internal cell motility. 792CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins 793CC in Fugu rubripes. 794CC -!- SIMILARITY: Belongs to the actin family. 795CC ----------------------------------------------------------------------- 796CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 797CC Distributed under the Creative Commons Attribution-NoDerivs License 798CC ----------------------------------------------------------------------- 799DR EMBL; U38849; AAC59891.1; -; Genomic_DNA. 800DR PIR; S71126; S71126. 801DR ProteinModelPortal; P53486; -. 802DR SMR; P53486; 2-375. 803DR STRING; P53486; -. 804DR PRIDE; P53486; -. 805DR eggNOG; COG5277; -. 806DR InParanoid; P53486; -. 807DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 808DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 809DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 810DR InterPro; IPR004000; Actin-like. 811DR InterPro; IPR020902; Actin/actin-like_CS. 812DR InterPro; IPR004001; Actin_CS. 813DR PANTHER; PTHR11937; Actin_like; 1. 814DR Pfam; PF00022; Actin; 1. 815DR PRINTS; PR00190; ACTIN. 816DR SMART; SM00268; ACTIN; 1. 817DR PROSITE; PS00406; ACTINS_1; 1. 818DR PROSITE; PS00432; ACTINS_2; 1. 819DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 820PE 2: Evidence at transcript level; 821KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 822KW Methylation; Nucleotide-binding; Oxidation; Reference proteome. 823FT CHAIN 1 375 Actin, cytoplasmic 3. 824FT /FTId=PRO_0000367096. 825FT INIT_MET 1 1 Removed; alternate (By similarity). 826FT CHAIN 2 375 Actin, cytoplasmic 3, N-terminally 827FT processed. 828FT /FTId=PRO_0000000841. 829FT MOD_RES 1 1 N-acetylmethionine; in Actin, cytoplasmic 830FT 3; alternate (By similarity). 831FT MOD_RES 2 2 N-acetylglutamate; in Actin, cytoplasmic 832FT 3, N-terminally processed (By 833FT similarity). 834FT MOD_RES 44 44 Methionine sulfoxide (By similarity). 835FT MOD_RES 73 73 Tele-methylhistidine (By similarity). 836SQ SEQUENCE 375 AA; 41783 MW; 8B451E0DB3399C0B CRC64; 837 MEDEVASLVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 838 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 839 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 840 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA SSSSSLEKSY 841 ELPDGQVITI GNERFRCPEA LFQPSFLGME SSGIHETTYN SIMKCDVDIR KDLYANTVLS 842 GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 843 EYDESGPSIV HRKCF 844// 845ID ACTB_OREMO Reviewed; 375 AA. 846AC P68143; P53484; 847DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. 848DT 25-OCT-2004, sequence version 1. 849DT 18-APR-2012, entry version 37. 850DE RecName: Full=Actin, cytoplasmic 1; 851DE AltName: Full=Beta-actin; 852DE Contains: 853DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed; 854GN Name=actb; 855OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica). 856OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 857OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 858OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei; 859OC Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini; 860OC Oreochromis. 861OX NCBI_TaxID=8127; 862RN [1] 863RP NUCLEOTIDE SEQUENCE [MRNA]. 864RC TISSUE=Gill; 865RA Takeuchi K.; 866RT "Cloning of Tilapia actin cDNAs."; 867RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. 868CC -!- FUNCTION: Actins are highly conserved proteins that are involved 869CC in various types of cell motility and are ubiquitously expressed 870CC in all eukaryotic cells. 871CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 872CC structural filament (F-actin) in the form of a two-stranded helix. 873CC Each actin can bind to 4 others. 874CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 875CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to 876CC form methionine sulfoxide promotes actin filament 877CC depolymerization. Methionine sulfoxide is produced 878CC stereospecifically, but it is not known whether the (S)-S-oxide or 879CC the (R)-S-oxide is produced (By similarity). 880CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 881CC alpha, beta and gamma have been identified. The alpha actins are 882CC found in muscle tissues and are a major constituent of the 883CC contractile apparatus. The beta and gamma actins coexist in most 884CC cell types as components of the cytoskeleton and as mediators of 885CC internal cell motility. 886CC -!- SIMILARITY: Belongs to the actin family. 887CC ----------------------------------------------------------------------- 888CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 889CC Distributed under the Creative Commons Attribution-NoDerivs License 890CC ----------------------------------------------------------------------- 891DR EMBL; AB037865; BAA90688.1; -; mRNA. 892DR ProteinModelPortal; P68143; -. 893DR SMR; P68143; 2-375. 894DR HOVERGEN; HBG003771; -. 895DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 896DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 897DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 898DR InterPro; IPR004000; Actin-like. 899DR InterPro; IPR020902; Actin/actin-like_CS. 900DR InterPro; IPR004001; Actin_CS. 901DR PANTHER; PTHR11937; Actin_like; 1. 902DR Pfam; PF00022; Actin; 1. 903DR PRINTS; PR00190; ACTIN. 904DR SMART; SM00268; ACTIN; 1. 905DR PROSITE; PS00406; ACTINS_1; 1. 906DR PROSITE; PS00432; ACTINS_2; 1. 907DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 908PE 2: Evidence at transcript level; 909KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation; 910KW Nucleotide-binding; Oxidation. 911FT CHAIN 1 375 Actin, cytoplasmic 1. 912FT /FTId=PRO_0000367091. 913FT INIT_MET 1 1 Removed; alternate (By similarity). 914FT CHAIN 2 375 Actin, cytoplasmic 1, N-terminally 915FT processed. 916FT /FTId=PRO_0000000803. 917FT MOD_RES 1 1 N-acetylmethionine; in Actin, cytoplasmic 918FT 1; alternate (By similarity). 919FT MOD_RES 2 2 N-acetylglutamate; in Actin, cytoplasmic 920FT 1, N-terminally processed (By 921FT similarity). 922FT MOD_RES 44 44 Methionine sulfoxide (By similarity). 923FT MOD_RES 73 73 Tele-methylhistidine (By similarity). 924SQ SEQUENCE 375 AA; 41767 MW; 9C505616D33E9495 CRC64; 925 MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 926 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 927 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 928 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY 929 ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS 930 GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 931 EYDESGPSIV HRKCF 932// 933ID ACTC_TAKRU Reviewed; 377 AA. 934AC P53480; 935DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 936DT 01-OCT-1996, sequence version 1. 937DT 16-MAY-2012, entry version 76. 938DE RecName: Full=Actin, alpha cardiac; 939DE Flags: Precursor; 940OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 941OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 942OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 943OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 944OC Tetradontoidea; Tetraodontidae; Takifugu. 945OX NCBI_TaxID=31033; 946RN [1] 947RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 948RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 949RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 950RT "Isolation, characterization and evolution of nine pufferfish (Fugu 951RT rubripes) actin genes."; 952RL J. Mol. Biol. 259:655-665(1996). 953CC -!- FUNCTION: Actins are highly conserved proteins that are involved 954CC in various types of cell motility and are ubiquitously expressed 955CC in all eukaryotic cells. 956CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 957CC structural filament (F-actin) in the form of a two-stranded helix. 958CC Each actin can bind to 4 others. 959CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 960CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart. Lower levels 961CC in skeletal muscle and skin. 962CC -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to 963CC form methionine sulfoxide promotes actin filament 964CC depolymerization. Methionine sulfoxide is produced 965CC stereospecifically, but it is not known whether the (S)-S-oxide or 966CC the (R)-S-oxide is produced (By similarity). 967CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 968CC alpha, beta and gamma have been identified. The alpha actins are 969CC found in muscle tissues and are a major constituent of the 970CC contractile apparatus. The beta and gamma actins coexist in most 971CC cell types as components of the cytoskeleton and as mediators of 972CC internal cell motility. 973CC -!- MISCELLANEOUS: There are three genes coding for cardiac actin in 974CC Fugu. 975CC -!- SIMILARITY: Belongs to the actin family. 976CC ----------------------------------------------------------------------- 977CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 978CC Distributed under the Creative Commons Attribution-NoDerivs License 979CC ----------------------------------------------------------------------- 980DR EMBL; U38959; AAC59894.1; -; Genomic_DNA. 981DR EMBL; U38960; AAC59895.1; -; Genomic_DNA. 982DR EMBL; U38961; AAC59896.1; -; Genomic_DNA. 983DR PIR; S71120; S71120. 984DR ProteinModelPortal; P53480; -. 985DR Ensembl; ENSTRUT00000011488; ENSTRUP00000011428; ENSTRUG00000004787. 986DR Ensembl; ENSTRUT00000036073; ENSTRUP00000035943; ENSTRUG00000014049. 987DR Ensembl; ENSTRUT00000046301; ENSTRUP00000046146; ENSTRUG00000018009. 988DR GeneTree; ENSGT00390000011529; -. 989DR GeneTree; ENSGT00630000089596; -. 990DR InParanoid; P53480; -. 991DR OMA; IXMESAG; -. 992DR OrthoDB; EOG4W9J40; -. 993DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 994DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 995DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 996DR InterPro; IPR004000; Actin-like. 997DR InterPro; IPR020902; Actin/actin-like_CS. 998DR InterPro; IPR004001; Actin_CS. 999DR PANTHER; PTHR11937; Actin_like; 1. 1000DR Pfam; PF00022; Actin; 1. 1001DR PRINTS; PR00190; ACTIN. 1002DR SMART; SM00268; ACTIN; 1. 1003DR PROSITE; PS00406; ACTINS_1; 1. 1004DR PROSITE; PS00432; ACTINS_2; 1. 1005DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 1006PE 2: Evidence at transcript level; 1007KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 1008KW Methylation; Muscle protein; Nucleotide-binding; Oxidation; 1009KW Reference proteome. 1010FT PROPEP 1 2 Removed in mature form (By similarity). 1011FT /FTId=PRO_0000000826. 1012FT CHAIN 3 377 Actin, alpha cardiac. 1013FT /FTId=PRO_0000000827. 1014FT MOD_RES 3 3 N-acetylaspartate (By similarity). 1015FT MOD_RES 46 46 Methionine sulfoxide (By similarity). 1016FT MOD_RES 75 75 Tele-methylhistidine (By similarity). 1017SQ SEQUENCE 377 AA; 41975 MW; 0499A43921D9BBCF CRC64; 1018 MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 1019 QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK 1020 MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL 1021 DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 1022 SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV 1023 LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS 1024 KQEYDEAGPS IVHRKCF 1025// 1026ID ACTSA_TAKRU Reviewed; 377 AA. 1027AC P68140; P53481; 1028DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. 1029DT 25-OCT-2004, sequence version 1. 1030DT 16-MAY-2012, entry version 48. 1031DE RecName: Full=Actin, alpha skeletal muscle A; 1032DE AltName: Full=Alpha-actin-1 A; 1033DE Flags: Precursor; 1034GN Name=acta1a; 1035OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 1036OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 1037OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 1038OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 1039OC Tetradontoidea; Tetraodontidae; Takifugu. 1040OX NCBI_TaxID=31033; 1041RN [1] 1042RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 1043RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 1044RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 1045RT "Isolation, characterization and evolution of nine pufferfish (Fugu 1046RT rubripes) actin genes."; 1047RL J. Mol. Biol. 259:655-665(1996). 1048CC -!- FUNCTION: Actins are highly conserved proteins that are involved 1049CC in various types of cell motility and are ubiquitously expressed 1050CC in all eukaryotic cells. 1051CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 1052CC structural filament (F-actin) in the form of a two-stranded helix. 1053CC Each actin can bind to 4 others. 1054CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 1055CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. 1056CC Lower levels in heart. 1057CC -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to 1058CC form methionine sulfoxide promotes actin filament 1059CC depolymerization. Methionine sulfoxide is produced 1060CC stereospecifically, but it is not known whether the (S)-S-oxide or 1061CC the (R)-S-oxide is produced (By similarity). 1062CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 1063CC alpha, beta and gamma have been identified. The alpha actins are 1064CC found in muscle tissues and are a major constituent of the 1065CC contractile apparatus. The beta and gamma actins coexist in most 1066CC cell types as components of the cytoskeleton and as mediators of 1067CC internal cell motility. 1068CC -!- MISCELLANEOUS: There are two different alpha-skeletal actins in 1069CC Fugu rubripes. 1070CC -!- SIMILARITY: Belongs to the actin family. 1071CC ----------------------------------------------------------------------- 1072CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1073CC Distributed under the Creative Commons Attribution-NoDerivs License 1074CC ----------------------------------------------------------------------- 1075DR EMBL; U38850; AAC59892.1; -; Genomic_DNA. 1076DR PIR; S71118; S71118. 1077DR ProteinModelPortal; P68140; -. 1078DR SMR; P68140; 6-377. 1079DR Ensembl; ENSTRUT00000019970; ENSTRUP00000019889; ENSTRUG00000007989. 1080DR eggNOG; COG5277; -. 1081DR GeneTree; ENSGT00630000089596; -. 1082DR InParanoid; P68140; -. 1083DR OMA; MIGMENP; -. 1084DR OrthoDB; EOG4W9J40; -. 1085DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 1086DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 1087DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 1088DR InterPro; IPR004000; Actin-like. 1089DR InterPro; IPR020902; Actin/actin-like_CS. 1090DR InterPro; IPR004001; Actin_CS. 1091DR PANTHER; PTHR11937; Actin_like; 1. 1092DR Pfam; PF00022; Actin; 1. 1093DR PRINTS; PR00190; ACTIN. 1094DR SMART; SM00268; ACTIN; 1. 1095DR PROSITE; PS00406; ACTINS_1; 1. 1096DR PROSITE; PS00432; ACTINS_2; 1. 1097DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 1098PE 2: Evidence at transcript level; 1099KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 1100KW Methylation; Muscle protein; Nucleotide-binding; Oxidation; 1101KW Reference proteome. 1102FT PROPEP 1 2 Removed in mature form (By similarity). 1103FT /FTId=PRO_0000000862. 1104FT CHAIN 3 377 Actin, alpha skeletal muscle A. 1105FT /FTId=PRO_0000000863. 1106FT MOD_RES 3 3 N-acetylaspartate (By similarity). 1107FT MOD_RES 46 46 Methionine sulfoxide (By similarity). 1108FT MOD_RES 75 75 Tele-methylhistidine (By similarity). 1109SQ SEQUENCE 377 AA; 41945 MW; 1C7185C0F7C19A26 CRC64; 1110 MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 1111 QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK 1112 MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL 1113 DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 1114 SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV 1115 LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS 1116 KQEYDEAGPS IVHRKCF 1117// 1118ID ACTSB_TAKRU Reviewed; 377 AA. 1119AC P53482; 1120DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 1121DT 01-OCT-1996, sequence version 1. 1122DT 16-MAY-2012, entry version 69. 1123DE RecName: Full=Actin, alpha skeletal muscle B; 1124DE AltName: Full=Alpha-actin-1 B; 1125DE Flags: Precursor; 1126GN Name=acta1b; 1127OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 1128OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 1129OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 1130OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 1131OC Tetradontoidea; Tetraodontidae; Takifugu. 1132OX NCBI_TaxID=31033; 1133RN [1] 1134RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 1135RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 1136RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 1137RT "Isolation, characterization and evolution of nine pufferfish (Fugu 1138RT rubripes) actin genes."; 1139RL J. Mol. Biol. 259:655-665(1996). 1140CC -!- FUNCTION: Actins are highly conserved proteins that are involved 1141CC in various types of cell motility and are ubiquitously expressed 1142CC in all eukaryotic cells. 1143CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 1144CC structural filament (F-actin) in the form of a two-stranded helix. 1145CC Each actin can bind to 4 others. 1146CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 1147CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. 1148CC Lower levels in heart, gills and skin. 1149CC -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to 1150CC form methionine sulfoxide promotes actin filament 1151CC depolymerization. Methionine sulfoxide is produced 1152CC stereospecifically, but it is not known whether the (S)-S-oxide or 1153CC the (R)-S-oxide is produced (By similarity). 1154CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 1155CC alpha, beta and gamma have been identified. The alpha actins are 1156CC found in muscle tissues and are a major constituent of the 1157CC contractile apparatus. The beta and gamma actins coexist in most 1158CC cell types as components of the cytoskeleton and as mediators of 1159CC internal cell motility. 1160CC -!- MISCELLANEOUS: There are two different alpha-skeletal actins in 1161CC Fugu rubripes. 1162CC -!- SIMILARITY: Belongs to the actin family. 1163CC ----------------------------------------------------------------------- 1164CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1165CC Distributed under the Creative Commons Attribution-NoDerivs License 1166CC ----------------------------------------------------------------------- 1167DR EMBL; U38958; AAC59893.1; -; Genomic_DNA. 1168DR PIR; S71119; S71119. 1169DR ProteinModelPortal; P53482; -. 1170DR SMR; P53482; 6-377. 1171DR InParanoid; P53482; -. 1172DR OrthoDB; EOG4W9J40; -. 1173DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 1174DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 1175DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 1176DR InterPro; IPR004000; Actin-like. 1177DR InterPro; IPR020902; Actin/actin-like_CS. 1178DR InterPro; IPR004001; Actin_CS. 1179DR PANTHER; PTHR11937; Actin_like; 1. 1180DR Pfam; PF00022; Actin; 1. 1181DR PRINTS; PR00190; ACTIN. 1182DR SMART; SM00268; ACTIN; 1. 1183DR PROSITE; PS00406; ACTINS_1; 1. 1184DR PROSITE; PS00432; ACTINS_2; 1. 1185DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 1186PE 2: Evidence at transcript level; 1187KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 1188KW Methylation; Muscle protein; Nucleotide-binding; Oxidation; 1189KW Reference proteome. 1190FT PROPEP 1 2 Removed in mature form (By similarity). 1191FT /FTId=PRO_0000000864. 1192FT CHAIN 3 377 Actin, alpha skeletal muscle B. 1193FT /FTId=PRO_0000000865. 1194FT MOD_RES 3 3 N-acetylaspartate (By similarity). 1195FT MOD_RES 46 46 Methionine sulfoxide (By similarity). 1196FT MOD_RES 75 75 Tele-methylhistidine (By similarity). 1197SQ SEQUENCE 377 AA; 41977 MW; A0973DD7B23B0C82 CRC64; 1198 MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 1199 QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK 1200 MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL 1201 DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMG TAASSSSLEK 1202 SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 1203 LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS 1204 KQEYDEAGPS IVHRKCF 1205// 1206ID ACTS_OREMO Reviewed; 377 AA. 1207AC P68264; P53481; 1208DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. 1209DT 25-OCT-2004, sequence version 1. 1210DT 18-APR-2012, entry version 36. 1211DE RecName: Full=Actin, alpha skeletal muscle; 1212DE AltName: Full=Alpha-actin-1; 1213DE Flags: Precursor; 1214GN Name=acta1; 1215OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica). 1216OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 1217OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 1218OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei; 1219OC Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini; 1220OC Oreochromis. 1221OX NCBI_TaxID=8127; 1222RN [1] 1223RP NUCLEOTIDE SEQUENCE [MRNA]. 1224RC TISSUE=Skeletal muscle; 1225RA Takeuchi K.; 1226RT "Cloning of Tilapia actin cDNAs."; 1227RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. 1228CC -!- FUNCTION: Actins are highly conserved proteins that are involved 1229CC in various types of cell motility and are ubiquitously expressed 1230CC in all eukaryotic cells. 1231CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 1232CC structural filament (F-actin) in the form of a two-stranded helix. 1233CC Each actin can bind to 4 others. 1234CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 1235CC -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to 1236CC form methionine sulfoxide promotes actin filament 1237CC depolymerization. Methionine sulfoxide is produced 1238CC stereospecifically, but it is not known whether the (S)-S-oxide or 1239CC the (R)-S-oxide is produced (By similarity). 1240CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, 1241CC alpha, beta and gamma have been identified. The alpha actins are 1242CC found in muscle tissues and are a major constituent of the 1243CC contractile apparatus. The beta and gamma actins coexist in most 1244CC cell types as components of the cytoskeleton and as mediators of 1245CC internal cell motility. 1246CC -!- SIMILARITY: Belongs to the actin family. 1247CC ----------------------------------------------------------------------- 1248CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1249CC Distributed under the Creative Commons Attribution-NoDerivs License 1250CC ----------------------------------------------------------------------- 1251DR EMBL; AB037866; BAA90689.1; -; mRNA. 1252DR ProteinModelPortal; P68264; -. 1253DR SMR; P68264; 6-377. 1254DR HOVERGEN; HBG003771; -. 1255DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 1256DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 1257DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 1258DR InterPro; IPR004000; Actin-like. 1259DR InterPro; IPR020902; Actin/actin-like_CS. 1260DR InterPro; IPR004001; Actin_CS. 1261DR PANTHER; PTHR11937; Actin_like; 1. 1262DR Pfam; PF00022; Actin; 1. 1263DR PRINTS; PR00190; ACTIN. 1264DR SMART; SM00268; ACTIN; 1. 1265DR PROSITE; PS00406; ACTINS_1; 1. 1266DR PROSITE; PS00432; ACTINS_2; 1. 1267DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 1268PE 2: Evidence at transcript level; 1269KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation; 1270KW Muscle protein; Nucleotide-binding; Oxidation. 1271FT PROPEP 1 2 Removed in mature form (By similarity). 1272FT /FTId=PRO_0000000866. 1273FT CHAIN 3 377 Actin, alpha skeletal muscle. 1274FT /FTId=PRO_0000000867. 1275FT MOD_RES 3 3 N-acetylaspartate (By similarity). 1276FT MOD_RES 46 46 Methionine sulfoxide (By similarity). 1277FT MOD_RES 75 75 Tele-methylhistidine (By similarity). 1278SQ SEQUENCE 377 AA; 41945 MW; 1C7185C0F7C19A26 CRC64; 1279 MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 1280 QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK 1281 MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL 1282 DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 1283 SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV 1284 LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS 1285 KQEYDEAGPS IVHRKCF 1286// 1287ID ACTX_TAKRU Reviewed; 376 AA. 1288AC P53483; 1289DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 1290DT 01-OCT-1996, sequence version 1. 1291DT 16-MAY-2012, entry version 65. 1292DE RecName: Full=Actin, alpha anomalous; 1293OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 1294OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 1295OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 1296OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 1297OC Tetradontoidea; Tetraodontidae; Takifugu. 1298OX NCBI_TaxID=31033; 1299RN [1] 1300RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. 1301RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; 1302RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; 1303RT "Isolation, characterization and evolution of nine pufferfish (Fugu 1304RT rubripes) actin genes."; 1305RL J. Mol. Biol. 259:655-665(1996). 1306CC -!- FUNCTION: Actins are highly conserved proteins that are involved 1307CC in various types of cell motility and are ubiquitously expressed 1308CC in all eukaryotic cells. 1309CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a 1310CC structural filament (F-actin) in the form of a two-stranded helix. 1311CC Each actin can bind to 4 others. 1312CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. 1313CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. 1314CC -!- PTM: Oxidation of Met-45 by MICALs (MICAL1, MICAL2 or MICAL3) to 1315CC form methionine sulfoxide promotes actin filament 1316CC depolymerization. Methionine sulfoxide is produced 1317CC stereospecifically, but it is not known whether the (S)-S-oxide or 1318CC the (R)-S-oxide is produced (By similarity). 1319CC -!- SIMILARITY: Belongs to the actin family. 1320CC ----------------------------------------------------------------------- 1321CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1322CC Distributed under the Creative Commons Attribution-NoDerivs License 1323CC ----------------------------------------------------------------------- 1324DR EMBL; U38962; AAC59897.1; -; Genomic_DNA. 1325DR PIR; S71123; S71123. 1326DR ProteinModelPortal; P53483; -. 1327DR SMR; P53483; 7-365. 1328DR Ensembl; ENSTRUT00000013262; ENSTRUP00000013201; ENSTRUG00000005494. 1329DR eggNOG; COG5277; -. 1330DR GeneTree; ENSGT00630000089629; -. 1331DR InParanoid; P53483; -. 1332DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. 1333DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. 1334DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 1335DR InterPro; IPR004000; Actin-like. 1336DR InterPro; IPR020902; Actin/actin-like_CS. 1337DR InterPro; IPR004001; Actin_CS. 1338DR PANTHER; PTHR11937; Actin_like; 1. 1339DR Pfam; PF00022; Actin; 1. 1340DR PRINTS; PR00190; ACTIN. 1341DR SMART; SM00268; ACTIN; 1. 1342DR PROSITE; PS00406; ACTINS_1; 1. 1343DR PROSITE; PS00432; ACTINS_2; 1. 1344DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. 1345PE 2: Evidence at transcript level; 1346KW ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; 1347KW Nucleotide-binding; Oxidation; Reference proteome. 1348FT CHAIN 1 376 Actin, alpha anomalous. 1349FT /FTId=PRO_0000089056. 1350FT MOD_RES 45 45 Methionine sulfoxide (By similarity). 1351SQ SEQUENCE 376 AA; 41979 MW; DB037F47BA1371D8 CRC64; 1352 MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ 1353 SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM 1354 TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN 1355 LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR 1356 YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL 1357 TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK 1358 QEYEEIGPSI IHCKCF 1359// 1360ID AMIC_PSEAE Reviewed; 385 AA. 1361AC P27017; 1362DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. 1363DT 23-JAN-2007, sequence version 5. 1364DT 16-MAY-2012, entry version 83. 1365DE RecName: Full=Aliphatic amidase expression-regulating protein; 1366GN Name=amiC; OrderedLocusNames=PA3364; 1367OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 1368OS 12228). 1369OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; 1370OC Pseudomonadaceae; Pseudomonas. 1371OX NCBI_TaxID=208964; 1372RN [1] 1373RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19. 1374RC STRAIN=PAC; 1375RX MEDLINE=91317707; PubMed=1907262; 1376RA Wilson S.A., Drew R.E.; 1377RT "Cloning and DNA sequence of amiC, a new gene regulating expression of 1378RT the Pseudomonas aeruginosa aliphatic amidase, and purification of the 1379RT amiC product."; 1380RL J. Bacteriol. 173:4914-4921(1991). 1381RN [2] 1382RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 1383RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; 1384RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; 1385RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., 1386RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., 1387RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., 1388RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., 1389RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., 1390RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; 1391RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an 1392RT opportunistic pathogen."; 1393RL Nature 406:959-964(2000). 1394RN [3] 1395RP CRYSTALLIZATION. 1396RX MEDLINE=92106343; PubMed=1762155; DOI=10.1016/0022-2836(91)90579-U; 1397RA Wilson S.A., Chayen N.E., Hemmings A.M., Drew R.E., Pearl L.H.; 1398RT "Crystallization of and preliminary X-ray data for the negative 1399RT regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa."; 1400RL J. Mol. Biol. 222:869-871(1991). 1401RN [4] 1402RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 27-28. 1403RX MEDLINE=95112789; PubMed=7813419; 1404RA Pearl L.H., O'Hara B.P., Drew R.E., Wilson S.A.; 1405RT "Crystal structure of AmiC: the controller of transcription 1406RT antitermination in the amidase operon of Pseudomonas aeruginosa."; 1407RL EMBO J. 13:5810-5817(1994). 1408RN [5] 1409RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIR. 1410RC STRAIN=PAC1; 1411RX MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175; 1412RA O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E., 1413RA Pearl L.H.; 1414RT "Crystal structure and induction mechanism of AmiC-AmiR: a ligand- 1415RT regulated transcription antitermination complex."; 1416RL EMBO J. 18:5175-5186(1999). 1417RN [6] 1418RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). 1419RC STRAIN=PAC1; 1420RX MEDLINE=20175740; PubMed=10708652; DOI=10.1093/protein/13.2.129; 1421RA O'Hara B.P., Wilson S.A., Lee A.W., Roe S.M., Siligardi G., Drew R.E., 1422RA Pearl L.H.; 1423RT "Structural adaptation to selective pressure for altered ligand 1424RT specificity in the Pseudomonas aeruginosa amide receptor, AmiC."; 1425RL Protein Eng. 13:129-132(2000). 1426CC -!- FUNCTION: Negatively regulates the expression of the aliphatic 1427CC amidase operon. AmiC functions by inhibiting the action of AmiR at 1428CC the protein level. It exhibits protein kinase activity. 1429CC -!- SUBUNIT: Homodimer. Forms a complex with AmiR. 1430CC -!- DOMAIN: Consists of two beta-alpha-beta domains with a central 1431CC cleft in which the amide binds. 1432CC ----------------------------------------------------------------------- 1433CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1434CC Distributed under the Creative Commons Attribution-NoDerivs License 1435CC ----------------------------------------------------------------------- 1436DR EMBL; X13776; CAA32024.1; -; Genomic_DNA. 1437DR EMBL; AE004091; AAG06752.1; -; Genomic_DNA. 1438DR PIR; A40359; A40359. 1439DR PIR; C83226; C83226. 1440DR RefSeq; NP_252054.1; NC_002516.2. 1441DR PDB; 1PEA; X-ray; 2.10 A; A=1-385. 1442DR PDB; 1QNL; X-ray; 2.70 A; A=1-385. 1443DR PDB; 1QO0; X-ray; 2.25 A; A/B=1-385. 1444DR PDBsum; 1PEA; -. 1445DR PDBsum; 1QNL; -. 1446DR PDBsum; 1QO0; -. 1447DR ProteinModelPortal; P27017; -. 1448DR SMR; P27017; 7-380. 1449DR IntAct; P27017; 1. 1450DR GeneID; 877798; -. 1451DR GenomeReviews; AE004091_GR; PA3364. 1452DR KEGG; pae:PA3364; -. 1453DR PATRIC; 19841329; VBIPseAer58763_3523. 1454DR PseudoCAP; PA3364; -. 1455DR eggNOG; COG0683; -. 1456DR HOGENOM; HOG000202643; -. 1457DR KO; K01999; -. 1458DR OMA; TLYEGFE; -. 1459DR ProtClustDB; CLSK867930; -. 1460DR BioCyc; PAER208964:PA3364-MONOMER; -. 1461DR EvolutionaryTrace; P27017; -. 1462DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro. 1463DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. 1464DR GO; GO:0006865; P:amino acid transport; IEA:InterPro. 1465DR InterPro; IPR000709; Leu_Ile_Val-bd. 1466DR PRINTS; PR00337; LEUILEVALBP. 1467PE 1: Evidence at protein level; 1468KW 3D-structure; Complete proteome; Direct protein sequencing; Kinase; 1469KW Reference proteome; Repressor; Transferase. 1470FT INIT_MET 1 1 Removed. 1471FT CHAIN 2 385 Aliphatic amidase expression-regulating 1472FT protein. 1473FT /FTId=PRO_0000064581. 1474FT VARIANT 106 106 T -> N (in strain: PAC181; butyramide 1475FT inducible phenotype). 1476FT CONFLICT 27 28 QR -> HA (in Ref. 1; CAA32024). 1477FT CONFLICT 186 186 V -> L (in Ref. 1; CAA32024). 1478FT CONFLICT 263 263 A -> P (in Ref. 1; CAA32024). 1479FT CONFLICT 305 305 S -> N (in Ref. 1; CAA32024). 1480FT CONFLICT 319 319 C -> D (in Ref. 1; CAA32024). 1481FT CONFLICT 383 383 A -> P (in Ref. 1; CAA32024). 1482FT STRAND 9 13 1483FT STRAND 16 18 1484FT HELIX 21 39 1485FT TURN 40 43 1486FT STRAND 50 54 1487FT HELIX 60 72 1488FT STRAND 78 81 1489FT HELIX 85 97 1490FT STRAND 101 104 1491FT STRAND 117 119 1492FT HELIX 124 126 1493FT HELIX 128 136 1494FT TURN 137 139 1495FT STRAND 141 150 1496FT HELIX 151 166 1497FT STRAND 170 177 1498FT HELIX 183 196 1499FT STRAND 199 204 1500FT HELIX 209 221 1501FT STRAND 229 233 1502FT HELIX 236 239 1503FT HELIX 244 247 1504FT STRAND 251 255 1505FT HELIX 263 273 1506FT HELIX 284 303 1507FT HELIX 308 315 1508FT STRAND 320 322 1509FT STRAND 325 329 1510FT TURN 331 333 1511FT STRAND 336 338 1512FT STRAND 341 345 1513FT STRAND 351 356 1514FT HELIX 369 371 1515FT HELIX 376 378 1516SQ SEQUENCE 385 AA; 42807 MW; 33924B6C36017B79 CRC64; 1517 MGSHQERPLI GLLFSETGVT ADIERSQRYG ALLAVEQLNR EGGVGGRPIE TLSQDPGGDP 1518 DRYRLCAEDF IRNRGVRFLV GCYMSHTRKA VMPVVERADA LLCYPTPYEG FEYSPNIVYG 1519 GPAPNQNSAP LAAYLIRHYG ERVVFIGSDY IYPRESNHVM RHLYRQHGGT VLEEIYIPLY 1520 PSDDDVQRAV ERIYQARADV VFSTVVGTGT AELYRAIARR YGDGRRPPIA SLTTSEAEVA 1521 KMESDVAEGQ VVVAPYFSSI DTAASRAFVQ ACHGFFPENA TITAWAEAAY WQTLLLGRAA 1522 QAAGSWRVED VQRHLYDICI DAPQGPVRVE RQNNHSRLSS RIAEIDARGV FQVRWQSPEP 1523 IRPDPYVVVH NLDDWSASMG GGALP 1524// 1525ID AMIR_PSEAE Reviewed; 196 AA. 1526AC P10932; 1527DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. 1528DT 08-DEC-2000, sequence version 2. 1529DT 16-MAY-2012, entry version 93. 1530DE RecName: Full=Aliphatic amidase regulator; 1531GN Name=amiR; OrderedLocusNames=PA3363; 1532OS Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 1533OS 12228). 1534OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; 1535OC Pseudomonadaceae; Pseudomonas. 1536OX NCBI_TaxID=208964; 1537RN [1] 1538RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 1539RC STRAIN=PAC433; 1540RX MEDLINE=89211409; PubMed=2495988; DOI=10.1016/0014-5793(89)80249-2; 1541RA Lowe N., Rice P.M., Drew R.E.; 1542RT "Nucleotide sequence of the aliphatic amidase regulator gene (amiR) of 1543RT Pseudomonas aeruginosa."; 1544RL FEBS Lett. 246:39-43(1989). 1545RN [2] 1546RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 1547RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; 1548RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; 1549RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., 1550RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., 1551RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., 1552RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., 1553RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., 1554RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; 1555RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an 1556RT opportunistic pathogen."; 1557RL Nature 406:959-964(2000). 1558RN [3] 1559RP CHARACTERIZATION. 1560RX MEDLINE=95286483; PubMed=7539417; 1561RA Wilson S.A., Drew R.E.; 1562RT "Transcriptional analysis of the amidase operon from Pseudomonas 1563RT aeruginosa."; 1564RL J. Bacteriol. 177:3052-3057(1995). 1565RN [4] 1566RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIC. 1567RC STRAIN=PAC1; 1568RX MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175; 1569RA O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E., 1570RA Pearl L.H.; 1571RT "Crystal structure and induction mechanism of AmiC-AmiR: a ligand- 1572RT regulated transcription antitermination complex."; 1573RL EMBO J. 18:5175-5186(1999). 1574CC -!- FUNCTION: Positive controlling element of AmiE, the gene for 1575CC aliphatic amidase. Acts as a transcriptional antitermination 1576CC factor. It is thought to allow RNA polymerase read through a rho- 1577CC independent transcription terminator between the AmiE promoter and 1578CC gene. 1579CC -!- SUBUNIT: Forms a complex with AmiC. 1580CC -!- SIMILARITY: Contains 1 ANTAR domain. 1581CC ----------------------------------------------------------------------- 1582CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1583CC Distributed under the Creative Commons Attribution-NoDerivs License 1584CC ----------------------------------------------------------------------- 1585DR EMBL; X13776; CAA32023.1; -; Genomic_DNA. 1586DR EMBL; AE004091; AAG06751.1; -; Genomic_DNA. 1587DR PIR; B83226; B83226. 1588DR PIR; S03884; S03884. 1589DR RefSeq; NP_252053.1; NC_002516.2. 1590DR PDB; 1QO0; X-ray; 2.25 A; D/E=1-196. 1591DR PDBsum; 1QO0; -. 1592DR ProteinModelPortal; P10932; -. 1593DR SMR; P10932; 2-195. 1594DR IntAct; P10932; 1. 1595DR DNASU; 880573; -. 1596DR GeneID; 880573; -. 1597DR GenomeReviews; AE004091_GR; PA3363. 1598DR KEGG; pae:PA3363; -. 1599DR PATRIC; 19841327; VBIPseAer58763_3522. 1600DR PseudoCAP; PA3363; -. 1601DR eggNOG; COG3707; -. 1602DR HOGENOM; HOG000247749; -. 1603DR OMA; QRIGCQV; -. 1604DR ProtClustDB; CLSK867929; -. 1605DR BioCyc; PAER208964:PA3363-MONOMER; -. 1606DR EvolutionaryTrace; P10932; -. 1607DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 1608DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW. 1609DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 1610DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. 1611DR InterPro; IPR005561; ANTAR. 1612DR InterPro; IPR011006; CheY-like_superfamily. 1613DR InterPro; IPR008327; Sig_transdc_resp-reg_antiterm. 1614DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 1615DR Pfam; PF03861; ANTAR; 1. 1616DR PIRSF; PIRSF036382; RR_antiterm; 1. 1617DR SMART; SM01012; ANTAR; 1. 1618DR SUPFAM; SSF52172; CheY_like; 1. 1619DR PROSITE; PS50921; ANTAR; 1. 1620PE 1: Evidence at protein level; 1621KW 3D-structure; Complete proteome; Reference proteome; Transcription; 1622KW Transcription antitermination; Transcription regulation. 1623FT CHAIN 1 196 Aliphatic amidase regulator. 1624FT /FTId=PRO_0000064582. 1625FT DOMAIN 129 190 ANTAR. 1626FT CONFLICT 48 48 S -> A (in Ref. 1; CAA32023). 1627FT CONFLICT 64 64 R -> G (in Ref. 1; CAA32023). 1628FT CONFLICT 141 141 E -> D (in Ref. 1; CAA32023). 1629FT CONFLICT 154 154 A -> V (in Ref. 1; CAA32023). 1630FT CONFLICT 170 170 Y -> H (in Ref. 1; CAA32023). 1631FT HELIX 3 8 1632FT HELIX 9 12 1633FT STRAND 14 19 1634FT HELIX 23 35 1635FT STRAND 38 42 1636FT STRAND 54 59 1637FT HELIX 65 75 1638FT STRAND 81 86 1639FT HELIX 91 100 1640FT STRAND 103 109 1641FT HELIX 112 114 1642FT HELIX 115 160 1643FT HELIX 164 175 1644FT TURN 176 179 1645FT HELIX 182 189 1646SQ SEQUENCE 196 AA; 21903 MW; 306A4F30E8E4C6C0 CRC64; 1647 MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPESFD VPVDVVFTSI 1648 FQNRHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV 1649 SARRISEEMA KLKQKTEQLQ ERIAGQARIN QAKALLMQRH GWDEREAHQY LSREAMKRRE 1650 PILKIAQELL GNEPSA 1651// 1652ID AQP1_HUMAN Reviewed; 269 AA. 1653AC P29972; B5BU39; Q8TBI5; Q8TDC1; 1654DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. 1655DT 23-JAN-2007, sequence version 3. 1656DT 16-MAY-2012, entry version 142. 1657DE RecName: Full=Aquaporin-1; 1658DE Short=AQP-1; 1659DE AltName: Full=Aquaporin-CHIP; 1660DE AltName: Full=Urine water channel; 1661DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule; 1662GN Name=AQP1; Synonyms=CHIP28; 1663OS Homo sapiens (Human). 1664OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 1665OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 1666OC Catarrhini; Hominidae; Homo. 1667OX NCBI_TaxID=9606; 1668RN [1] 1669RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. 1670RX MEDLINE=92107900; PubMed=1722319; DOI=10.1073/pnas.88.24.11110; 1671RA Preston G.M., Agre P.; 1672RT "Isolation of the cDNA for erythrocyte integral membrane protein of 28 1673RT kilodaltons: member of an ancient channel family."; 1674RL Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991). 1675RN [2] 1676RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 1677RX MEDLINE=93340184; PubMed=8340403; 1678RA Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.; 1679RT "The human aquaporin-CHIP gene. Structure, organization, and 1680RT chromosomal localization."; 1681RL J. Biol. Chem. 268:15772-15778(1993). 1682RN [3] 1683RP NUCLEOTIDE SEQUENCE [MRNA]. 1684RC TISSUE=Retinal pigment epithelium; 1685RX MEDLINE=96326579; PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4; 1686RA Ruiz A.C., Bok D.; 1687RT "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in 1688RT human retinal pigment epithelium."; 1689RL Biochim. Biophys. Acta 1282:174-178(1996). 1690RN [4] 1691RP NUCLEOTIDE SEQUENCE [MRNA]. 1692RC TISSUE=Uterus; 1693RX MEDLINE=94290349; PubMed=7517253; 1694RA Li X., Yu H., Koide S.S.; 1695RT "The water channel gene in human uterus."; 1696RL Biochem. Mol. Biol. Int. 32:371-377(1994). 1697RN [5] 1698RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165. 1699RG SeattleSNPs variation discovery resource; 1700RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. 1701RN [6] 1702RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 1703RX PubMed=19054851; DOI=10.1038/nmeth.1273; 1704RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., 1705RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., 1706RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., 1707RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., 1708RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., 1709RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., 1710RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., 1711RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., 1712RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., 1713RA Isogai T., Imai J., Watanabe S., Nomura N.; 1714RT "Human protein factory for converting the transcriptome into an in 1715RT vitro-expressed proteome."; 1716RL Nat. Methods 5:1011-1017(2008). 1717RN [7] 1718RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 1719RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; 1720RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., 1721RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., 1722RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., 1723RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., 1724RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., 1725RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., 1726RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., 1727RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., 1728RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., 1729RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., 1730RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., 1731RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., 1732RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., 1733RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., 1734RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., 1735RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., 1736RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., 1737RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., 1738RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., 1739RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., 1740RA Waterston R.H., Wilson R.K.; 1741RT "The DNA sequence of human chromosome 7."; 1742RL Nature 424:157-164(2003). 1743RN [8] 1744RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 1745RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 1746RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 1747RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 1748RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 1749RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 1750RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 1751RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 1752RA Venter J.C.; 1753RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 1754RN [9] 1755RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 1756RC TISSUE=Brain; 1757RX PubMed=15489334; DOI=10.1101/gr.2596504; 1758RG The MGC Project Team; 1759RT "The status, quality, and expansion of the NIH full-length cDNA 1760RT project: the Mammalian Gene Collection (MGC)."; 1761RL Genome Res. 14:2121-2127(2004). 1762RN [10] 1763RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269. 1764RC TISSUE=Articular cartilage; 1765RA Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.; 1766RT "Human chondrocytes in situ express aquaporin water channels: changes 1767RT in AQP1 abundance in pathologies of articular cartilage."; 1768RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. 1769RN [11] 1770RP PROTEIN SEQUENCE OF 2-36. 1771RX PubMed=2007592; 1772RA Smith B.L., Agre P.; 1773RT "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit 1774RT oligomer similar to channel proteins."; 1775RL J. Biol. Chem. 266:6407-6415(1991). 1776RN [12] 1777RP FUNCTION. 1778RX MEDLINE=92229472; PubMed=1373524; DOI=10.1126/science.256.5055.385; 1779RA Preston G.M., Carroll T.P., Guggino W.B., Agre P.; 1780RT "Appearance of water channels in Xenopus oocytes expressing red cell 1781RT CHIP28 protein."; 1782RL Science 256:385-387(1992). 1783RN [13] 1784RP TARGET OF MERCURY INHIBITION. 1785RX MEDLINE=93106996; PubMed=7677994; 1786RA Preston G.M., Jung J.S., Guggino W.B., Agre P.; 1787RT "The mercury-sensitive residue at cysteine 189 in the CHIP28 water 1788RT channel."; 1789RL J. Biol. Chem. 268:17-20(1993). 1790RN [14] 1791RP TOPOLOGY. 1792RX MEDLINE=94124503; PubMed=7507481; 1793RA Preston G.M., Jung J.S., Guggino W.B., Agre P.; 1794RT "Membrane topology of aquaporin CHIP. Analysis of functional epitope- 1795RT scanning mutants by vectorial proteolysis."; 1796RL J. Biol. Chem. 269:1668-1673(1994). 1797RN [15] 1798RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS 1799RP SPECTROMETRY. 1800RC TISSUE=Cervix carcinoma; 1801RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; 1802RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., 1803RA Greff Z., Keri G., Stemmann O., Mann M.; 1804RT "Kinase-selective enrichment enables quantitative phosphoproteomics of 1805RT the kinome across the cell cycle."; 1806RL Mol. Cell 31:438-448(2008). 1807RN [16] 1808RP STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS). 1809RX MEDLINE=94313979; PubMed=7518771; 1810RA Walz T., Smith B.L., Agre P., Engel A.; 1811RT "The three-dimensional structure of human erythrocyte aquaporin 1812RT CHIP."; 1813RL EMBO J. 13:2985-2993(1994). 1814RN [17] 1815RP STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS). 1816RX MEDLINE=97320502; PubMed=9177353; DOI=10.1038/42512; 1817RA Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y., 1818RA Smith B.L., Agre P., Engel A.; 1819RT "The three-dimensional structure of aquaporin-1."; 1820RL Nature 387:624-627(1997). 1821RN [18] 1822RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS). 1823RX MEDLINE=20487015; PubMed=11034202; DOI=10.1038/35036519; 1824RA Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., 1825RA Engel A., Fujiyoshi Y.; 1826RT "Structural determinants of water permeation through aquaporin-1."; 1827RL Nature 407:599-605(2000). 1828RN [19] 1829RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS). 1830RX MEDLINE=21423577; PubMed=11532455; DOI=10.1016/S0014-5793(01)02743-0; 1831RA de Groot B.L., Engel A., Grubmueller H.; 1832RT "A refined structure of human aquaporin-1."; 1833RL FEBS Lett. 504:206-211(2001). 1834RN [20] 1835RP STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS). 1836RX PubMed=11171962; DOI=10.1073/pnas.041489198; 1837RA Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.; 1838RT "Visualization of a water-selective pore by electron crystallography 1839RT in vitreous ice."; 1840RL Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001). 1841RN [21] 1842RP VARIANT BLOOD GROUP COLTON VAL-45. 1843RX MEDLINE=94365170; PubMed=7521882; DOI=10.1172/JCI117418; 1844RA Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.; 1845RT "Human red cell aquaporin CHIP. I. Molecular characterization of ABH 1846RT and Colton blood group antigens."; 1847RL J. Clin. Invest. 94:1043-1049(1994). 1848RN [22] 1849RP VARIANT LEU-38. 1850RX MEDLINE=94360246; PubMed=7521540; DOI=10.1126/science.7521540; 1851RA Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.; 1852RT "Mutations in aquaporin-1 in phenotypically normal humans without 1853RT functional CHIP water channels."; 1854RL Science 265:1585-1587(1994). 1855CC -!- FUNCTION: Forms a water-specific channel that provides the plasma 1856CC membranes of red cells and kidney proximal tubules with high 1857CC permeability to water, thereby permitting water to move in the 1858CC direction of an osmotic gradient. 1859CC -!- SUBUNIT: Homotetramer. Interacts with EPHB2; involved in endolymph 1860CC production in the inner ear (By similarity). 1861CC -!- INTERACTION: 1862CC Q99750:MDFI; NbExp=4; IntAct=EBI-745213, EBI-724076; 1863CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 1864CC -!- TISSUE SPECIFICITY: Expressed in a number of tissues including 1865CC erythrocytes, renal tubules, retinal pigment epithelium, heart, 1866CC lung, skeletal muscle, kidney and pancreas. Weakly expressed in 1867CC brain, placenta and liver. 1868CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing 1869CC three membrane-spanning domains and a pore-forming loop with the 1870CC signature motif Asn-Pro-Ala (NPA). 1871CC -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group 1872CC system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46), 1873CC approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val- 1874CC 46). Co(A-B-) which is very rare, is due to a complete absence of 1875CC AQP1. 1876CC -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar 1877CC concentrations of mercury. 1878CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. 1879CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene 1880CC mutation database; 1881CC URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=colton"; 1882CC -!- WEB RESOURCE: Name=SeattleSNPs; 1883CC URL="http://pga.gs.washington.edu/data/aqp1/"; 1884CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue 1885CC 36 of July 2003; 1886CC URL="http://web.expasy.org/spotlight/back_issues/sptlt036.shtml"; 1887CC ----------------------------------------------------------------------- 1888CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 1889CC Distributed under the Creative Commons Attribution-NoDerivs License 1890CC ----------------------------------------------------------------------- 1891DR EMBL; M77829; AAA58425.1; -; mRNA. 1892DR EMBL; U41517; AAC50648.1; -; mRNA. 1893DR EMBL; U41518; AAC50649.1; -; mRNA. 1894DR EMBL; S73482; AAB31193.1; -; mRNA. 1895DR EMBL; AC004691; AAC16481.1; -; Genomic_DNA. 1896DR EMBL; AC005155; AAC23788.1; -; Genomic_DNA. 1897DR EMBL; AY953319; AAX24129.1; -; Genomic_DNA. 1898DR EMBL; AB451275; BAG70089.1; -; mRNA. 1899DR EMBL; AB451402; BAG70216.1; -; mRNA. 1900DR EMBL; CH471073; EAW93971.1; -; Genomic_DNA. 1901DR EMBL; BC022486; AAH22486.1; -; mRNA. 1902DR EMBL; AF480415; AAL87136.1; -; Genomic_DNA. 1903DR IPI; IPI00024689; -. 1904DR PIR; A41616; A41616. 1905DR PIR; I52366; I52366. 1906DR RefSeq; NP_932766.1; NM_198098.2. 1907DR UniGene; Hs.76152; -. 1908DR PDB; 1FQY; X-ray; 3.80 A; A=1-269. 1909DR PDB; 1H6I; X-ray; 3.54 A; A=1-269. 1910DR PDB; 1IH5; X-ray; 3.70 A; A=1-269. 1911DR PDBsum; 1FQY; -. 1912DR PDBsum; 1H6I; -. 1913DR PDBsum; 1IH5; -. 1914DR ProteinModelPortal; P29972; -. 1915DR SMR; P29972; 9-233. 1916DR DIP; DIP-29607N; -. 1917DR IntAct; P29972; 7. 1918DR MINT; MINT-1439356; -. 1919DR STRING; P29972; -. 1920DR TCDB; 1.A.8.8.1; major intrinsic protein (MIP) family. 1921DR PhosphoSite; P29972; -. 1922DR DMDM; 267412; -. 1923DR PRIDE; P29972; -. 1924DR DNASU; 358; -. 1925DR Ensembl; ENST00000311813; ENSP00000311165; ENSG00000240583. 1926DR GeneID; 358; -. 1927DR KEGG; hsa:358; -. 1928DR UCSC; uc003tbv.2; human. 1929DR CTD; 358; -. 1930DR GeneCards; GC07P030917; -. 1931DR HGNC; HGNC:633; AQP1. 1932DR HPA; CAB001707; -. 1933DR HPA; HPA019206; -. 1934DR MIM; 107776; gene. 1935DR MIM; 110450; phenotype. 1936DR neXtProt; NX_P29972; -. 1937DR PharmGKB; PA24918; -. 1938DR eggNOG; COG0580; -. 1939DR GeneTree; ENSGT00550000074347; -. 1940DR HOGENOM; HOG000288286; -. 1941DR HOVERGEN; HBG000312; -. 1942DR InParanoid; P29972; -. 1943DR KO; K09864; -. 1944DR OMA; ITHNFKD; -. 1945DR OrthoDB; EOG46T328; -. 1946DR PhylomeDB; P29972; -. 1947DR Reactome; REACT_15518; Transmembrane transport of small molecules. 1948DR DrugBank; DB00819; Acetazolamide. 1949DR EvolutionaryTrace; P29972; -. 1950DR NextBio; 1497; -. 1951DR ArrayExpress; P29972; -. 1952DR Bgee; P29972; -. 1953DR CleanEx; HS_AQP1; -. 1954DR Genevestigator; P29972; -. 1955DR GermOnline; ENSG00000106125; Homo sapiens. 1956DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. 1957DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB. 1958DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB. 1959DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 1960DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. 1961DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB. 1962DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB. 1963DR GO; GO:0020003; C:symbiont-containing vacuole; ISS:UniProtKB. 1964DR GO; GO:0051739; F:ammonia transmembrane transporter activity; IDA:UniProtKB. 1965DR GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; IDA:UniProtKB. 1966DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB. 1967DR GO; GO:0005223; F:intracellular cGMP activated cation channel activity; IDA:UniProtKB. 1968DR GO; GO:0030184; F:nitric oxide transmembrane transporter activity; IDA:UniProtKB. 1969DR GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB. 1970DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. 1971DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB. 1972DR GO; GO:0015696; P:ammonium transport; IDA:UniProtKB. 1973DR GO; GO:0006884; P:cell volume homeostasis; IMP:UniProtKB. 1974DR GO; GO:0071474; P:cellular hyperosmotic response; IMP:UniProtKB. 1975DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB. 1976DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB. 1977DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB. 1978DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB. 1979DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB. 1980DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB. 1981DR GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB. 1982DR GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB. 1983DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB. 1984DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB. 1985DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB. 1986DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEP:UniProtKB. 1987DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB. 1988DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB. 1989DR GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB. 1990DR GO; GO:0085018; P:maintenance of symbiont-containing vacuole via substance secreted by host; IMP:UniProtKB. 1991DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. 1992DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. 1993DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB. 1994DR GO; GO:0030157; P:pancreatic juice secretion; IEP:UniProtKB. 1995DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB. 1996DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB. 1997DR GO; GO:0046878; P:positive regulation of saliva secretion; IMP:UniProtKB. 1998DR GO; GO:0003097; P:renal water transport; IDA:UniProtKB. 1999DR GO; GO:0042493; P:response to drug; IDA:UniProtKB. 2000DR GO; GO:0035377; P:transepithelial water transport; IDA:UniProtKB. 2001DR Gene3D; G3DSA:1.20.1080.10; MIP; 1. 2002DR InterPro; IPR012269; Aquaporin. 2003DR InterPro; IPR023271; Aquaporin-like. 2004DR InterPro; IPR023274; Aquaporin_1. 2005DR InterPro; IPR000425; MIP. 2006DR InterPro; IPR022357; MIP_CS. 2007DR PANTHER; PTHR19139; MIP; 1. 2008DR Pfam; PF00230; MIP; 1. 2009DR PRINTS; PR02013; AQUAPORIN1. 2010DR PRINTS; PR00783; MINTRINSICP. 2011DR SUPFAM; SSF81338; MIP; 1. 2012DR TIGRFAMs; TIGR00861; MIP; 1. 2013DR PROSITE; PS00221; MIP; 1. 2014PE 1: Evidence at protein level; 2015KW 3D-structure; Blood group antigen; Complete proteome; 2016KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; 2017KW Polymorphism; Reference proteome; Repeat; Transmembrane; 2018KW Transmembrane helix; Transport. 2019FT INIT_MET 1 1 Removed. 2020FT CHAIN 2 269 Aquaporin-1. 2021FT /FTId=PRO_0000063920. 2022FT TOPO_DOM 2 7 Cytoplasmic. 2023FT TRANSMEM 8 36 Helical; Name=Helix 1. 2024FT TOPO_DOM 37 48 Extracellular. 2025FT TRANSMEM 49 66 Helical; Name=Helix 2. 2026FT TOPO_DOM 67 70 Cytoplasmic. 2027FT INTRAMEM 71 76 2028FT INTRAMEM 77 84 Helical; Name=Helix B. 2029FT TOPO_DOM 85 94 Cytoplasmic. 2030FT TRANSMEM 95 115 Helical; Name=Helix 3. 2031FT TOPO_DOM 116 136 Extracellular. 2032FT TRANSMEM 137 155 Helical; Name=Helix 4. 2033FT TOPO_DOM 156 166 Cytoplasmic. 2034FT TRANSMEM 167 183 Helical; Name=Helix 5. 2035FT TOPO_DOM 184 186 Extracellular. 2036FT INTRAMEM 187 192 2037FT INTRAMEM 193 200 Helical; Name=Helix E. 2038FT TOPO_DOM 201 207 Extracellular. 2039FT TRANSMEM 208 228 Helical; Name=Helix 6. 2040FT TOPO_DOM 229 269 Cytoplasmic. 2041FT MOTIF 76 78 NPA 1. 2042FT MOTIF 192 194 NPA 2. 2043FT COMPBIAS 159 162 Poly-Arg. 2044FT SITE 56 56 Substrate discrimination. 2045FT SITE 180 180 Substrate discrimination. 2046FT SITE 189 189 Hg(2+)-sensitive residue. 2047FT SITE 195 195 Substrate discrimination. 2048FT MOD_RES 246 246 Phosphothreonine (By similarity). 2049FT MOD_RES 247 247 Phosphoserine (By similarity). 2050FT MOD_RES 262 262 Phosphoserine. 2051FT CARBOHYD 42 42 N-linked (GlcNAc...). 2052FT CARBOHYD 205 205 N-linked (GlcNAc...) (Potential). 2053FT VARIANT 38 38 P -> L (in Co(A-B-) antigen; non 2054FT functional AQP1; red cells show low 2055FT osmotic water permeability). 2056FT /FTId=VAR_013279. 2057FT VARIANT 45 45 A -> V (in Co(A-B+) antigen; 2058FT dbSNP:rs28362692). 2059FT /FTId=VAR_004400. 2060FT VARIANT 165 165 G -> D (in dbSNP:rs28362731). 2061FT /FTId=VAR_022318. 2062FT CONFLICT 45 45 A -> T (in Ref. 9; AAH22486). 2063FT HELIX 8 35 2064FT STRAND 37 42 2065FT HELIX 48 65 2066FT STRAND 68 71 2067FT HELIX 76 83 2068FT HELIX 94 114 2069FT TURN 119 122 2070FT STRAND 132 135 2071FT HELIX 136 154 2072FT HELIX 166 182 2073FT TURN 183 185 2074FT HELIX 192 199 2075FT HELIX 207 227 2076SQ SEQUENCE 269 AA; 28526 MW; BA204D82FB26352E CRC64; 2077 MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI 2078 ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT 2079 GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 2080 LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD 2081 RVKVWTSGQV EEYDLDADDI NSRVEMKPK 2082// 2083ID ARF3_TAKRU Reviewed; 181 AA. 2084AC P61207; P16587; 2085DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. 2086DT 23-JAN-2007, sequence version 2. 2087DT 16-MAY-2012, entry version 60. 2088DE RecName: Full=ADP-ribosylation factor 3; 2089GN Name=arf3; 2090OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 2091OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 2092OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 2093OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 2094OC Tetradontoidea; Tetraodontidae; Takifugu. 2095OX NCBI_TaxID=31033; 2096RN [1] 2097RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 2098RX MEDLINE=99177347; PubMed=10077531; 2099RA Gellner K., Brenner S.; 2100RT "Analysis of 148 kb of genomic DNA around the wnt1 locus of Fugu 2101RT rubripes."; 2102RL Genome Res. 9:251-258(1999). 2103CC -!- FUNCTION: GTP-binding protein that functions as an allosteric 2104CC activator of the cholera toxin catalytic subunit, an ADP- 2105CC ribosyltransferase. Involved in protein trafficking; may modulate 2106CC vesicle budding and uncoating within the Golgi apparatus. 2107CC -!- SUBCELLULAR LOCATION: Golgi apparatus. 2108CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. 2109CC ----------------------------------------------------------------------- 2110CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 2111CC Distributed under the Creative Commons Attribution-NoDerivs License 2112CC ----------------------------------------------------------------------- 2113DR EMBL; AF056116; AAC34390.1; -; Genomic_DNA. 2114DR ProteinModelPortal; P61207; -. 2115DR SMR; P61207; 18-177. 2116DR PRIDE; P61207; -. 2117DR eggNOG; COG1100; -. 2118DR InParanoid; P61207; -. 2119DR OrthoDB; EOG4PZJ7Q; -. 2120DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. 2121DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 2122DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 2123DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 2124DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW. 2125DR InterPro; IPR005225; Small_GTP-bd_dom. 2126DR InterPro; IPR024156; Small_GTPase_ARF. 2127DR InterPro; IPR006689; Small_GTPase_ARF/SAR. 2128DR PANTHER; PTHR11711; ARF/SAR; 1. 2129DR Pfam; PF00025; Arf; 1. 2130DR PRINTS; PR00328; SAR1GTPBP. 2131DR SMART; SM00177; ARF; 1. 2132DR TIGRFAMs; TIGR00231; Small_GTP; 1. 2133DR PROSITE; PS51417; ARF; 1. 2134PE 3: Inferred from homology; 2135KW Complete proteome; ER-Golgi transport; Golgi apparatus; GTP-binding; 2136KW Lipoprotein; Myristate; Nucleotide-binding; Protein transport; 2137KW Reference proteome; Transport. 2138FT INIT_MET 1 1 Removed (Potential). 2139FT CHAIN 2 181 ADP-ribosylation factor 3. 2140FT /FTId=PRO_0000207390. 2141FT NP_BIND 24 31 GTP (By similarity). 2142FT NP_BIND 67 71 GTP (By similarity). 2143FT NP_BIND 126 129 GTP (By similarity). 2144FT LIPID 2 2 N-myristoyl glycine (Potential). 2145SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; 2146 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 2147 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 2148 LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK 2149 K 2150// 2151ID ARF3_HUMAN Reviewed; 181 AA. 2152AC P61204; A8K6G8; P16587; 2153DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. 2154DT 23-JAN-2007, sequence version 2. 2155DT 13-JUN-2012, entry version 83. 2156DE RecName: Full=ADP-ribosylation factor 3; 2157GN Name=ARF3; 2158OS Homo sapiens (Human). 2159OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 2160OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 2161OC Catarrhini; Hominidae; Homo. 2162OX NCBI_TaxID=9606; 2163RN [1] 2164RP NUCLEOTIDE SEQUENCE [MRNA]. 2165RC TISSUE=Cerebellum; 2166RX MEDLINE=89345613; PubMed=2474826; DOI=10.1073/pnas.86.16.6101; 2167RA Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J., 2168RA Vaughan M.; 2169RT "Molecular cloning, characterization, and expression of human ADP- 2170RT ribosylation factors: two guanine nucleotide-dependent activators of 2171RT cholera toxin."; 2172RL Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989). 2173RN [2] 2174RP NUCLEOTIDE SEQUENCE [MRNA]. 2175RX MEDLINE=92078170; PubMed=1744102; 2176RA Tsai S.C., Haun R.S., Tsuchiya M., Moss J., Vaughan M.; 2177RT "Isolation and characterization of the human gene for ADP-ribosylation 2178RT factor 3, a 20-kDa guanine nucleotide-binding protein activator of 2179RT cholera toxin."; 2180RL J. Biol. Chem. 266:23053-23059(1991). 2181RN [3] 2182RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2183RC TISSUE=Brain; 2184RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; 2185RT "cDNA clones of human proteins involved in signal transduction 2186RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; 2187RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. 2188RN [4] 2189RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2190RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., 2191RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., 2192RA Phelan M., Farmer A.; 2193RT "Cloning of human full-length CDSs in BD Creator(TM) system donor 2194RT vector."; 2195RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. 2196RN [5] 2197RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2198RC TISSUE=Placenta; 2199RX PubMed=14702039; DOI=10.1038/ng1285; 2200RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., 2201RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., 2202RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., 2203RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., 2204RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., 2205RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., 2206RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., 2207RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., 2208RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., 2209RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., 2210RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., 2211RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., 2212RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., 2213RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., 2214RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., 2215RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., 2216RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., 2217RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., 2218RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., 2219RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., 2220RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., 2221RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., 2222RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., 2223RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., 2224RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., 2225RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., 2226RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., 2227RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; 2228RT "Complete sequencing and characterization of 21,243 full-length human 2229RT cDNAs."; 2230RL Nat. Genet. 36:40-45(2004). 2231RN [6] 2232RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 2233RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 2234RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 2235RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 2236RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 2237RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 2238RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 2239RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 2240RA Venter J.C.; 2241RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 2242RN [7] 2243RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2244RC TISSUE=Brain, Lung, and Skin; 2245RX PubMed=15489334; DOI=10.1101/gr.2596504; 2246RG The MGC Project Team; 2247RT "The status, quality, and expansion of the NIH full-length cDNA 2248RT project: the Mammalian Gene Collection (MGC)."; 2249RL Genome Res. 14:2121-2127(2004). 2250RN [8] 2251RP INTERACTION WITH PRKCABP. 2252RX MEDLINE=20090608; PubMed=10623590; DOI=10.1006/bbrc.1999.1932; 2253RA Takeya R., Takeshige K., Sumimoto H.; 2254RT "Interaction of the PDZ domain of human PICK1 with class I ADP- 2255RT ribosylation factors."; 2256RL Biochem. Biophys. Res. Commun. 267:149-155(2000). 2257RN [9] 2258RP INTERACTION WITH PI4KB AND NCS1, AND SUBCELLULAR LOCATION. 2259RX PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x; 2260RA Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.; 2261RT "Specificity, promiscuity and localization of ARF protein interactions 2262RT with NCS-1 and phosphatidylinositol-4 kinase-III beta."; 2263RL Traffic 8:1080-1092(2007). 2264RN [10] 2265RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 2266RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; 2267RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., 2268RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; 2269RT "Initial characterization of the human central proteome."; 2270RL BMC Syst. Biol. 5:17-17(2011). 2271CC -!- FUNCTION: GTP-binding protein that functions as an allosteric 2272CC activator of the cholera toxin catalytic subunit, an ADP- 2273CC ribosyltransferase. Involved in protein trafficking; may modulate 2274CC vesicle budding and uncoating within the Golgi apparatus. 2275CC -!- SUBUNIT: Interacts with PRKCABP. Interacts with PI4KB and 2276CC NCS1/FREQ at the Golgi complex. 2277CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear 2278CC region. 2279CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. 2280CC ----------------------------------------------------------------------- 2281CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 2282CC Distributed under the Creative Commons Attribution-NoDerivs License 2283CC ----------------------------------------------------------------------- 2284DR EMBL; M74493; AAA58359.1; -; Genomic_DNA. 2285DR EMBL; M33384; AAA83931.1; -; mRNA. 2286DR EMBL; M74491; AAB59425.1; -; mRNA. 2287DR EMBL; AF493882; AAM12596.1; -; mRNA. 2288DR EMBL; BT006670; AAP35316.1; -; mRNA. 2289DR EMBL; AK291633; BAF84322.1; -; mRNA. 2290DR EMBL; CH471111; EAW58026.1; -; Genomic_DNA. 2291DR EMBL; BC007647; AAH07647.1; -; mRNA. 2292DR EMBL; BC007762; AAH07762.1; -; mRNA. 2293DR EMBL; BC017565; AAH17565.1; -; mRNA. 2294DR EMBL; BC028402; AAH28402.1; -; mRNA. 2295DR IPI; IPI00215917; -. 2296DR PIR; A41570; A41570. 2297DR RefSeq; NP_001650.1; NM_001659.2. 2298DR UniGene; Hs.119177; -. 2299DR ProteinModelPortal; P61204; -. 2300DR SMR; P61204; 18-177. 2301DR IntAct; P61204; 7. 2302DR STRING; P61204; -. 2303DR PhosphoSite; P61204; -. 2304DR DMDM; 47117657; -. 2305DR OGP; P16587; -. 2306DR PeptideAtlas; P61204; -. 2307DR PRIDE; P61204; -. 2308DR DNASU; 377; -. 2309DR Ensembl; ENST00000256682; ENSP00000256682; ENSG00000134287. 2310DR Ensembl; ENST00000541959; ENSP00000438510; ENSG00000134287. 2311DR GeneID; 377; -. 2312DR KEGG; hsa:377; -. 2313DR UCSC; uc001rsr.2; human. 2314DR CTD; 377; -. 2315DR GeneCards; GC12M049299; -. 2316DR HGNC; HGNC:654; ARF3. 2317DR MIM; 103190; gene. 2318DR neXtProt; NX_P61204; -. 2319DR PharmGKB; PA24936; -. 2320DR eggNOG; COG1100; -. 2321DR GeneTree; ENSGT00650000093078; -. 2322DR HOGENOM; HOG000163691; -. 2323DR HOVERGEN; HBG002073; -. 2324DR InParanoid; P61204; -. 2325DR KO; K07938; -. 2326DR OMA; LWGKKEM; -. 2327DR OrthoDB; EOG4PZJ7Q; -. 2328DR PhylomeDB; P61204; -. 2329DR NextBio; 1579; -. 2330DR ArrayExpress; P61204; -. 2331DR Bgee; P61204; -. 2332DR CleanEx; HS_ARF3; -. 2333DR Genevestigator; P61204; -. 2334DR GermOnline; ENSG00000134287; Homo sapiens. 2335DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. 2336DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. 2337DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. 2338DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. 2339DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 2340DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 2341DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW. 2342DR InterPro; IPR005225; Small_GTP-bd_dom. 2343DR InterPro; IPR024156; Small_GTPase_ARF. 2344DR InterPro; IPR006689; Small_GTPase_ARF/SAR. 2345DR PANTHER; PTHR11711; ARF/SAR; 1. 2346DR Pfam; PF00025; Arf; 1. 2347DR PRINTS; PR00328; SAR1GTPBP. 2348DR SMART; SM00177; ARF; 1. 2349DR TIGRFAMs; TIGR00231; Small_GTP; 1. 2350DR PROSITE; PS51417; ARF; 1. 2351PE 1: Evidence at protein level; 2352KW Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus; 2353KW GTP-binding; Lipoprotein; Myristate; Nucleotide-binding; 2354KW Protein transport; Reference proteome; Transport. 2355FT INIT_MET 1 1 Removed (Potential). 2356FT CHAIN 2 181 ADP-ribosylation factor 3. 2357FT /FTId=PRO_0000207386. 2358FT NP_BIND 24 31 GTP (By similarity). 2359FT NP_BIND 67 71 GTP (By similarity). 2360FT NP_BIND 126 129 GTP (By similarity). 2361FT LIPID 2 2 N-myristoyl glycine (Potential). 2362SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; 2363 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 2364 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 2365 LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK 2366 K 2367// 2368ID ARF3_MOUSE Reviewed; 181 AA. 2369AC P61205; P16587; 2370DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. 2371DT 23-JAN-2007, sequence version 2. 2372DT 16-MAY-2012, entry version 82. 2373DE RecName: Full=ADP-ribosylation factor 3; 2374GN Name=Arf3; 2375OS Mus musculus (Mouse). 2376OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 2377OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 2378OC Muroidea; Muridae; Murinae; Mus; Mus. 2379OX NCBI_TaxID=10090; 2380RN [1] 2381RP NUCLEOTIDE SEQUENCE [MRNA]. 2382RC STRAIN=ICR; TISSUE=Brain; 2383RX MEDLINE=97103475; PubMed=8947846; 2384RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.; 2385RT "Structure and intracellular localization of mouse ADP-ribosylation 2386RT factors type 1 to type 6 (ARF1-ARF6)."; 2387RL J. Biochem. 120:813-819(1996). 2388RN [2] 2389RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2390RC STRAIN=FVB/N; TISSUE=Mammary tumor; 2391RX PubMed=15489334; DOI=10.1101/gr.2596504; 2392RG The MGC Project Team; 2393RT "The status, quality, and expansion of the NIH full-length cDNA 2394RT project: the Mammalian Gene Collection (MGC)."; 2395RL Genome Res. 14:2121-2127(2004). 2396CC -!- FUNCTION: GTP-binding protein that functions as an allosteric 2397CC activator of the cholera toxin catalytic subunit, an ADP- 2398CC ribosyltransferase. Involved in protein trafficking; may modulate 2399CC vesicle budding and uncoating within the Golgi apparatus. 2400CC -!- SUBUNIT: Interacts with PRKCABP (By similarity). Interacts with 2401CC PI4KB and NCS1/FREQ at the Golgi complex (By similarity). 2402CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasm, 2403CC perinuclear region (By similarity). 2404CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. 2405CC ----------------------------------------------------------------------- 2406CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 2407CC Distributed under the Creative Commons Attribution-NoDerivs License 2408CC ----------------------------------------------------------------------- 2409DR EMBL; D87900; BAA13492.1; -; mRNA. 2410DR EMBL; BC014778; AAH14778.1; -; mRNA. 2411DR EMBL; BC024935; AAH24935.1; -; mRNA. 2412DR IPI; IPI00221614; -. 2413DR PIR; JC4947; JC4947. 2414DR RefSeq; NP_031504.1; NM_007478.3. 2415DR UniGene; Mm.221298; -. 2416DR ProteinModelPortal; P61205; -. 2417DR SMR; P61205; 18-177. 2418DR IntAct; P61205; 2. 2419DR STRING; P61205; -. 2420DR PhosphoSite; P61205; -. 2421DR PRIDE; P61205; -. 2422DR Ensembl; ENSMUST00000053183; ENSMUSP00000050689; ENSMUSG00000051853. 2423DR GeneID; 11842; -. 2424DR KEGG; mmu:11842; -. 2425DR CTD; 377; -. 2426DR MGI; MGI:99432; Arf3. 2427DR HOGENOM; HOG000163691; -. 2428DR HOVERGEN; HBG002073; -. 2429DR InParanoid; P61205; -. 2430DR KO; K07938; -. 2431DR OMA; LWGKKEM; -. 2432DR OrthoDB; EOG4PZJ7Q; -. 2433DR NextBio; 279791; -. 2434DR ArrayExpress; P61205; -. 2435DR Bgee; P61205; -. 2436DR CleanEx; MM_ARF3; -. 2437DR Genevestigator; P61205; -. 2438DR GermOnline; ENSMUSG00000051853; Mus musculus. 2439DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. 2440DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. 2441DR GO; GO:0005525; F:GTP binding; TAS:MGI. 2442DR GO; GO:0015031; P:protein transport; TAS:MGI. 2443DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 2444DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW. 2445DR InterPro; IPR005225; Small_GTP-bd_dom. 2446DR InterPro; IPR024156; Small_GTPase_ARF. 2447DR InterPro; IPR006689; Small_GTPase_ARF/SAR. 2448DR PANTHER; PTHR11711; ARF/SAR; 1. 2449DR Pfam; PF00025; Arf; 1. 2450DR PRINTS; PR00328; SAR1GTPBP. 2451DR SMART; SM00177; ARF; 1. 2452DR TIGRFAMs; TIGR00231; Small_GTP; 1. 2453DR PROSITE; PS51417; ARF; 1. 2454PE 2: Evidence at transcript level; 2455KW Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus; 2456KW GTP-binding; Lipoprotein; Myristate; Nucleotide-binding; 2457KW Protein transport; Reference proteome; Transport. 2458FT INIT_MET 1 1 Removed (Potential). 2459FT CHAIN 2 181 ADP-ribosylation factor 3. 2460FT /FTId=PRO_0000207387. 2461FT NP_BIND 24 31 GTP (By similarity). 2462FT NP_BIND 67 71 GTP (By similarity). 2463FT NP_BIND 126 129 GTP (By similarity). 2464FT LIPID 2 2 N-myristoyl glycine (Potential). 2465SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; 2466 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 2467 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 2468 LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK 2469 K 2470// 2471ID ARF3_RAT Reviewed; 181 AA. 2472AC P61206; P16587; 2473DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. 2474DT 23-JAN-2007, sequence version 2. 2475DT 16-MAY-2012, entry version 77. 2476DE RecName: Full=ADP-ribosylation factor 3; 2477DE AltName: Full=Liver regeneration-related protein LRRG202; 2478GN Name=Arf3; ORFNames=Ac1-253; 2479OS Rattus norvegicus (Rat). 2480OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 2481OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 2482OC Muroidea; Muridae; Murinae; Rattus. 2483OX NCBI_TaxID=10116; 2484RN [1] 2485RP NUCLEOTIDE SEQUENCE [MRNA]. 2486RC TISSUE=Brain; 2487RX MEDLINE=96408698; PubMed=8813705; DOI=10.1007/BF00226058; 2488RA Price S.R., Nightingale M.S., Tsuchiya M., Moss J., Vaughan M.; 2489RT "Interspecies relationships among ADP-ribosylation factors (ARFs): 2490RT evidence of evolutionary pressure to maintain individual identities."; 2491RL Mol. Cell. Biochem. 159:15-23(1996). 2492RN [2] 2493RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2494RC TISSUE=Liver; 2495RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., 2496RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., 2497RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.; 2498RT "Liver regeneration after PH."; 2499RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. 2500RN [3] 2501RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 2502RC TISSUE=Brain; 2503RX PubMed=15489334; DOI=10.1101/gr.2596504; 2504RG The MGC Project Team; 2505RT "The status, quality, and expansion of the NIH full-length cDNA 2506RT project: the Mammalian Gene Collection (MGC)."; 2507RL Genome Res. 14:2121-2127(2004). 2508CC -!- FUNCTION: GTP-binding protein that functions as an allosteric 2509CC activator of the cholera toxin catalytic subunit, an ADP- 2510CC ribosyltransferase. Involved in protein trafficking; may modulate 2511CC vesicle budding and uncoating within the Golgi apparatus. 2512CC -!- SUBUNIT: Interacts with PRKCABP (By similarity). Interacts with 2513CC PI4KB and NCS1/FREQ at the Golgi complex (By similarity). 2514CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasm, 2515CC perinuclear region (By similarity). 2516CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. 2517CC ----------------------------------------------------------------------- 2518CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 2519CC Distributed under the Creative Commons Attribution-NoDerivs License 2520CC ----------------------------------------------------------------------- 2521DR EMBL; L12382; AAA40687.1; -; mRNA. 2522DR EMBL; AY325223; AAP92624.1; -; mRNA. 2523DR EMBL; BC088865; AAH88865.1; -; mRNA. 2524DR IPI; IPI00231674; -. 2525DR RefSeq; NP_543180.1; NM_080904.2. 2526DR UniGene; Rn.106440; -. 2527DR ProteinModelPortal; P61206; -. 2528DR SMR; P61206; 18-177. 2529DR IntAct; P61206; 1. 2530DR MINT; MINT-1775307; -. 2531DR STRING; P61206; -. 2532DR PhosphoSite; P61206; -. 2533DR World-2DPAGE; 0004:P61206; -. 2534DR PRIDE; P61206; -. 2535DR Ensembl; ENSRNOT00000044558; ENSRNOP00000047811; ENSRNOG00000033155. 2536DR GeneID; 140940; -. 2537DR KEGG; rno:140940; -. 2538DR UCSC; NM_080904; rat. 2539DR CTD; 377; -. 2540DR RGD; 621273; Arf3. 2541DR GeneTree; ENSGT00650000093078; -. 2542DR HOGENOM; HOG000163691; -. 2543DR HOVERGEN; HBG002073; -. 2544DR InParanoid; P61206; -. 2545DR KO; K07938; -. 2546DR OMA; LWGKKEM; -. 2547DR OrthoDB; EOG4PZJ7Q; -. 2548DR NextBio; 620834; -. 2549DR ArrayExpress; P61206; -. 2550DR Genevestigator; P61206; -. 2551DR GermOnline; ENSRNOG00000033155; Rattus norvegicus. 2552DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. 2553DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. 2554DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 2555DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. 2556DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. 2557DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW. 2558DR InterPro; IPR005225; Small_GTP-bd_dom. 2559DR InterPro; IPR024156; Small_GTPase_ARF. 2560DR InterPro; IPR006689; Small_GTPase_ARF/SAR. 2561DR PANTHER; PTHR11711; ARF/SAR; 1. 2562DR Pfam; PF00025; Arf; 1. 2563DR PRINTS; PR00328; SAR1GTPBP. 2564DR SMART; SM00177; ARF; 1. 2565DR TIGRFAMs; TIGR00231; Small_GTP; 1. 2566DR PROSITE; PS51417; ARF; 1. 2567PE 1: Evidence at protein level; 2568KW Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus; 2569KW GTP-binding; Lipoprotein; Myristate; Nucleotide-binding; 2570KW Protein transport; Reference proteome; Transport. 2571FT INIT_MET 1 1 Removed (Potential). 2572FT CHAIN 2 181 ADP-ribosylation factor 3. 2573FT /FTId=PRO_0000207389. 2574FT NP_BIND 24 31 GTP (By similarity). 2575FT NP_BIND 67 71 GTP (By similarity). 2576FT NP_BIND 126 129 GTP (By similarity). 2577FT LIPID 2 2 N-myristoyl glycine (Potential). 2578SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; 2579 MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN 2580 ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV 2581 LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK 2582 K 2583// 2584ID BGAL_ECOLI Reviewed; 1024 AA. 2585AC P00722; Q2MC80; 2586DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 2587DT 23-JAN-2007, sequence version 2. 2588DT 13-JUN-2012, entry version 140. 2589DE RecName: Full=Beta-galactosidase; 2590DE Short=Beta-gal; 2591DE EC=3.2.1.23; 2592DE AltName: Full=Lactase; 2593GN Name=lacZ; OrderedLocusNames=b0344, JW0335; 2594OS Escherichia coli (strain K12). 2595OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 2596OC Enterobacteriaceae; Escherichia. 2597OX NCBI_TaxID=83333; 2598RN [1] 2599RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 2600RX MEDLINE=84028567; PubMed=6313347; 2601RA Kalnins A., Otto K., Ruether U., Mueller-Hill B.; 2602RT "Sequence of the lacZ gene of Escherichia coli."; 2603RL EMBO J. 2:593-597(1983). 2604RN [2] 2605RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 2606RC STRAIN=K12 / MG1655 / ATCC 47076; 2607RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., 2608RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., 2609RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; 2610RT "Sequence of minutes 4-25 of Escherichia coli."; 2611RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 2612RN [3] 2613RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 2614RC STRAIN=K12 / MG1655 / ATCC 47076; 2615RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; 2616RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., 2617RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., 2618RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., 2619RA Mau B., Shao Y.; 2620RT "The complete genome sequence of Escherichia coli K-12."; 2621RL Science 277:1453-1474(1997). 2622RN [4] 2623RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 2624RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 2625RX PubMed=16738553; DOI=10.1038/msb4100049; 2626RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., 2627RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; 2628RT "Highly accurate genome sequences of Escherichia coli K-12 strains 2629RT MG1655 and W3110."; 2630RL Mol. Syst. Biol. 2:E1-E5(2006). 2631RN [5] 2632RP PROTEIN SEQUENCE OF 2-1024. 2633RX MEDLINE=78218239; PubMed=97298; 2634RA Fowler A.V., Zabin I.; 2635RT "Amino acid sequence of beta-galactosidase. XI. Peptide ordering 2636RT procedures and the complete sequence."; 2637RL J. Biol. Chem. 253:5521-5525(1978). 2638RN [6] 2639RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476. 2640RX MEDLINE=80188189; PubMed=6246435; DOI=10.1038/285038a0; 2641RA Calos M.P., Miller J.H.; 2642RT "Molecular consequences of deletion formation mediated by the 2643RT transposon Tn9."; 2644RL Nature 285:38-41(1980). 2645RN [7] 2646RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024. 2647RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; 2648RA Buechel D.E., Gronenborn B., Mueller-Hill B.; 2649RT "Sequence of the lactose permease gene."; 2650RL Nature 283:541-545(1980). 2651RN [8] 2652RP INDUCTION BY ALLOLACTOSE. 2653RX PubMed=4562709; DOI=10.1016/0022-2836(72)90253-7; 2654RA Jobe A., Bourgeois S.; 2655RT "lac repressor-operator interaction. VI. The natural inducer of the 2656RT lac operon."; 2657RL J. Mol. Biol. 69:397-408(1972). 2658RN [9] 2659RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. 2660RX PubMed=114210; DOI=10.1021/bi00586a005; 2661RA Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.; 2662RT "Interaction of divalent cations with beta-galactosidase (Escherichia 2663RT coli)."; 2664RL Biochemistry 18:4090-4095(1979). 2665RN [10] 2666RP ACTIVE SITE REGIONS. 2667RX MEDLINE=83290932; PubMed=6411710; 2668RA Fowler A.V., Smith P.J.; 2669RT "The active site regions of lacZ and ebg beta-galactosidases are 2670RT homologous."; 2671RL J. Biol. Chem. 258:10204-10207(1983). 2672RN [11] 2673RP ACTIVE SITE GLU-462. 2674RX MEDLINE=84108409; PubMed=6420154; 2675RX DOI=10.1111/j.1432-1033.1984.tb07947.x; 2676RA Herrchen M., Legler G.; 2677RT "Identification of an essential carboxylate group at the active site 2678RT of lacZ beta-galactosidase from Escherichia coli."; 2679RL Eur. J. Biochem. 138:527-531(1984). 2680RN [12] 2681RP ACTIVE SITE GLU-538. 2682RX MEDLINE=92283812; PubMed=1350782; 2683RA Gebler J.C., Aebersold R., Withers S.G.; 2684RT "Glu-537, not Glu-461, is the nucleophile in the active site of (lac 2685RT Z) beta-galactosidase from Escherichia coli."; 2686RL J. Biol. Chem. 267:11126-11130(1992). 2687RN [13] 2688RP MUTAGENESIS OF GLU-462, AND COFACTOR. 2689RX PubMed=7577931; DOI=10.1021/bi00041a022; 2690RA Martinez-Bilbao M., Gaunt M.T., Huber R.E.; 2691RT "E461H-beta-galactosidase (Escherichia coli): altered divalent metal 2692RT specificity and slow but reversible metal inactivation."; 2693RL Biochemistry 34:13437-13442(1995). 2694RN [14] 2695RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-541. 2696RX PubMed=8662937; DOI=10.1074/jbc.271.24.14296; 2697RA Roth N.J., Huber R.E.; 2698RT "The beta-galactosidase (Escherichia coli) reaction is partly 2699RT facilitated by interactions of His-540 with the C6 hydroxyl of 2700RT galactose."; 2701RL J. Biol. Chem. 271:14296-14301(1996). 2702RN [15] 2703RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-358. 2704RX PubMed=9665715; DOI=10.1021/bi972796t; 2705RA Roth N.J., Rob B., Huber R.E.; 2706RT "His-357 of beta-galactosidase (Escherichia coli) interacts with the 2707RT C3 hydroxyl in the transition state and helps to mediate catalysis."; 2708RL Biochemistry 37:10099-10107(1998). 2709RN [16] 2710RP MUTAGENESIS OF HIS-392. 2711RX PubMed=11310566; DOI=10.1139/bcb-79-2-183; 2712RA Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K.; 2713RT "His-391 of beta-galactosidase (Escherichia coli) promotes catalyses 2714RT by strong interactions with the transition state."; 2715RL Biochem. Cell Biol. 79:183-193(2001). 2716RN [17] 2717RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TRP-1000. 2718RX PubMed=12578395; DOI=10.1021/bi0270642; 2719RA Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.; 2720RT "Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for 2721RT binding, catalysis, and synthesis of allolactose, the natural lac 2722RT operon inducer."; 2723RL Biochemistry 42:1796-1803(2003). 2724RN [18] 2725RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-202. 2726RX PubMed=15060622; DOI=10.1139/o04-004; 2727RA Xu J., McRae M.A., Harron S., Rob B., Huber R.E.; 2728RT "A study of the relationships of interactions between Asp-201, Na+ or 2729RT K+, and galactosyl C6 hydroxyl and their effects on binding and 2730RT reactivity of beta-galactosidase."; 2731RL Biochem. Cell Biol. 82:275-284(2004). 2732RN [19] 2733RP REVIEW. 2734RX PubMed=15950161; DOI=10.1016/j.crvi.2005.03.006; 2735RA Matthews B.W.; 2736RT "The structure of E. coli beta-galactosidase."; 2737RL C. R. Biol. 328:549-556(2005). 2738RN [20] 2739RP COFACTOR, AND MUTAGENESIS OF GLU-798. 2740RX PubMed=17126292; DOI=10.1016/j.bbrc.2006.11.061; 2741RA Sutendra G., Wong S., Fraser M.E., Huber R.E.; 2742RT "Beta-galactosidase (Escherichia coli) has a second catalytically 2743RT important Mg2+ site."; 2744RL Biochem. Biophys. Res. Commun. 352:566-570(2007). 2745RN [21] 2746RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, 2747RP AND SUBUNIT. 2748RX MEDLINE=94277211; PubMed=8008071; DOI=10.1038/369761a0; 2749RA Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.; 2750RT "Three-dimensional structure of beta-galactosidase from E. coli."; 2751RL Nature 369:761-766(1994). 2752RN [22] 2753RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND 2754RP SODIUM IONS. 2755RX PubMed=11045615; 2756RA Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E., 2757RA Tronrud D.E., Matthews B.W.; 2758RT "High resolution refinement of beta-galactosidase in a new crystal 2759RT form reveals multiple metal-binding sites and provides a structural 2760RT basis for alpha-complementation."; 2761RL Protein Sci. 9:1685-1699(2000). 2762RN [23] 2763RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ANALOGS 2764RP SUBSTRATE, MUTAGENESIS OF GLU-538 AND PHE-602, AND REACTION MECHANISM. 2765RX MEDLINE=21590184; PubMed=11732897; DOI=10.1021/bi011727i; 2766RA Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L., 2767RA Withers S.G., Matthews B.W.; 2768RT "A structural view of the action of Escherichia coli (lacZ) beta- 2769RT galactosidase."; 2770RL Biochemistry 40:14781-14794(2001). 2771RN [24] 2772RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN 2773RP COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND ANALOGS SUBSTRATE, 2774RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND MUTAGENESIS OF 2775RP GLY-795. 2776RX PubMed=14621996; DOI=10.1021/bi035506j; 2777RA Juers D.H., Hakda S., Matthews B.W., Huber R.E.; 2778RT "Structural basis for the altered activity of Gly794 variants of 2779RT Escherichia coli beta-galactosidase."; 2780RL Biochemistry 42:13505-13511(2003). 2781CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- 2782CC galactose residues in beta-D-galactosides. 2783CC -!- COFACTOR: Binds 2 magnesium ions per monomer. Can also use 2784CC manganese. 2785CC -!- COFACTOR: Binds 1 sodium ion per monomer. 2786CC -!- ENZYME REGULATION: Inhibited by phenylethyl thio-beta-D- 2787CC galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L- 2788CC ribose, D-galactonolactone, lactose and 2-amino-D-galactose. 2789CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 2790CC Kinetic parameters: 2791CC KM=0.04 mM for p-nitrophenyl beta-D-galactoside; 2792CC KM=0.12 mM for o-nitrophenyl beta-D-galactoside; 2793CC KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside; 2794CC KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside; 2795CC KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside; 2796CC KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside; 2797CC KM=34 uM for p-nitrophenyl beta-D-galactoside (with magnesium as 2798CC cofactor and 30 degrees Celsius); 2799CC KM=140 uM for o-nitrophenyl beta-D-galactoside (with magnesium 2800CC as cofactor and 30 degrees Celsius); 2801CC KM=940 uM for allolactose (with magnesium as cofactor and 30 2802CC degrees Celsius); 2803CC KM=1350 uM for lactose (with magnesium as cofactor and 30 2804CC degrees Celsius); 2805CC Vmax=30.9 umol/min/mg enzyme with lactose as substrate (with 2806CC magnesium as cofactor and 30 degrees Celsius); 2807CC Vmax=49.7 umol/min/mg enzyme with allolactose as substrate (with 2808CC magnesium as cofactor and 30 degrees Celsius); 2809CC Vmax=59.7 umol/min/mg enzyme with p-nitrophenyl beta-D- 2810CC galactoside as substrate (with magnesium as cofactor and 30 2811CC degrees Celsius); 2812CC Vmax=360 umol/min/mg enzyme with o-nitrophenyl beta-D- 2813CC galactoside as substrate (with magnesium as cofactor and 30 2814CC degrees Celsius); 2815CC Note=The values for the enzymatic assays using manganese as 2816CC cofactor are very close; 2817CC -!- SUBUNIT: Homotetramer. 2818CC -!- INTERACTION: 2819CC P03023:lacI; NbExp=1; IntAct=EBI-369998, EBI-909231; 2820CC P0ACA1:yibF; NbExp=1; IntAct=EBI-369998, EBI-1133142; 2821CC -!- INDUCTION: By allolactose. 2822CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. 2823CC -!- WEB RESOURCE: Name=Worthington enzyme manual; 2824CC URL="http://www.worthington-biochem.com/BG/"; 2825CC ----------------------------------------------------------------------- 2826CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 2827CC Distributed under the Creative Commons Attribution-NoDerivs License 2828CC ----------------------------------------------------------------------- 2829DR EMBL; J01636; AAA24053.1; -; Genomic_DNA. 2830DR EMBL; V00296; CAA23573.1; -; Genomic_DNA. 2831DR EMBL; U73857; AAB18068.1; -; Genomic_DNA. 2832DR EMBL; U00096; AAC73447.1; -; Genomic_DNA. 2833DR EMBL; AP009048; BAE76126.1; -; Genomic_DNA. 2834DR EMBL; V00295; CAA23570.1; -; Genomic_DNA. 2835DR PIR; A90981; GBEC. 2836DR RefSeq; NP_414878.1; NC_000913.2. 2837DR PDB; 1BGL; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-1024. 2838DR PDB; 1BGM; X-ray; 2.50 A; I/J/K/L/M/N/O/P=2-1024. 2839DR PDB; 1DP0; X-ray; 1.70 A; A/B/C/D=10-1024. 2840DR PDB; 1F49; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-1024. 2841DR PDB; 1F4A; X-ray; 2.80 A; A/B/C/D=4-1024. 2842DR PDB; 1F4H; X-ray; 2.80 A; A/B/C/D=4-1024. 2843DR PDB; 1GHO; X-ray; 2.50 A; I/J/K/L/M/N/O/P=2-1024. 2844DR PDB; 1HN1; X-ray; 3.00 A; A/B/C/D=10-1023. 2845DR PDB; 1JYN; X-ray; 1.80 A; A/B/C/D=10-1024. 2846DR PDB; 1JYV; X-ray; 1.75 A; A/B/C/D=10-1024. 2847DR PDB; 1JYW; X-ray; 1.55 A; A/B/C/D=10-1024. 2848DR PDB; 1JYX; X-ray; 1.75 A; A/B/C/D=10-1024. 2849DR PDB; 1JYY; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-1024. 2850DR PDB; 1JYZ; X-ray; 2.70 A; I/J/K/L/M/N/O/P=2-1024. 2851DR PDB; 1JZ0; X-ray; 2.60 A; A/B/C/D/E/F/G/H=2-1024. 2852DR PDB; 1JZ1; X-ray; 2.60 A; I/J/K/L/M/N/O/P=2-1024. 2853DR PDB; 1JZ2; X-ray; 2.10 A; A/B/C/D=2-1024. 2854DR PDB; 1JZ3; X-ray; 1.75 A; A/B/C/D=10-1024. 2855DR PDB; 1JZ4; X-ray; 2.10 A; A/B/C/D=10-1024. 2856DR PDB; 1JZ5; X-ray; 1.80 A; A/B/C/D=10-1024. 2857DR PDB; 1JZ6; X-ray; 2.10 A; A/B/C/D=10-1024. 2858DR PDB; 1JZ7; X-ray; 1.50 A; A/B/C/D=10-1024. 2859DR PDB; 1JZ8; X-ray; 1.50 A; A/B/C/D=10-1024. 2860DR PDB; 1PX3; X-ray; 1.60 A; A/B/C/D=10-1024. 2861DR PDB; 1PX4; X-ray; 1.60 A; A/B/C/D=10-1024. 2862DR PDB; 3CZJ; X-ray; 2.05 A; A/B/C/D=10-1024. 2863DR PDB; 3DYM; X-ray; 2.05 A; A/B/C/D=10-1024. 2864DR PDB; 3DYO; X-ray; 1.80 A; A/B/C/D=10-1024. 2865DR PDB; 3DYP; X-ray; 1.75 A; A/B/C/D=10-1024. 2866DR PDB; 3E1F; X-ray; 3.00 A; 1/2/3/4=10-1024. 2867DR PDB; 3I3B; X-ray; 2.20 A; A/B/C/D=10-1024. 2868DR PDB; 3I3D; X-ray; 2.20 A; A/B/C/D=10-1024. 2869DR PDB; 3I3E; X-ray; 2.10 A; A/B/C/D=10-1024. 2870DR PDB; 3IAP; X-ray; 2.00 A; A/B/C/D=10-1024. 2871DR PDB; 3IAQ; X-ray; 2.70 A; A/B/C/D=10-1024. 2872DR PDB; 3MUY; X-ray; 2.50 A; 1/2/3/4=10-1024. 2873DR PDB; 3MUZ; X-ray; 1.90 A; 1/2/3/4=10-1024. 2874DR PDB; 3MV0; X-ray; 2.20 A; 1/2/3/4=10-1024. 2875DR PDB; 3MV1; X-ray; 2.20 A; 1/2/3/4=10-1024. 2876DR PDB; 3SEP; X-ray; 2.05 A; A/B/C/D=10-1024. 2877DR PDB; 3T08; X-ray; 2.00 A; A/B/C/D=10-1024. 2878DR PDB; 3T09; X-ray; 1.75 A; A/B/C/D=10-1024. 2879DR PDB; 3T0A; X-ray; 1.90 A; A/B/C/D=10-1024. 2880DR PDB; 3T0B; X-ray; 2.40 A; A/B/C/D=10-1024. 2881DR PDB; 3T0D; X-ray; 1.93 A; A/B/C/D=10-1024. 2882DR PDB; 3T2O; X-ray; 1.85 A; A/B/C/D=10-1024. 2883DR PDB; 3T2P; X-ray; 2.60 A; A/B/C/D=10-1024. 2884DR PDB; 3T2Q; X-ray; 2.40 A; A/B/C/D=10-1024. 2885DR PDB; 3VD3; X-ray; 2.80 A; A/B/C/D=10-1024. 2886DR PDB; 3VD4; X-ray; 2.00 A; A/B/C/D=10-1024. 2887DR PDB; 3VD5; X-ray; 2.70 A; A/B/C/D=10-1024. 2888DR PDB; 3VD7; X-ray; 2.87 A; A/B/C/D=10-1024. 2889DR PDB; 3VD9; X-ray; 2.05 A; A/B/C/D=10-1024. 2890DR PDB; 3VDA; X-ray; 2.50 A; A/B/C/D=10-1024. 2891DR PDB; 3VDB; X-ray; 2.05 A; A/B/C/D=10-1024. 2892DR PDB; 3VDC; X-ray; 2.55 A; A/B/C/D=10-1024. 2893DR PDBsum; 1BGL; -. 2894DR PDBsum; 1BGM; -. 2895DR PDBsum; 1DP0; -. 2896DR PDBsum; 1F49; -. 2897DR PDBsum; 1F4A; -. 2898DR PDBsum; 1F4H; -. 2899DR PDBsum; 1GHO; -. 2900DR PDBsum; 1HN1; -. 2901DR PDBsum; 1JYN; -. 2902DR PDBsum; 1JYV; -. 2903DR PDBsum; 1JYW; -. 2904DR PDBsum; 1JYX; -. 2905DR PDBsum; 1JYY; -. 2906DR PDBsum; 1JYZ; -. 2907DR PDBsum; 1JZ0; -. 2908DR PDBsum; 1JZ1; -. 2909DR PDBsum; 1JZ2; -. 2910DR PDBsum; 1JZ3; -. 2911DR PDBsum; 1JZ4; -. 2912DR PDBsum; 1JZ5; -. 2913DR PDBsum; 1JZ6; -. 2914DR PDBsum; 1JZ7; -. 2915DR PDBsum; 1JZ8; -. 2916DR PDBsum; 1PX3; -. 2917DR PDBsum; 1PX4; -. 2918DR PDBsum; 3CZJ; -. 2919DR PDBsum; 3DYM; -. 2920DR PDBsum; 3DYO; -. 2921DR PDBsum; 3DYP; -. 2922DR PDBsum; 3E1F; -. 2923DR PDBsum; 3I3B; -. 2924DR PDBsum; 3I3D; -. 2925DR PDBsum; 3I3E; -. 2926DR PDBsum; 3IAP; -. 2927DR PDBsum; 3IAQ; -. 2928DR PDBsum; 3MUY; -. 2929DR PDBsum; 3MUZ; -. 2930DR PDBsum; 3MV0; -. 2931DR PDBsum; 3MV1; -. 2932DR PDBsum; 3SEP; -. 2933DR PDBsum; 3T08; -. 2934DR PDBsum; 3T09; -. 2935DR PDBsum; 3T0A; -. 2936DR PDBsum; 3T0B; -. 2937DR PDBsum; 3T0D; -. 2938DR PDBsum; 3T2O; -. 2939DR PDBsum; 3T2P; -. 2940DR PDBsum; 3T2Q; -. 2941DR PDBsum; 3VD3; -. 2942DR PDBsum; 3VD4; -. 2943DR PDBsum; 3VD5; -. 2944DR PDBsum; 3VD7; -. 2945DR PDBsum; 3VD9; -. 2946DR PDBsum; 3VDA; -. 2947DR PDBsum; 3VDB; -. 2948DR PDBsum; 3VDC; -. 2949DR ProteinModelPortal; P00722; -. 2950DR SMR; P00722; 14-1024. 2951DR IntAct; P00722; 76. 2952DR CAZy; GH2; Glycoside Hydrolase Family 2. 2953DR ECO2DBASE; E123.0; 6TH EDITION. 2954DR PRIDE; P00722; -. 2955DR EnsemblBacteria; EBESCT00000001916; EBESCP00000001916; EBESCG00000001573. 2956DR EnsemblBacteria; EBESCT00000001917; EBESCP00000001917; EBESCG00000001573. 2957DR EnsemblBacteria; EBESCT00000001918; EBESCP00000001918; EBESCG00000001573. 2958DR EnsemblBacteria; EBESCT00000001919; EBESCP00000001919; EBESCG00000001573. 2959DR EnsemblBacteria; EBESCT00000016416; EBESCP00000015707; EBESCG00000015476. 2960DR GeneID; 945006; -. 2961DR GenomeReviews; AP009048_GR; JW0335. 2962DR GenomeReviews; U00096_GR; b0344. 2963DR KEGG; eco:b0344; -. 2964DR PATRIC; 32115821; VBIEscCol129921_0352. 2965DR EchoBASE; EB0522; -. 2966DR EcoGene; EG10527; lacZ. 2967DR HOGENOM; HOG000252443; -. 2968DR KO; K01190; -. 2969DR OMA; DFHVATH; -. 2970DR ProtClustDB; PRK09525; -. 2971DR BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -. 2972DR BioCyc; MetaCyc:BETAGALACTOSID-MONOMER; -. 2973DR DrugBank; DB01093; Dimethyl sulfoxide. 2974DR EvolutionaryTrace; P00722; -. 2975DR Genevestigator; P00722; -. 2976DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. 2977DR GO; GO:0004565; F:beta-galactosidase activity; IDA:EcoCyc. 2978DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. 2979DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 2980DR GO; GO:0005990; P:lactose catabolic process; IMP:EcoCyc. 2981DR Gene3D; G3DSA:2.60.40.320; Glyco_hydro_2/20_Ig-like; 2. 2982DR Gene3D; G3DSA:2.70.98.10; Glyco_hydro_42_D5; 1. 2983DR Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1. 2984DR HAMAP; MF_01687; Beta_gal; 1; -. 2985DR InterPro; IPR004199; B-gal_small/dom_5. 2986DR InterPro; IPR008979; Galactose-bd-like. 2987DR InterPro; IPR011013; Glyco_hydro-type_carb-bd. 2988DR InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub. 2989DR InterPro; IPR006101; Glyco_hydro_2. 2990DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. 2991DR InterPro; IPR023232; Glyco_hydro_2_AS. 2992DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase. 2993DR InterPro; IPR023230; Glyco_hydro_2_CS. 2994DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. 2995DR InterPro; IPR006104; Glyco_hydro_2_N. 2996DR InterPro; IPR006103; Glyco_hydro_2_TIM. 2997DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. 2998DR InterPro; IPR017853; Glycoside_hydrolase_SF. 2999DR Pfam; PF02929; Bgal_small_N; 1. 3000DR Pfam; PF00703; Glyco_hydro_2; 1. 3001DR Pfam; PF02836; Glyco_hydro_2_C; 1. 3002DR Pfam; PF02837; Glyco_hydro_2_N; 1. 3003DR PRINTS; PR00132; GLHYDRLASE2. 3004DR SMART; SM01038; Bgal_small_N; 1. 3005DR SUPFAM; SSF49785; Gal_bind_like; 1. 3006DR SUPFAM; SSF74650; Gal_mut_like; 1. 3007DR SUPFAM; SSF49303; Glyco_hydro_2Ig; 2. 3008DR SUPFAM; SSF51445; Glyco_hydro_cat; 1. 3009DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. 3010DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. 3011PE 1: Evidence at protein level; 3012KW 3D-structure; Complete proteome; Direct protein sequencing; 3013KW Glycosidase; Hydrolase; Magnesium; Manganese; Metal-binding; 3014KW Reference proteome; Sodium. 3015FT INIT_MET 1 1 Removed. 3016FT CHAIN 2 1024 Beta-galactosidase. 3017FT /FTId=PRO_0000057650. 3018FT REGION 538 541 Substrate binding. 3019FT ACT_SITE 462 462 Proton donor. 3020FT ACT_SITE 538 538 Nucleophile. 3021FT METAL 202 202 Sodium. 3022FT METAL 417 417 Magnesium 1. 3023FT METAL 419 419 Magnesium 1. 3024FT METAL 462 462 Magnesium 1. 3025FT METAL 598 598 Magnesium 2. 3026FT METAL 602 602 Sodium; via carbonyl oxygen. 3027FT METAL 605 605 Sodium. 3028FT BINDING 103 103 Substrate. 3029FT BINDING 202 202 Substrate. 3030FT BINDING 462 462 Substrate. 3031FT BINDING 605 605 Substrate. 3032FT BINDING 1000 1000 Substrate. 3033FT SITE 358 358 Transition state stabilizer. 3034FT SITE 392 392 Transition state stabilizer. 3035FT SITE 1000 1000 Important for ensuring that an 3036FT appropriate proportion of lactose is 3037FT converted to allolactose. 3038FT MUTAGEN 202 202 D->E,N: Causes a significant decrease in 3039FT binding affinity in the absence of 3040FT monovalent cations or in the presence of 3041FT potassium ions, but only a moderate 3042FT decrease in the presence of sodium ions. 3043FT MUTAGEN 202 202 D->F: Obliterates all binding and 3044FT catalysis. 3045FT MUTAGEN 358 358 H->D,F,L,N: Less stable to heat than 3046FT wild-type. Causes significant 3047FT destabilizations of the first transition 3048FT state. 3049FT MUTAGEN 392 392 H->E,F,K: Essentially inactive unless 3050FT very rapid purification. Causes very 3051FT large destabilizations of the transition 3052FT state. 3053FT MUTAGEN 462 462 E->H: Slowly inactivates galactosidase 3054FT activity by reducing the binding of 3055FT magnesium. It increases binding 3056FT specificity. 3057FT MUTAGEN 538 538 E->Q: 10000-fold decrease in the beta- 3058FT galactosidase activity. 3059FT MUTAGEN 541 541 H->E,F,N: Poorly reactive with galactosyl 3060FT substrates. Less stable to heat than 3061FT wild-type. 3062FT MUTAGEN 602 602 F->A: Decreases the stability of the loop 3063FT 794-804. 3064FT MUTAGEN 795 795 G->A: It forces the apoenzyme to adopt 3065FT the closed rather than the open 3066FT conformation. Reduces the binding 3067FT affinity. 3068FT MUTAGEN 798 798 E->A,L: The catalytic efficiency is not 3069FT increased, when the sodium concentration 3070FT increases. 3071FT MUTAGEN 798 798 E->D,Q: Small increase of the catalytic 3072FT efficiency, when the sodium concentration 3073FT increases. 3074FT MUTAGEN 1000 1000 W->F,G,L,T: Decreases affinity for 3075FT substrate. 3076FT HELIX 16 18 3077FT STRAND 23 26 3078FT STRAND 37 39 3079FT HELIX 40 45 3080FT STRAND 52 54 3081FT STRAND 57 66 3082FT HELIX 67 69 3083FT HELIX 73 76 3084FT STRAND 83 88 3085FT HELIX 91 94 3086FT STRAND 100 105 3087FT STRAND 121 130 3088FT HELIX 132 136 3089FT STRAND 137 145 3090FT STRAND 147 155 3091FT STRAND 158 164 3092FT STRAND 170 173 3093FT TURN 175 177 3094FT STRAND 180 192 3095FT HELIX 194 198 3096FT STRAND 202 205 3097FT STRAND 213 218 3098FT STRAND 220 232 3099FT STRAND 236 249 3100FT STRAND 255 263 3101FT STRAND 266 275 3102FT STRAND 289 298 3103FT STRAND 304 307 3104FT STRAND 310 318 3105FT STRAND 323 331 3106FT STRAND 336 339 3107FT STRAND 342 345 3108FT STRAND 352 356 3109FT TURN 362 364 3110FT HELIX 370 382 3111FT STRAND 387 389 3112FT HELIX 398 406 3113FT STRAND 409 413 3114FT STRAND 421 423 3115FT TURN 424 429 3116FT HELIX 431 433 3117FT HELIX 434 448 3118FT STRAND 454 458 3119FT HELIX 467 479 3120FT TURN 489 491 3121FT STRAND 492 494 3122FT STRAND 498 500 3123FT STRAND 514 516 3124FT HELIX 521 525 3125FT STRAND 534 540 3126FT HELIX 550 559 3127FT STRAND 563 569 3128FT STRAND 576 579 3129FT STRAND 585 588 3130FT TURN 590 593 3131FT HELIX 600 603 3132FT HELIX 617 624 3133FT STRAND 627 633 3134FT STRAND 636 641 3135FT STRAND 652 659 3136FT STRAND 662 670 3137FT STRAND 678 682 3138FT STRAND 690 703 3139FT STRAND 708 710 3140FT STRAND 714 726 3141FT STRAND 740 743 3142FT STRAND 745 752 3143FT STRAND 755 760 3144FT TURN 761 763 3145FT STRAND 765 771 3146FT STRAND 777 784 3147FT HELIX 791 794 3148FT HELIX 807 814 3149FT TURN 815 818 3150FT STRAND 820 830 3151FT STRAND 832 845 3152FT STRAND 848 860 3153FT STRAND 865 873 3154FT STRAND 881 890 3155FT STRAND 894 904 3156FT STRAND 915 922 3157FT HELIX 923 926 3158FT STRAND 939 947 3159FT STRAND 950 963 3160FT HELIX 965 970 3161FT HELIX 974 976 3162FT STRAND 981 991 3163FT STRAND 999 1001 3164FT HELIX 1006 1008 3165FT STRAND 1013 1022 3166SQ SEQUENCE 1024 AA; 116483 MW; 9D295EF4CEF90B08 CRC64; 3167 MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR 3168 FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP 3169 TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA 3170 GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV 3171 LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK 3172 LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH 3173 HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG 3174 MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD 3175 PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA 3176 HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 3177 QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD 3178 GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ 3179 WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP 3180 LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA 3181 HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG 3182 LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI 3183 SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV 3184 WCQK 3185// 3186ID CNR1A_TAKRU Reviewed; 468 AA. 3187AC Q98894; 3188DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 3189DT 01-FEB-1997, sequence version 1. 3190DT 16-MAY-2012, entry version 73. 3191DE RecName: Full=Cannabinoid receptor type 1A; 3192GN Name=cnr1a; Synonyms=cb1a; 3193OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3194OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3195OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3196OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3197OC Tetradontoidea; Tetraodontidae; Takifugu. 3198OX NCBI_TaxID=31033; 3199RN [1] 3200RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3201RC TISSUE=Testis; 3202RX MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406; 3203RA Yamaguchi F., Macrae A., Brenner S.; 3204RT "Molecular cloning of two cannabinoid type 1-like receptor genes from 3205RT the puffer fish Fugu rubripes."; 3206RL Genomics 35:603-605(1996). 3207CC -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential). 3208CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 3209CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 3210CC ----------------------------------------------------------------------- 3211CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3212CC Distributed under the Creative Commons Attribution-NoDerivs License 3213CC ----------------------------------------------------------------------- 3214DR EMBL; X94401; CAA64174.1; -; Genomic_DNA. 3215DR ProteinModelPortal; Q98894; -. 3216DR eggNOG; NOG148018; -. 3217DR InParanoid; Q98894; -. 3218DR OrthoDB; EOG41ZF9S; -. 3219DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 3220DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 3221DR GO; GO:0004949; F:cannabinoid receptor activity; IEA:InterPro. 3222DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 3223DR InterPro; IPR002230; Cnbnoid_rcpt. 3224DR InterPro; IPR000810; Cnoid_rcpt_1. 3225DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 3226DR PANTHER; PTHR22750:SF10; Cnoid_rcpt_1; 1. 3227DR Pfam; PF00001; 7tm_1; 1. 3228DR PIRSF; PIRSF037995; Cnoid_rcpt_1; 1. 3229DR PRINTS; PR00522; CANABINOID1R. 3230DR PRINTS; PR00362; CANNABINOIDR. 3231DR PRINTS; PR00237; GPCRRHODOPSN. 3232DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 3233DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 3234PE 3: Inferred from homology; 3235KW Cell membrane; Complete proteome; G-protein coupled receptor; 3236KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; 3237KW Transmembrane; Transmembrane helix. 3238FT CHAIN 1 468 Cannabinoid receptor type 1A. 3239FT /FTId=PRO_0000069320. 3240FT TOPO_DOM 1 115 Extracellular (Potential). 3241FT TRANSMEM 116 141 Helical; Name=1; (Potential). 3242FT TOPO_DOM 142 153 Cytoplasmic (Potential). 3243FT TRANSMEM 154 174 Helical; Name=2; (Potential). 3244FT TOPO_DOM 175 186 Extracellular (Potential). 3245FT TRANSMEM 187 211 Helical; Name=3; (Potential). 3246FT TOPO_DOM 212 231 Cytoplasmic (Potential). 3247FT TRANSMEM 232 254 Helical; Name=4; (Potential). 3248FT TOPO_DOM 255 272 Extracellular (Potential). 3249FT TRANSMEM 273 298 Helical; Name=5; (Potential). 3250FT TOPO_DOM 299 343 Cytoplasmic (Potential). 3251FT TRANSMEM 344 364 Helical; Name=6; (Potential). 3252FT TOPO_DOM 365 376 Extracellular (Potential). 3253FT TRANSMEM 377 398 Helical; Name=7; (Potential). 3254FT TOPO_DOM 399 468 Cytoplasmic (Potential). 3255FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). 3256FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential). 3257SQ SEQUENCE 468 AA; 52391 MW; B8628C1B043B42D7 CRC64; 3258 MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK 3259 VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV 3260 LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH 3261 KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW 3262 TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA 3263 HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA 3264 IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ 3265 LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV 3266// 3267ID CNR1B_TAKRU Reviewed; 470 AA. 3268AC Q98895; 3269DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 3270DT 01-FEB-1997, sequence version 1. 3271DT 16-MAY-2012, entry version 72. 3272DE RecName: Full=Cannabinoid receptor type 1B; 3273GN Name=cnr1b; Synonyms=cb1b; 3274OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3275OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3276OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3277OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3278OC Tetradontoidea; Tetraodontidae; Takifugu. 3279OX NCBI_TaxID=31033; 3280RN [1] 3281RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3282RC TISSUE=Testis; 3283RX MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406; 3284RA Yamaguchi F., Macrae A., Brenner S.; 3285RT "Molecular cloning of two cannabinoid type 1-like receptor genes from 3286RT the puffer fish Fugu rubripes."; 3287RL Genomics 35:603-605(1996). 3288CC -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential). 3289CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 3290CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 3291CC ----------------------------------------------------------------------- 3292CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3293CC Distributed under the Creative Commons Attribution-NoDerivs License 3294CC ----------------------------------------------------------------------- 3295DR EMBL; X94402; CAA64175.1; -; Genomic_DNA. 3296DR ProteinModelPortal; Q98895; -. 3297DR eggNOG; NOG308746; -. 3298DR InParanoid; Q98895; -. 3299DR OrthoDB; EOG4J3WH0; -. 3300DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 3301DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 3302DR GO; GO:0004949; F:cannabinoid receptor activity; IEA:InterPro. 3303DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 3304DR InterPro; IPR002230; Cnbnoid_rcpt. 3305DR InterPro; IPR000810; Cnoid_rcpt_1. 3306DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 3307DR PANTHER; PTHR22750:SF10; Cnoid_rcpt_1; 1. 3308DR Pfam; PF00001; 7tm_1; 1. 3309DR PIRSF; PIRSF037995; Cnoid_rcpt_1; 1. 3310DR PRINTS; PR00522; CANABINOID1R. 3311DR PRINTS; PR00362; CANNABINOIDR. 3312DR PRINTS; PR00237; GPCRRHODOPSN. 3313DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 3314DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 3315PE 3: Inferred from homology; 3316KW Cell membrane; Complete proteome; G-protein coupled receptor; 3317KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; 3318KW Transmembrane; Transmembrane helix. 3319FT CHAIN 1 470 Cannabinoid receptor type 1B. 3320FT /FTId=PRO_0000069321. 3321FT TOPO_DOM 1 113 Extracellular (Potential). 3322FT TRANSMEM 114 139 Helical; Name=1; (Potential). 3323FT TOPO_DOM 140 151 Cytoplasmic (Potential). 3324FT TRANSMEM 152 172 Helical; Name=2; (Potential). 3325FT TOPO_DOM 173 184 Extracellular (Potential). 3326FT TRANSMEM 185 209 Helical; Name=3; (Potential). 3327FT TOPO_DOM 210 229 Cytoplasmic (Potential). 3328FT TRANSMEM 230 252 Helical; Name=4; (Potential). 3329FT TOPO_DOM 253 270 Extracellular (Potential). 3330FT TRANSMEM 271 296 Helical; Name=5; (Potential). 3331FT TOPO_DOM 297 341 Cytoplasmic (Potential). 3332FT TRANSMEM 342 362 Helical; Name=6; (Potential). 3333FT TOPO_DOM 363 374 Extracellular (Potential). 3334FT TRANSMEM 375 396 Helical; Name=7; (Potential). 3335FT TOPO_DOM 397 470 Cytoplasmic (Potential). 3336FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). 3337FT CARBOHYD 86 86 N-linked (GlcNAc...) (Potential). 3338SQ SEQUENCE 470 AA; 52081 MW; CEE87CD37FDF9192 CRC64; 3339 MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI 3340 PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA 3341 ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK 3342 DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI 3343 SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH 3344 HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM 3345 VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD 3346 SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV 3347// 3348ID CO9_TAKRU Reviewed; 586 AA. 3349AC P79755; 3350DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 3351DT 01-MAY-1997, sequence version 1. 3352DT 16-MAY-2012, entry version 77. 3353DE RecName: Full=Complement component C9; 3354DE Flags: Precursor; 3355GN Name=c9; 3356OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3357OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3358OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3359OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3360OC Tetradontoidea; Tetraodontidae; Takifugu. 3361OX NCBI_TaxID=31033; 3362RN [1] 3363RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3364RX MEDLINE=98038993; PubMed=9373156; DOI=10.1016/S0378-1119(97)00423-X; 3365RA Yeo G.S.H., Elgar G., Sandford R., Brenner S.; 3366RT "Cloning and sequencing of complement component C9 and its linkage to 3367RT DOC-2 in the pufferfish Fugu rubripes."; 3368RL Gene 200:203-211(1997). 3369CC -!- FUNCTION: C9 is the final component of the complement system to be 3370CC added in the assembly of the membrane attack complex. It is able 3371CC to enter lipid bilayers, forming transmembrane channels (By 3372CC similarity). 3373CC -!- SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane 3374CC protein (By similarity). Note=Secreted as soluble monomer. 3375CC Oligomerizes at target membranes, forming a pre-pore. A 3376CC conformation change then leads to the formation of a pore (By 3377CC similarity). 3378CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family. 3379CC -!- SIMILARITY: Contains 1 EGF-like domain. 3380CC -!- SIMILARITY: Contains 1 LDL-receptor class A domain. 3381CC -!- SIMILARITY: Contains 1 MACPF domain. 3382CC -!- SIMILARITY: Contains 2 TSP type-1 domains. 3383CC ----------------------------------------------------------------------- 3384CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3385CC Distributed under the Creative Commons Attribution-NoDerivs License 3386CC ----------------------------------------------------------------------- 3387DR EMBL; U87241; AAC60288.1; -; Genomic_DNA. 3388DR ProteinModelPortal; P79755; -. 3389DR TCDB; 1.C.39.1.2; membrane attack complex/perforin (MACPF) family. 3390DR eggNOG; NOG46204; -. 3391DR InParanoid; P79755; -. 3392DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 3393DR GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW. 3394DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW. 3395DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW. 3396DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. 3397DR Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1. 3398DR InterPro; IPR023415; LDLR_class-A_CS. 3399DR InterPro; IPR002172; LDrepeatLR_classA_rpt. 3400DR InterPro; IPR001862; MAC_perforin. 3401DR InterPro; IPR020864; MACPF. 3402DR InterPro; IPR020863; MACPF_CS. 3403DR InterPro; IPR000884; Thrombospondin_1_rpt. 3404DR Pfam; PF00057; Ldl_recept_a; 1. 3405DR Pfam; PF01823; MACPF; 1. 3406DR PRINTS; PR00764; COMPLEMENTC9. 3407DR SMART; SM00192; LDLa; 1. 3408DR SMART; SM00209; TSP1; 1. 3409DR SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 1. 3410DR SUPFAM; SSF82895; TSP1; 2. 3411DR PROSITE; PS00022; EGF_1; 1. 3412DR PROSITE; PS01186; EGF_2; FALSE_NEG. 3413DR PROSITE; PS50026; EGF_3; FALSE_NEG. 3414DR PROSITE; PS01209; LDLRA_1; 1. 3415DR PROSITE; PS50068; LDLRA_2; 1. 3416DR PROSITE; PS00279; MACPF_1; 1. 3417DR PROSITE; PS51412; MACPF_2; 1. 3418DR PROSITE; PS50092; TSP1; 2. 3419PE 3: Inferred from homology; 3420KW Cell membrane; Complement alternate pathway; Complement pathway; 3421KW Complete proteome; Cytolysis; Disulfide bond; EGF-like domain; 3422KW Glycoprotein; Immunity; Innate immunity; Membrane; 3423KW Membrane attack complex; Reference proteome; Repeat; Secreted; Signal; 3424KW Transmembrane; Transmembrane beta strand. 3425FT SIGNAL 1 26 Potential. 3426FT CHAIN 27 586 Complement component C9. 3427FT /FTId=PRO_0000023608. 3428FT DOMAIN 36 89 TSP type-1 1. 3429FT DOMAIN 94 131 LDL-receptor class A. 3430FT DOMAIN 132 493 MACPF. 3431FT DOMAIN 494 524 EGF-like. 3432FT DOMAIN 543 585 TSP type-1 2. 3433FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). 3434FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential). 3435FT CARBOHYD 354 354 N-linked (GlcNAc...) (Potential). 3436FT CARBOHYD 545 545 N-linked (GlcNAc...) (Potential). 3437FT DISULFID 37 72 By similarity. 3438FT DISULFID 48 51 By similarity. 3439FT DISULFID 82 88 By similarity. 3440FT DISULFID 96 108 By similarity. 3441FT DISULFID 103 121 By similarity. 3442FT DISULFID 115 129 By similarity. 3443FT DISULFID 136 175 By similarity. 3444FT DISULFID 363 389 By similarity. 3445FT DISULFID 494 510 By similarity. 3446FT DISULFID 497 512 By similarity. 3447FT DISULFID 514 523 By similarity. 3448SQ SEQUENCE 586 AA; 65198 MW; 8466EB7B8B8FDC18 CRC64; 3449 MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG 3450 VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD 3451 CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN 3452 PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST 3453 EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD 3454 EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI 3455 QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES 3456 AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ 3457 ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV 3458 TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC 3459// 3460ID DRD1L_TAKRU Reviewed; 459 AA. 3461AC P53452; 3462DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 3463DT 01-OCT-1996, sequence version 1. 3464DT 16-MAY-2012, entry version 70. 3465DE RecName: Full=D(1)-like dopamine receptor; 3466GN Name=d14; 3467OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3468OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3469OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3470OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3471OC Tetradontoidea; Tetraodontidae; Takifugu. 3472OX NCBI_TaxID=31033; 3473RN [1] 3474RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3475RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; 3476RA Machae A.D., Brenner S.; 3477RT "Analysis of the dopamine receptor family in the compact genome of the 3478RT puffer fish Fugu rubripes."; 3479RL Genomics 25:436-446(1995). 3480CC -!- FUNCTION: Receptor for dopamine. 3481CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 3482CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 3483CC ----------------------------------------------------------------------- 3484CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3485CC Distributed under the Creative Commons Attribution-NoDerivs License 3486CC ----------------------------------------------------------------------- 3487DR EMBL; X80174; CAA56455.1; -; Genomic_DNA. 3488DR PIR; A56849; A56849. 3489DR ProteinModelPortal; P53452; -. 3490DR eggNOG; NOG262978; -. 3491DR InParanoid; P53452; -. 3492DR OrthoDB; EOG4BG8W3; -. 3493DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 3494DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 3495DR GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro. 3496DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 3497DR InterPro; IPR001413; Dopa_1A_rcpt. 3498DR InterPro; IPR000929; Dopamine_rcpt. 3499DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 3500DR Pfam; PF00001; 7tm_1; 1. 3501DR PRINTS; PR00565; DOPAMINED1AR. 3502DR PRINTS; PR00242; DOPAMINER. 3503DR PRINTS; PR00237; GPCRRHODOPSN. 3504DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 3505DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 3506PE 3: Inferred from homology; 3507KW Cell membrane; Complete proteome; Disulfide bond; 3508KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; 3509KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. 3510FT CHAIN 1 459 D(1)-like dopamine receptor. 3511FT /FTId=PRO_0000069382. 3512FT TOPO_DOM 1 23 Extracellular (Potential). 3513FT TRANSMEM 24 49 Helical; Name=1; (Potential). 3514FT TOPO_DOM 50 60 Cytoplasmic (Potential). 3515FT TRANSMEM 61 87 Helical; Name=2; (Potential). 3516FT TOPO_DOM 88 96 Extracellular (Potential). 3517FT TRANSMEM 97 119 Helical; Name=3; (Potential). 3518FT TOPO_DOM 120 138 Cytoplasmic (Potential). 3519FT TRANSMEM 139 164 Helical; Name=4; (Potential). 3520FT TOPO_DOM 165 191 Extracellular (Potential). 3521FT TRANSMEM 192 216 Helical; Name=5; (Potential). 3522FT TOPO_DOM 217 269 Cytoplasmic (Potential). 3523FT TRANSMEM 270 297 Helical; Name=6; (Potential). 3524FT TOPO_DOM 298 311 Extracellular (Potential). 3525FT TRANSMEM 312 333 Helical; Name=7; (Potential). 3526FT TOPO_DOM 334 459 Cytoplasmic (Potential). 3527FT CARBOHYD 4 4 N-linked (GlcNAc...) (Potential). 3528FT DISULFID 96 187 By similarity. 3529SQ SEQUENCE 459 AA; 51080 MW; B69857A3A4E4E10B CRC64; 3530 MAQNFSTVGD GKQMLLERDS SKRVLTGCFL SLLIFTTLLG NTLVCVAVTK FRHLRSKVTN 3531 FFVISLAISD LLVAILVMPW KAATEIMGFW PFGEFCNIWV AFDIMCSTAS ILNLCVISVD 3532 RYWAISSPFR YERKMTPKVA CLMISVAWTL SVLISFIPVQ LNWHKAQTAS YVELNGTYAG 3533 DLPPDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQKQIRRIS ALERAAESAQ 3534 NRHSSMGNSL SMESECSFKM SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCEADD 3535 TTDFPCISST TFDVFVWFGW ANSSLNPIIY AFNADFRKAF SILLGCHRLC PGNSAIEIVS 3536 INNTGAPLSN PSCQYQPKSH IPKEGNHSSS YVIPHSILCQ EEELQKKDGF GGEMEVGLVN 3537 NAMEKVSPAI SGNFDSDAAV TLETINPITQ NGQHKSMSC 3538// 3539ID DRD2L_TAKRU Reviewed; 463 AA. 3540AC P53453; 3541DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 3542DT 01-OCT-1996, sequence version 1. 3543DT 16-MAY-2012, entry version 68. 3544DE RecName: Full=D(2)-like dopamine receptor; 3545GN Name=d215; 3546OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3547OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3548OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3549OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3550OC Tetradontoidea; Tetraodontidae; Takifugu. 3551OX NCBI_TaxID=31033; 3552RN [1] 3553RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3554RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; 3555RA Machae A.D., Brenner S.; 3556RT "Analysis of the dopamine receptor family in the compact genome of the 3557RT puffer fish Fugu rubripes."; 3558RL Genomics 25:436-446(1995). 3559CC -!- FUNCTION: Receptor for dopamine. 3560CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 3561CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 3562CC ----------------------------------------------------------------------- 3563CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3564CC Distributed under the Creative Commons Attribution-NoDerivs License 3565CC ----------------------------------------------------------------------- 3566DR EMBL; X80175; CAA56456.1; -; Genomic_DNA. 3567DR ProteinModelPortal; P53453; -. 3568DR eggNOG; NOG309657; -. 3569DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 3570DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 3571DR GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro. 3572DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 3573DR InterPro; IPR001922; Dopa_D2_rcpt. 3574DR InterPro; IPR000929; Dopamine_rcpt. 3575DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 3576DR Pfam; PF00001; 7tm_1; 1. 3577DR PRINTS; PR00567; DOPAMINED2R. 3578DR PRINTS; PR00242; DOPAMINER. 3579DR PRINTS; PR00237; GPCRRHODOPSN. 3580DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 3581DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 3582PE 3: Inferred from homology; 3583KW Cell membrane; Complete proteome; Disulfide bond; 3584KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; 3585KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. 3586FT CHAIN 1 463 D(2)-like dopamine receptor. 3587FT /FTId=PRO_0000069392. 3588FT TOPO_DOM 1 35 Extracellular (By similarity). 3589FT TRANSMEM 36 58 Helical; Name=1; (By similarity). 3590FT TOPO_DOM 59 68 Cytoplasmic (By similarity). 3591FT TRANSMEM 69 91 Helical; Name=2; (By similarity). 3592FT TOPO_DOM 92 106 Extracellular (By similarity). 3593FT TRANSMEM 107 128 Helical; Name=3; (By similarity). 3594FT TOPO_DOM 129 149 Cytoplasmic (By similarity). 3595FT TRANSMEM 150 170 Helical; Name=4; (By similarity). 3596FT TOPO_DOM 171 189 Extracellular (By similarity). 3597FT TRANSMEM 190 214 Helical; Name=5; (By similarity). 3598FT TOPO_DOM 215 392 Cytoplasmic (By similarity). 3599FT TRANSMEM 393 414 Helical; Name=6; (By similarity). 3600FT TOPO_DOM 415 429 Extracellular (By similarity). 3601FT TRANSMEM 430 451 Helical; Name=7; (By similarity). 3602FT TOPO_DOM 452 463 Cytoplasmic (By similarity). 3603FT REGION 191 198 Agonist binding (By similarity). 3604FT REGION 405 413 Agonist binding (By similarity). 3605FT BINDING 112 112 Agonist (By similarity). 3606FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). 3607FT CARBOHYD 16 16 N-linked (GlcNAc...) (Potential). 3608FT CARBOHYD 22 22 N-linked (GlcNAc...) (Potential). 3609FT DISULFID 105 183 By similarity. 3610FT DISULFID 418 421 By similarity. 3611SQ SEQUENCE 463 AA; 52120 MW; A54B178D7718AF6B CRC64; 3612 MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE 3613 KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI 3614 LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ 3615 SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI 3616 PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK 3617 QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA 3618 PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR 3619 CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC 3620// 3621ID DRD5L_TAKRU Reviewed; 463 AA. 3622AC P53454; 3623DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 3624DT 01-OCT-1996, sequence version 1. 3625DT 16-MAY-2012, entry version 70. 3626DE RecName: Full=D(5)-like dopamine receptor; 3627GN Name=dl; 3628OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3629OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3630OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3631OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3632OC Tetradontoidea; Tetraodontidae; Takifugu. 3633OX NCBI_TaxID=31033; 3634RN [1] 3635RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3636RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; 3637RA Machae A.D., Brenner S.; 3638RT "Analysis of the dopamine receptor family in the compact genome of the 3639RT puffer fish Fugu rubripes."; 3640RL Genomics 25:436-446(1995). 3641CC -!- FUNCTION: Receptor for dopamine. 3642CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 3643CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 3644CC ----------------------------------------------------------------------- 3645CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3646CC Distributed under the Creative Commons Attribution-NoDerivs License 3647CC ----------------------------------------------------------------------- 3648DR EMBL; X80177; CAA56457.1; -; Genomic_DNA. 3649DR PIR; B56849; B56849. 3650DR ProteinModelPortal; P53454; -. 3651DR eggNOG; NOG262978; -. 3652DR InParanoid; P53454; -. 3653DR OrthoDB; EOG4PVNZH; -. 3654DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 3655DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 3656DR GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro. 3657DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 3658DR InterPro; IPR000929; Dopamine_rcpt. 3659DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 3660DR Pfam; PF00001; 7tm_1; 1. 3661DR PRINTS; PR00242; DOPAMINER. 3662DR PRINTS; PR00237; GPCRRHODOPSN. 3663DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 3664DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 3665PE 3: Inferred from homology; 3666KW Cell membrane; Complete proteome; Disulfide bond; 3667KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; 3668KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. 3669FT CHAIN 1 463 D(5)-like dopamine receptor. 3670FT /FTId=PRO_0000069409. 3671FT TOPO_DOM 1 39 Extracellular (Potential). 3672FT TRANSMEM 40 65 Helical; Name=1; (Potential). 3673FT TOPO_DOM 66 76 Cytoplasmic (Potential). 3674FT TRANSMEM 77 103 Helical; Name=2; (Potential). 3675FT TOPO_DOM 104 112 Extracellular (Potential). 3676FT TRANSMEM 113 135 Helical; Name=3; (Potential). 3677FT TOPO_DOM 136 154 Cytoplasmic (Potential). 3678FT TRANSMEM 155 180 Helical; Name=4; (Potential). 3679FT TOPO_DOM 181 198 Extracellular (Potential). 3680FT TRANSMEM 199 223 Helical; Name=5; (Potential). 3681FT TOPO_DOM 224 273 Cytoplasmic (Potential). 3682FT TRANSMEM 274 301 Helical; Name=6; (Potential). 3683FT TOPO_DOM 302 315 Extracellular (Potential). 3684FT TRANSMEM 316 337 Helical; Name=7; (Potential). 3685FT TOPO_DOM 338 463 Cytoplasmic (Potential). 3686FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). 3687FT DISULFID 112 194 By similarity. 3688SQ SEQUENCE 463 AA; 51096 MW; 7FD627F69A699F6B CRC64; 3689 MENFYNETEP TEPRGGVDPL RVVTAAEDVP APVGGVSVRA LTGCVLCALI VSTLLGNTLV 3690 CAAVIKFRHL RSKVTNAFVV SLAVSDLFVA VLVMPWRAVS EVAGVWLFGR FCDTWVAFDI 3691 MCSTASILNL CVISMDRYWA ISNPFRYERR MTRRFAFLMI AVAWTLSVLI SFIPVQLNWH 3692 RADNNSSAHE QGDCNASLNR TYAISSSLIS FYIPVLIMVG TYTRIFRIAQ TQIRRISSLE 3693 RAAGQRAQNQ SHRASTHDES ALKTSFKRET KVLKTLSVIM GVFVFCWLPF FVLNCVVPFC 3694 DVDKVGEPPC VSDTTFNIFV WFGWANSSLN PVIYAFNADF RKAFTTILGC SKFCSSSAVQ 3695 AVDFSNELVS YHHDTTLQKE PVPGPGAHRL VAPLPQNRGD AGPNFDKVSV VSDDSRADRN 3696 LLLPAILQCD CEAEISLDMV PFGSSGPADS FLIPGQIQDL GDL 3697// 3698ID EI2BB_TAKRU Reviewed; 355 AA. 3699AC Q90511; 3700DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. 3701DT 01-NOV-1996, sequence version 1. 3702DT 16-MAY-2012, entry version 58. 3703DE RecName: Full=Translation initiation factor eIF-2B subunit beta; 3704DE AltName: Full=S20I15; 3705DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta; 3706GN Name=eif2b2; Synonyms=eif2bb; 3707OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3708OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3709OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3710OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3711OC Tetradontoidea; Tetraodontidae; Takifugu. 3712OX NCBI_TaxID=31033; 3713RN [1] 3714RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3715RX MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366; 3716RA Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., 3717RA Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., 3718RA Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.; 3719RT "Conservation of synteny between the genome of the pufferfish (Fugu 3720RT rubripes) and the region on human chromosome 14 (14q24.3) associated 3721RT with familial Alzheimer disease (AD3 locus)."; 3722RL Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996). 3723CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 3724CC 2-bound GDP for GTP (By similarity). 3725CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, 3726CC delta and epsilon (By similarity). 3727CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits 3728CC family. 3729CC ----------------------------------------------------------------------- 3730CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3731CC Distributed under the Creative Commons Attribution-NoDerivs License 3732CC ----------------------------------------------------------------------- 3733DR EMBL; U40756; AAC59777.1; -; Genomic_DNA. 3734DR ProteinModelPortal; Q90511; -. 3735DR STRING; Q90511; -. 3736DR Ensembl; ENSTRUT00000027526; ENSTRUP00000027417; ENSTRUG00000010849. 3737DR eggNOG; COG1184; -. 3738DR GeneTree; ENSGT00550000074908; -. 3739DR InParanoid; Q90511; -. 3740DR OMA; RRSSEDM; -. 3741DR OrthoDB; EOG4JT05R; -. 3742DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB. 3743DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. 3744DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. 3745DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:RefGenome. 3746DR GO; GO:0003743; F:translation initiation factor activity; ISS:RefGenome. 3747DR GO; GO:0051716; P:cellular response to stimulus; ISS:UniProtKB. 3748DR GO; GO:0042552; P:myelination; ISS:UniProtKB. 3749DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB. 3750DR GO; GO:0006446; P:regulation of translational initiation; ISS:RefGenome. 3751DR InterPro; IPR000649; IF-2B-related. 3752DR PANTHER; PTHR10233; IF-2B_related; 1. 3753DR Pfam; PF01008; IF-2B; 1. 3754PE 3: Inferred from homology; 3755KW Complete proteome; Initiation factor; Protein biosynthesis; 3756KW Reference proteome. 3757FT CHAIN 1 355 Translation initiation factor eIF-2B 3758FT subunit beta. 3759FT /FTId=PRO_0000156065. 3760SQ SEQUENCE 355 AA; 39130 MW; 4375743877F6B132 CRC64; 3761 MPGADKEVDL TERIEAFLSD LKRGGSGTGP LRGSSETARE TTALLRRITA QARWSSAGDL 3762 MEIIRKEGRR LIAAQPSETT VGNMIRRVLK IIREEYARSR GSSEEADQQE SLHKLLTSGG 3763 LSEENFRQHF AALRANVIEA INELLTELEG TTDNIAMQAL EHIHSNEVIM TVGRSRTVEA 3764 FLKDAARKRK FHVIVAECAP FCQGHKMATS LSTAGIETTV IADAAIFAVM SRVNKVIIGT 3765 QTVLANGGLR AVNGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDTFH KFVSPHEVLP 3766 FTEGEILSKV NVHCPVFDYV PPELITLFIS NIGGHAPSYI YRLMSELYHP EDHEL 3767// 3768ID EM55_TAKRU Reviewed; 467 AA. 3769AC P49697; 3770DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. 3771DT 01-FEB-1996, sequence version 1. 3772DT 16-MAY-2012, entry version 75. 3773DE RecName: Full=55 kDa erythrocyte membrane protein; 3774DE Short=p55; 3775DE AltName: Full=Membrane protein, palmitoylated 1; 3776GN Name=mpp1; 3777OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 3778OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 3779OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 3780OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 3781OC Tetradontoidea; Tetraodontidae; Takifugu. 3782OX NCBI_TaxID=31033; 3783RN [1] 3784RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3785RC TISSUE=Testis; 3786RX MEDLINE=96047329; PubMed=7558025; DOI=10.1006/geno.1995.1075; 3787RA Elgar G.S., Rattray F.M., Greystrong J.S., Brenner S.; 3788RT "Genomic structure and nucleotide sequence of the p55 gene of the 3789RT puffer fish Fugu rubripes."; 3790RL Genomics 27:442-446(1995). 3791CC -!- FUNCTION: May play a role in the regulation of neutrophil 3792CC polarization (By similarity). 3793CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By 3794CC similarity). 3795CC -!- PTM: Extensively palmitoylated (By similarity). 3796CC -!- SIMILARITY: Belongs to the MAGUK family. 3797CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. 3798CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. 3799CC -!- SIMILARITY: Contains 1 SH3 domain. 3800CC ----------------------------------------------------------------------- 3801CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3802CC Distributed under the Creative Commons Attribution-NoDerivs License 3803CC ----------------------------------------------------------------------- 3804DR EMBL; X81359; CAA57127.1; -; Genomic_DNA. 3805DR PIR; A57627; A57627. 3806DR ProteinModelPortal; P49697; -. 3807DR SMR; P49697; 71-155. 3808DR eggNOG; COG0194; -. 3809DR InParanoid; P49697; -. 3810DR OrthoDB; EOG46HG9K; -. 3811DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 3812DR InterPro; IPR008144; Guanylate_kin. 3813DR InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel. 3814DR InterPro; IPR020590; Guanylate_kinase_CS. 3815DR InterPro; IPR001478; PDZ. 3816DR InterPro; IPR011511; SH3_2. 3817DR InterPro; IPR001452; SH3_domain. 3818DR Pfam; PF00625; Guanylate_kin; 1. 3819DR Pfam; PF00595; PDZ; 1. 3820DR Pfam; PF07653; SH3_2; 1. 3821DR SMART; SM00072; GuKc; 1. 3822DR SMART; SM00228; PDZ; 1. 3823DR SMART; SM00326; SH3; 1. 3824DR SUPFAM; SSF50156; PDZ; 1. 3825DR SUPFAM; SSF50044; SH3; 1. 3826DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. 3827DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. 3828DR PROSITE; PS50106; PDZ; 1. 3829DR PROSITE; PS50002; SH3; 1. 3830PE 3: Inferred from homology; 3831KW Complete proteome; Lipoprotein; Membrane; Palmitate; 3832KW Reference proteome; SH3 domain. 3833FT CHAIN 1 467 55 kDa erythrocyte membrane protein. 3834FT /FTId=PRO_0000094567. 3835FT DOMAIN 73 154 PDZ. 3836FT DOMAIN 160 230 SH3. 3837FT DOMAIN 283 452 Guanylate kinase-like. 3838SQ SEQUENCE 467 AA; 52609 MW; 48BA1CE3ED524EDC CRC64; 3839 MTLKSNKNEP ALILDSVTSV RTALSDLYLE QLLQNKPTDK QAAMQTYENK GAEVFSNGSA 3840 GHINGAELSR MREVAFEKNQ SEPLGVTLKL NDKQRCSVAR ILHGGMIHRQ GSLHEGDEIA 3841 EINGKSVANQ TVDQLQKILK ETNGVVTMKI IPRPQSRSKP CEMYMRGQFD YDPAMDDLIP 3842 CKEAGLKFQT GDIIQIINKQ DPNWWQGRVE NNAANFAGLI PSPELQEWRA ASKSKAREGS 3843 QSCSPFGKKK KCKDKYLAKH SSIFDQLDVI SYEEVVRLPA FKRKTLVLIG APGVGRRHIK 3844 NVLLTKYPEK FSYPVPHTTR PQRKGDANGE EYFFISNEAM TKCISANELL EYGSFQGYMF 3845 GTITETIQKI HEQDKIALLD VEPQTMKVLR TADFGPLMVF IAPTDTAAQT ENLQMIQKES 3846 ETILNTYRQY FDVVLVNNDV NESVKIVEEA LEHATTTPQW VPVSWVY 3847// 3848ID FLAV_ANASO Reviewed; 170 AA. 3849AC P0A3E0; P11241; 3850DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. 3851DT 23-JAN-2007, sequence version 2. 3852DT 18-APR-2012, entry version 40. 3853DE RecName: Full=Flavodoxin; 3854GN Name=isiB; 3855OS Anabaena sp. (strain PCC 7119). 3856OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. 3857OX NCBI_TaxID=1168; 3858RN [1] 3859RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3860RX MEDLINE=92074973; PubMed=1720613; 3861RA Fillat M.F., Borrias W.E., Weisbeek P.J.; 3862RT "Isolation and overexpression in Escherichia coli of the flavodoxin 3863RT gene from Anabaena PCC 7119."; 3864RL Biochem. J. 280:187-191(1991). 3865RN [2] 3866RP PROTEIN SEQUENCE OF 2-37. 3867RX MEDLINE=90381288; PubMed=2119231; DOI=10.1016/0167-4838(90)90091-S; 3868RA Fillat M.F., Edmondson D.E., Gomez-Moreno C.; 3869RT "Structural and chemical properties of a flavodoxin from Anabaena PCC 3870RT 7119."; 3871RL Biochim. Biophys. Acta 1040:301-307(1990). 3872RN [3] 3873RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). 3874RX MEDLINE=99318886; PubMed=10388575; DOI=10.1006/jmbi.1999.2863; 3875RA Fernandez-Recio J., Romero A., Sancho J.; 3876RT "Energetics of a hydrogen bond (charged and neutral) and of a cation- 3877RT pi interaction in apoflavodoxin."; 3878RL J. Mol. Biol. 290:319-330(1999). 3879CC -!- FUNCTION: Low-potential electron donor to a number of redox 3880CC enzymes. 3881CC -!- COFACTOR: FMN. 3882CC -!- INTERACTION: 3883CC P08165:FDXR (xeno); NbExp=3; IntAct=EBI-593907, EBI-593948; 3884CC P21890:petH; NbExp=5; IntAct=EBI-593907, EBI-593915; 3885CC -!- SIMILARITY: Belongs to the flavodoxin family. 3886CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 3887CC ----------------------------------------------------------------------- 3888CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 3889CC Distributed under the Creative Commons Attribution-NoDerivs License 3890CC ----------------------------------------------------------------------- 3891DR EMBL; S68006; AAB20462.1; -; Genomic_DNA. 3892DR PDB; 1DX9; X-ray; 2.05 A; A/B/C/D=2-170. 3893DR PDB; 1FTG; X-ray; 2.00 A; A=3-169. 3894DR PDB; 1OBO; X-ray; 1.20 A; A/B=3-170. 3895DR PDB; 1OBV; X-ray; 2.10 A; A=3-170. 3896DR PDB; 1QHE; X-ray; 2.00 A; A=3-170. 3897DR PDB; 2KQU; NMR; -; A=3-170. 3898DR PDB; 2V5U; X-ray; 1.99 A; A/B=3-169. 3899DR PDB; 2V5V; X-ray; 1.88 A; A/B=3-170. 3900DR PDB; 3ESX; X-ray; 2.31 A; A/B=2-170. 3901DR PDB; 3ESY; X-ray; 2.39 A; A/B/C/D=2-170. 3902DR PDB; 3ESZ; X-ray; 1.94 A; A/B=5-170. 3903DR PDBsum; 1DX9; -. 3904DR PDBsum; 1FTG; -. 3905DR PDBsum; 1OBO; -. 3906DR PDBsum; 1OBV; -. 3907DR PDBsum; 1QHE; -. 3908DR PDBsum; 2KQU; -. 3909DR PDBsum; 2V5U; -. 3910DR PDBsum; 2V5V; -. 3911DR PDBsum; 3ESX; -. 3912DR PDBsum; 3ESY; -. 3913DR PDBsum; 3ESZ; -. 3914DR ProteinModelPortal; P0A3E0; -. 3915DR SMR; P0A3E0; 2-170. 3916DR IntAct; P0A3E0; 3. 3917DR EvolutionaryTrace; P0A3E0; -. 3918DR GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB. 3919DR GO; GO:0010181; F:FMN binding; TAS:UniProtKB. 3920DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 3921DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. 3922DR GO; GO:0010106; P:cellular response to iron ion starvation; TAS:UniProtKB. 3923DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 3924DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 3925DR InterPro; IPR008254; Flavodoxin/NO_synth. 3926DR InterPro; IPR001226; Flavodoxin_CS. 3927DR InterPro; IPR010086; Flavodoxin_lc. 3928DR Pfam; PF00258; Flavodoxin_1; 1. 3929DR TIGRFAMs; TIGR01752; Flav_long; 1. 3930DR PROSITE; PS00201; FLAVODOXIN; 1. 3931DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 3932PE 1: Evidence at protein level; 3933KW 3D-structure; Direct protein sequencing; Electron transport; 3934KW Flavoprotein; FMN; Transport. 3935FT INIT_MET 1 1 Removed. 3936FT CHAIN 2 170 Flavodoxin. 3937FT /FTId=PRO_0000171600. 3938FT DOMAIN 5 165 Flavodoxin-like. 3939FT STRAND 4 9 3940FT STRAND 12 14 3941FT HELIX 15 27 3942FT TURN 29 31 3943FT STRAND 32 36 3944FT TURN 37 39 3945FT HELIX 42 47 3946FT STRAND 49 58 3947FT TURN 59 61 3948FT HELIX 65 71 3949FT HELIX 72 76 3950FT STRAND 83 89 3951FT TURN 92 97 3952FT HELIX 101 112 3953FT STRAND 138 144 3954FT TURN 146 148 3955FT HELIX 150 152 3956FT HELIX 153 168 3957SQ SEQUENCE 170 AA; 18964 MW; 069E8DEBA9E33302 CRC64; 3958 MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI 3959 GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY 3960 WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL 3961// 3962ID FLAV_NOSS1 Reviewed; 170 AA. 3963AC P0A3D9; P11241; 3964DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. 3965DT 23-JAN-2007, sequence version 2. 3966DT 16-MAY-2012, entry version 55. 3967DE RecName: Full=Flavodoxin; 3968GN Name=isiB; OrderedLocusNames=alr2405; 3969OS Nostoc sp. (strain PCC 7120 / UTEX 2576). 3970OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. 3971OX NCBI_TaxID=103690; 3972RN [1] 3973RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 3974RX MEDLINE=89296496; PubMed=2500643; DOI=10.1093/nar/17.11.4384; 3975RA Leonhardt K.G., Straus N.A.; 3976RT "Sequence of the flavodoxin gene from Anabaena variabilis 7120."; 3977RL Nucleic Acids Res. 17:4384-4384(1989). 3978RN [2] 3979RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 3980RC STRAIN=PCC 7120 / UTEX 2576; 3981RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205; 3982RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., 3983RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., 3984RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., 3985RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., 3986RA Yasuda M., Tabata S.; 3987RT "Complete genomic sequence of the filamentous nitrogen-fixing 3988RT cyanobacterium Anabaena sp. strain PCC 7120."; 3989RL DNA Res. 8:205-213(2001). 3990RN [3] 3991RP STRUCTURE BY NMR. 3992RX MEDLINE=91104858; PubMed=2125478; DOI=10.1021/bi00493a014; 3993RA Stockman B.J., Krezel A.M., Markley J.L., Leonhardt K.G., Straus N.A.; 3994RT "Hydrogen-1, carbon-13, and nitrogen-15 NMR spectroscopy of Anabaena 3995RT 7120 flavodoxin: assignment of beta-sheet and flavin binding site 3996RT resonances and analysis of protein-flavin interactions."; 3997RL Biochemistry 29:9600-9609(1990). 3998RN [4] 3999RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). 4000RX MEDLINE=93271891; PubMed=1303762; 4001RA Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J., 4002RA Markley J.L., Sundaralingam M.; 4003RT "Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 4004RT 2-A resolution."; 4005RL Protein Sci. 1:1413-1427(1992). 4006RN [5] 4007RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). 4008RX PubMed=15299298; DOI=10.1107/S0907444994011716; 4009RA Burkhart B.M., Ramakrishnan B., Yan H., Reedstrom R.J., Markley J.L., 4010RA Straus N.A., Sundaralingam M.; 4011RT "Structure of the trigonal form of recombinant oxidized flavodoxin 4012RT from Anabaena 7120 at 1.40-A resolution."; 4013RL Acta Crystallogr. D 51:318-330(1995). 4014CC -!- FUNCTION: Low-potential electron donor to a number of redox 4015CC enzymes. 4016CC -!- COFACTOR: FMN. 4017CC -!- SIMILARITY: Belongs to the flavodoxin family. 4018CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4019CC ----------------------------------------------------------------------- 4020CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4021CC Distributed under the Creative Commons Attribution-NoDerivs License 4022CC ----------------------------------------------------------------------- 4023DR EMBL; X14577; CAA32720.1; -; Genomic_DNA. 4024DR EMBL; BA000019; BAB74104.1; -; Genomic_DNA. 4025DR PIR; AF2106; AF2106. 4026DR RefSeq; NP_486445.1; NC_003272.1. 4027DR PDB; 1FLV; X-ray; 2.00 A; A=2-170. 4028DR PDB; 1RCF; X-ray; 1.40 A; A=2-170. 4029DR PDBsum; 1FLV; -. 4030DR PDBsum; 1RCF; -. 4031DR ProteinModelPortal; P0A3D9; -. 4032DR SMR; P0A3D9; 2-170. 4033DR STRING; P0A3D9; -. 4034DR GeneID; 1106002; -. 4035DR GenomeReviews; BA000019_GR; alr2405. 4036DR KEGG; ana:alr2405; -. 4037DR PATRIC; 22774998; VBINosSp37423_2965. 4038DR eggNOG; COG0716; -. 4039DR HOGENOM; HOG000030543; -. 4040DR KO; K03839; -. 4041DR OMA; DDKHFVG; -. 4042DR ProtClustDB; PRK09267; -. 4043DR BioCyc; NSP103690:ALR2405-MONOMER; -. 4044DR EvolutionaryTrace; P0A3D9; -. 4045DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4046DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4047DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4048DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4049DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4050DR InterPro; IPR008254; Flavodoxin/NO_synth. 4051DR InterPro; IPR001226; Flavodoxin_CS. 4052DR InterPro; IPR010086; Flavodoxin_lc. 4053DR Pfam; PF00258; Flavodoxin_1; 1. 4054DR TIGRFAMs; TIGR01752; Flav_long; 1. 4055DR PROSITE; PS00201; FLAVODOXIN; 1. 4056DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4057PE 1: Evidence at protein level; 4058KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; 4059KW FMN; Transport. 4060FT INIT_MET 1 1 Removed (By similarity). 4061FT CHAIN 2 170 Flavodoxin. 4062FT /FTId=PRO_0000171601. 4063FT DOMAIN 5 165 Flavodoxin-like. 4064FT STRAND 5 9 4065FT STRAND 12 14 4066FT HELIX 15 26 4067FT TURN 27 29 4068FT STRAND 32 36 4069FT HELIX 42 47 4070FT STRAND 49 54 4071FT TURN 59 61 4072FT HELIX 65 71 4073FT HELIX 72 76 4074FT STRAND 83 89 4075FT TURN 92 97 4076FT HELIX 101 112 4077FT STRAND 138 144 4078FT TURN 146 148 4079FT HELIX 150 152 4080FT HELIX 153 167 4081SQ SEQUENCE 170 AA; 18964 MW; 069E8DEBA9E33302 CRC64; 4082 MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI 4083 GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY 4084 WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL 4085// 4086ID FLAV_AQUAE Reviewed; 185 AA. 4087AC O67866; 4088DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. 4089DT 01-AUG-1998, sequence version 1. 4090DT 16-MAY-2012, entry version 71. 4091DE RecName: Full=Flavodoxin; 4092GN Name=fldA; Synonyms=floX; OrderedLocusNames=aq_2096; 4093OS Aquifex aeolicus (strain VF5). 4094OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. 4095OX NCBI_TaxID=224324; 4096RN [1] 4097RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 4098RC STRAIN=VF5; 4099RX MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831; 4100RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., 4101RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., 4102RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; 4103RT "The complete genome of the hyperthermophilic bacterium Aquifex 4104RT aeolicus."; 4105RL Nature 392:353-358(1998). 4106CC -!- FUNCTION: Low-potential electron donor to a number of redox 4107CC enzymes (By similarity). 4108CC -!- COFACTOR: FMN (By similarity). 4109CC -!- SIMILARITY: Belongs to the flavodoxin family. 4110CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4111CC ----------------------------------------------------------------------- 4112CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4113CC Distributed under the Creative Commons Attribution-NoDerivs License 4114CC ----------------------------------------------------------------------- 4115DR EMBL; AE000657; AAC07825.1; -; Genomic_DNA. 4116DR PIR; F70479; F70479. 4117DR RefSeq; NP_214435.1; NC_000918.1. 4118DR PDB; 2ARK; X-ray; 2.40 A; A/B/C/D/E/F=1-185. 4119DR PDBsum; 2ARK; -. 4120DR ProteinModelPortal; O67866; -. 4121DR SMR; O67866; 1-185. 4122DR GeneID; 1193855; -. 4123DR GenomeReviews; AE000657_GR; aq_2096. 4124DR KEGG; aae:aq_2096; -. 4125DR PATRIC; 20961048; VBIAquAeo85532_1617. 4126DR eggNOG; COG0655; -. 4127DR HOGENOM; HOG000030539; -. 4128DR OMA; WEEGSLA; -. 4129DR ProtClustDB; CLSK230748; -. 4130DR BioCyc; AAEO224324:AQ_2096-MONOMER; -. 4131DR EvolutionaryTrace; O67866; -. 4132DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4133DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4134DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4135DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4136DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4137DR InterPro; IPR008254; Flavodoxin/NO_synth. 4138DR InterPro; IPR001226; Flavodoxin_CS. 4139DR Pfam; PF00258; Flavodoxin_1; 1. 4140DR PROSITE; PS00201; FLAVODOXIN; 1. 4141DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4142PE 1: Evidence at protein level; 4143KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; 4144KW FMN; Reference proteome; Transport. 4145FT CHAIN 1 185 Flavodoxin. 4146FT /FTId=PRO_0000171602. 4147FT DOMAIN 4 159 Flavodoxin-like. 4148FT STRAND 2 8 4149FT STRAND 11 13 4150FT HELIX 14 27 4151FT STRAND 32 38 4152FT TURN 39 41 4153FT HELIX 44 49 4154FT STRAND 51 58 4155FT HELIX 66 74 4156FT HELIX 76 78 4157FT TURN 79 81 4158FT STRAND 87 97 4159FT HELIX 101 114 4160FT STRAND 122 127 4161FT STRAND 130 141 4162FT HELIX 145 165 4163FT HELIX 172 178 4164FT HELIX 180 182 4165SQ SEQUENCE 185 AA; 20444 MW; 7C138666D5B89281 CRC64; 4166 MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN 4167 MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF 4168 GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP 4169 ARFVD 4170// 4171ID FLAV_AZOCH Reviewed; 180 AA. 4172AC P23001; P35708; 4173DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. 4174DT 23-JAN-2007, sequence version 3. 4175DT 31-MAY-2011, entry version 62. 4176DE RecName: Full=Flavodoxin-B; 4177DE Short=FldB; 4178GN Name=nifF; 4179OS Azotobacter chroococcum mcd 1. 4180OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; 4181OC Pseudomonadaceae; Azotobacter. 4182OX NCBI_TaxID=355; 4183RN [1] 4184RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4185RX PubMed=8765738; DOI=10.1007/BF00200433; 4186RA Peelen S., Wijmenga S., Erbel P.J., Robson R.L., Eady R.R., 4187RA Vervoort J.; 4188RT "Possible role of a short extra loop of the long-chain flavodoxin from 4189RT Azotobacter chroococcum in electron transfer to nitrogenase: complete 4190RT 1H, 15N and 13C backbone assignments and secondary solution structure 4191RT of the flavodoxin."; 4192RL J. Biomol. NMR 7:315-330(1996). 4193RN [2] 4194RP PROTEIN SEQUENCE OF 2-21. 4195RC STRAIN=MCD 1155; 4196RX MEDLINE=91315397; PubMed=1859358; 4197RA Bagby S., Barker P.D., Hill H.A.O., Sanghera G.S., Dunbar B., 4198RA Ashby G.A., Eady R.R., Thorneley R.N.F.; 4199RT "Direct electrochemistry of two genetically distinct flavodoxins 4200RT isolated from Azotobacter chroococcum grown under nitrogen-fixing 4201RT conditions."; 4202RL Biochem. J. 277:313-319(1991). 4203CC -!- FUNCTION: Low-potential electron donor to a number of redox 4204CC enzymes. NifF is the electron donor to nitrogenase. 4205CC -!- COFACTOR: FMN. 4206CC -!- SIMILARITY: Belongs to the flavodoxin family. 4207CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4208CC ----------------------------------------------------------------------- 4209CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4210CC Distributed under the Creative Commons Attribution-NoDerivs License 4211CC ----------------------------------------------------------------------- 4212DR EMBL; M73019; AAB36613.1; -; Genomic_DNA. 4213DR ProteinModelPortal; P23001; -. 4214DR SMR; P23001; 2-180. 4215DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4216DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4217DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 4218DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4219DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4220DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW. 4221DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4222DR InterPro; IPR001094; Flavdoxin. 4223DR InterPro; IPR008254; Flavodoxin/NO_synth. 4224DR InterPro; IPR001226; Flavodoxin_CS. 4225DR InterPro; IPR010086; Flavodoxin_lc. 4226DR Pfam; PF00258; Flavodoxin_1; 1. 4227DR PRINTS; PR00369; FLAVODOXIN. 4228DR TIGRFAMs; TIGR01752; Flav_long; 1. 4229DR PROSITE; PS00201; FLAVODOXIN; 1. 4230DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4231PE 1: Evidence at protein level; 4232KW Direct protein sequencing; Electron transport; Flavoprotein; FMN; 4233KW Nitrogen fixation; Transport. 4234FT INIT_MET 1 1 Removed. 4235FT CHAIN 2 180 Flavodoxin-B. 4236FT /FTId=PRO_0000171603. 4237FT DOMAIN 4 173 Flavodoxin-like. 4238SQ SEQUENCE 180 AA; 19524 MW; A19BE720B93F551D CRC64; 4239 MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDAVNVNRV SAEDFAQYQF LILGTPTLGE 4240 GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENFLDA MGELHSFFTE 4241 RGAKVVGAWS TDGYEFEGST AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL 4242// 4243ID FLAV_AZOVI Reviewed; 180 AA. 4244AC P00324; 4245DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 4246DT 23-JAN-2007, sequence version 2. 4247DT 18-APR-2012, entry version 82. 4248DE RecName: Full=Flavodoxin-2; 4249GN Name=nifF; 4250OS Azotobacter vinelandii. 4251OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; 4252OC Pseudomonadaceae; Azotobacter. 4253OX NCBI_TaxID=354; 4254RN [1] 4255RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4256RX MEDLINE=89123097; PubMed=2644218; 4257RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., 4258RA Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.; 4259RT "Physical and genetic map of the major nif gene cluster from 4260RT Azotobacter vinelandii."; 4261RL J. Bacteriol. 171:1017-1027(1989). 4262RN [2] 4263RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4264RX MEDLINE=88087273; PubMed=3121629; 4265RA Bennett L., Jacobson M., Dean D.R.; 4266RT "Isolation, sequencing, and mutagenesis of the nifF gene encoding 4267RT flavodoxin from Azotobacter vinelandii."; 4268RL J. Biol. Chem. 263:1364-1369(1988). 4269RN [3] 4270RP PROTEIN SEQUENCE OF 2-180. 4271RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW; 4272RX MEDLINE=77242321; PubMed=889809; DOI=10.1021/bi00635a005; 4273RA Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.; 4274RT "Complete amino acid sequence of azotoflavin, a flavodoxin from 4275RT Azotobacter vinelandii."; 4276RL Biochemistry 16:3525-3537(1977). 4277RN [4] 4278RP PROTEIN SEQUENCE OF 2-21, AND MASS SPECTROMETRY. 4279RC STRAIN=OP / UW136; 4280RX MEDLINE=96276406; PubMed=8694750; 4281RA Gangeswaran R., Eady R.R.; 4282RT "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in 4283RT electron donation to purified assimilatory nitrate reductase."; 4284RL Biochem. J. 317:103-108(1996). 4285RN [5] 4286RP STRUCTURE BY NMR. 4287RC STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617; 4288RX MEDLINE=98180401; PubMed=9521106; 4289RA Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A., 4290RA van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.; 4291RT "Apparent local stability of the secondary structure of Azotobacter 4292RT vinelandii holoflavodoxin II as probed by hydrogen exchange: 4293RT implications for redox potential regulation and flavodoxin folding."; 4294RL Protein Sci. 7:306-317(1998). 4295CC -!- FUNCTION: Low-potential electron donor to a number of redox 4296CC enzymes. NifF is the electron donor to nitrogenase. 4297CC -!- COFACTOR: FMN. 4298CC -!- SUBUNIT: Monomer. 4299CC -!- MASS SPECTROMETRY: Mass=19533; Mass_error=5; Method=Electrospray; 4300CC Range=2-180; Source=PubMed:8694750; 4301CC -!- SIMILARITY: Belongs to the flavodoxin family. 4302CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4303CC ----------------------------------------------------------------------- 4304CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4305CC Distributed under the Creative Commons Attribution-NoDerivs License 4306CC ----------------------------------------------------------------------- 4307DR EMBL; M20568; AAA64735.1; -; Genomic_DNA. 4308DR EMBL; J03519; AAA22154.1; -; Genomic_DNA. 4309DR PIR; A29935; FXAVEP. 4310DR PDB; 1YOB; X-ray; 2.25 A; A/B=2-179. 4311DR PDBsum; 1YOB; -. 4312DR ProteinModelPortal; P00324; -. 4313DR SMR; P00324; 2-180. 4314DR EvolutionaryTrace; P00324; -. 4315DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4316DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4317DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 4318DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4319DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4320DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW. 4321DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4322DR InterPro; IPR001094; Flavdoxin. 4323DR InterPro; IPR008254; Flavodoxin/NO_synth. 4324DR InterPro; IPR001226; Flavodoxin_CS. 4325DR InterPro; IPR010086; Flavodoxin_lc. 4326DR Pfam; PF00258; Flavodoxin_1; 1. 4327DR PRINTS; PR00369; FLAVODOXIN. 4328DR TIGRFAMs; TIGR01752; Flav_long; 1. 4329DR PROSITE; PS00201; FLAVODOXIN; 1. 4330DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4331PE 1: Evidence at protein level; 4332KW 3D-structure; Direct protein sequencing; Electron transport; 4333KW Flavoprotein; FMN; Nitrogen fixation; Transport. 4334FT INIT_MET 1 1 Removed. 4335FT CHAIN 2 180 Flavodoxin-2. 4336FT /FTId=PRO_0000171605. 4337FT DOMAIN 4 173 Flavodoxin-like. 4338FT STRAND 4 8 4339FT STRAND 11 13 4340FT HELIX 14 23 4341FT TURN 28 30 4342FT HELIX 37 39 4343FT HELIX 42 46 4344FT STRAND 49 56 4345FT TURN 59 61 4346FT HELIX 66 68 4347FT HELIX 75 82 4348FT STRAND 91 97 4349FT TURN 100 102 4350FT TURN 104 108 4351FT HELIX 109 119 4352FT TURN 120 122 4353FT STRAND 124 126 4354FT STRAND 142 152 4355FT TURN 154 156 4356FT HELIX 158 160 4357FT HELIX 161 172 4358FT HELIX 173 176 4359SQ SEQUENCE 180 AA; 19663 MW; 8B1B43F23AB5E8B4 CRC64; 4360 MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDALNVNRV SAEDFAQYQF LILGTPTLGE 4361 GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENYLDA LGELYSFFKD 4362 RGAKIVGSWS TDGYEFESSE AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL 4363// 4364ID FLAV_BACSU Reviewed; 158 AA. 4365AC O34737; 4366DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 4367DT 01-JAN-1998, sequence version 1. 4368DT 16-MAY-2012, entry version 82. 4369DE RecName: Full=Probable flavodoxin-1; 4370GN Name=ykuN; OrderedLocusNames=BSU14150; 4371OS Bacillus subtilis (strain 168). 4372OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. 4373OX NCBI_TaxID=224308; 4374RN [1] 4375RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4376RC STRAIN=168; 4377RA Scanlan E., Devine K.M.; 4378RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. 4379RN [2] 4380RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 4381RC STRAIN=168; 4382RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; 4383RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., 4384RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., 4385RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., 4386RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., 4387RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., 4388RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., 4389RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., 4390RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., 4391RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., 4392RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., 4393RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., 4394RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., 4395RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., 4396RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., 4397RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., 4398RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., 4399RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., 4400RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., 4401RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., 4402RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., 4403RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., 4404RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., 4405RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., 4406RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., 4407RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., 4408RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., 4409RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., 4410RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., 4411RA Yoshikawa H., Danchin A.; 4412RT "The complete genome sequence of the Gram-positive bacterium Bacillus 4413RT subtilis."; 4414RL Nature 390:249-256(1997). 4415CC -!- FUNCTION: Low-potential electron donor to a number of redox 4416CC enzymes (Potential). 4417CC -!- COFACTOR: FMN (By similarity). 4418CC -!- SIMILARITY: Belongs to the flavodoxin family. 4419CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4420CC ----------------------------------------------------------------------- 4421CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4422CC Distributed under the Creative Commons Attribution-NoDerivs License 4423CC ----------------------------------------------------------------------- 4424DR EMBL; AJ222587; CAA10877.1; -; Genomic_DNA. 4425DR EMBL; AL009126; CAB13288.1; -; Genomic_DNA. 4426DR PIR; C69866; C69866. 4427DR RefSeq; NP_389298.1; NC_000964.3. 4428DR ProteinModelPortal; O34737; -. 4429DR SMR; O34737; 2-146. 4430DR EnsemblBacteria; EBBACT00000000146; EBBACP00000000146; EBBACG00000000146. 4431DR GeneID; 939194; -. 4432DR GenomeReviews; AL009126_GR; BSU14150. 4433DR KEGG; bsu:BSU14150; -. 4434DR PATRIC; 18974619; VBIBacSub10457_1501. 4435DR GenoList; BSU14150; -. 4436DR eggNOG; COG0716; -. 4437DR HOGENOM; HOG000030540; -. 4438DR KO; K03839; -. 4439DR OMA; ATKGADS; -. 4440DR ProtClustDB; PRK06703; -. 4441DR BioCyc; BSUB:BSU14150-MONOMER; -. 4442DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4443DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 4444DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4445DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4446DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4447DR InterPro; IPR010087; Flav_short. 4448DR InterPro; IPR001094; Flavdoxin. 4449DR InterPro; IPR008254; Flavodoxin/NO_synth. 4450DR Pfam; PF00258; Flavodoxin_1; 1. 4451DR PRINTS; PR00369; FLAVODOXIN. 4452DR TIGRFAMs; TIGR01753; Flav_short; 1. 4453DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. 4454DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4455PE 3: Inferred from homology; 4456KW Complete proteome; Electron transport; Flavoprotein; FMN; 4457KW Reference proteome; Transport. 4458FT CHAIN 1 158 Probable flavodoxin-1. 4459FT /FTId=PRO_0000171607. 4460FT DOMAIN 4 144 Flavodoxin-like. 4461SQ SEQUENCE 158 AA; 17793 MW; FECE71BF6E552D3F CRC64; 4462 MAKALITYAS MSGNTEDIAF IIKDTLQEYE LDIDCVEIND MDASCLTSYD YVLIGTYTWG 4463 DGDLPYEAED FFEEVKQIQL NGLKTACFGS GDYSYPKFCE AVNLFNVMLQ EAGAAVYQET 4464 LKIELAPETD EDVESCRAFA RGFLAWADYM NKEKIHVS 4465// 4466ID FLAV_CHOCR Reviewed; 173 AA. 4467AC P14070; 4468DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. 4469DT 01-JAN-1990, sequence version 1. 4470DT 18-APR-2012, entry version 72. 4471DE RecName: Full=Flavodoxin; 4472OS Chondrus crispus (Carragheen moss) (Irish moss). 4473OC Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae; 4474OC Chondrus. 4475OX NCBI_TaxID=2769; 4476RN [1] 4477RP PROTEIN SEQUENCE. 4478RX MEDLINE=90088453; PubMed=2597140; 4479RA Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.; 4480RT "The amino acid sequence of a flavodoxin from the eukaryotic red alga 4481RT Chondrus crispus."; 4482RL Biochem. J. 263:981-984(1989). 4483RN [2] 4484RP PROTEIN SEQUENCE OF 1-34. 4485RA Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.; 4486RT "N-terminal amino acid sequences of flavodoxins from Chondrus crispus 4487RT and Nostoc strain MAC."; 4488RL Phytochemistry 25:2113-2115(1986). 4489RN [3] 4490RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). 4491RX MEDLINE=90368796; PubMed=2394748; 4492RA Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.; 4493RT "Tertiary structure of oxidized flavodoxin from an eukaryotic red alga 4494RT Chondrus crispus at 2.35-A resolution. Localization of charged 4495RT residues and implication for interaction with electron transfer 4496RT partners."; 4497RL J. Biol. Chem. 265:15804-15812(1990). 4498RN [4] 4499RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). 4500RX MEDLINE=92292160; PubMed=1602481; DOI=10.1016/0022-2836(92)90400-E; 4501RA Fukuyama K., Matsubara H., Rogers L.J.; 4502RT "Crystal structure of oxidized flavodoxin from a red alga Chondrus 4503RT crispus refined at 1.8-A resolution. Description of the flavin 4504RT mononucleotide binding site."; 4505RL J. Mol. Biol. 225:775-789(1992). 4506CC -!- FUNCTION: Low-potential electron donor to a number of redox 4507CC enzymes. 4508CC -!- COFACTOR: FMN. 4509CC -!- SIMILARITY: Belongs to the flavodoxin family. 4510CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4511CC ----------------------------------------------------------------------- 4512CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4513CC Distributed under the Creative Commons Attribution-NoDerivs License 4514CC ----------------------------------------------------------------------- 4515DR PIR; S06648; S06648. 4516DR PDB; 2FCR; X-ray; 1.80 A; A=1-173. 4517DR PDBsum; 2FCR; -. 4518DR ProteinModelPortal; P14070; -. 4519DR SMR; P14070; 1-173. 4520DR EvolutionaryTrace; P14070; -. 4521DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4522DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4523DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4524DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4525DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4526DR InterPro; IPR008254; Flavodoxin/NO_synth. 4527DR InterPro; IPR001226; Flavodoxin_CS. 4528DR InterPro; IPR010086; Flavodoxin_lc. 4529DR Pfam; PF00258; Flavodoxin_1; 1. 4530DR TIGRFAMs; TIGR01752; Flav_long; 1. 4531DR PROSITE; PS00201; FLAVODOXIN; 1. 4532DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4533PE 1: Evidence at protein level; 4534KW 3D-structure; Direct protein sequencing; Electron transport; 4535KW Flavoprotein; FMN; Transport. 4536FT CHAIN 1 173 Flavodoxin. 4537FT /FTId=PRO_0000171612. 4538FT DOMAIN 2 168 Flavodoxin-like. 4539FT CONFLICT 29 29 D -> S (in Ref. 2; AA sequence). 4540FT CONFLICT 33 33 D -> S (in Ref. 2; AA sequence). 4541FT STRAND 2 6 4542FT STRAND 9 11 4543FT HELIX 12 24 4544FT HELIX 25 27 4545FT HELIX 34 36 4546FT HELIX 40 45 4547FT STRAND 47 54 4548FT HELIX 69 75 4549FT HELIX 77 79 4550FT STRAND 86 93 4551FT TURN 95 97 4552FT TURN 102 104 4553FT HELIX 105 115 4554FT STRAND 119 121 4555FT HELIX 126 128 4556FT STRAND 141 148 4557FT TURN 149 151 4558FT HELIX 156 171 4559SQ SEQUENCE 173 AA; 18871 MW; EF1F3A3554CA4166 CRC64; 4560 KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA 4561 DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP 4562 VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV 4563// 4564ID FLAV_CLOBE Reviewed; 138 AA. 4565AC P00322; 4566DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 4567DT 21-JUL-1986, sequence version 1. 4568DT 18-APR-2012, entry version 75. 4569DE RecName: Full=Flavodoxin; 4570OS Clostridium beijerinckii (Clostridium MP). 4571OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; 4572OC Clostridium. 4573OX NCBI_TaxID=1520; 4574RN [1] 4575RP PROTEIN SEQUENCE. 4576RX MEDLINE=74277392; PubMed=4843142; 4577RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.; 4578RT "The amino acid sequence of the Clostridium MP flavodoxin."; 4579RL J. Biol. Chem. 249:4393-4396(1974). 4580RN [2] 4581RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM. 4582RX MEDLINE=74277391; PubMed=4843141; 4583RA Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G., 4584RA Smith W.W., Ludwig M.L.; 4585RT "The structure of the oxidized form of clostridial flavodoxin at 1.9-A 4586RT resolution."; 4587RL J. Biol. Chem. 249:4383-4392(1974). 4588RN [3] 4589RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). 4590RX MEDLINE=97178811; PubMed=9063874; DOI=10.1021/bi962180o; 4591RA Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M., 4592RA Feng Y., Swenson R.P.; 4593RT "Control of oxidation-reduction potentials in flavodoxin from 4594RT Clostridium beijerinckii: the role of conformation changes."; 4595RL Biochemistry 36:1259-1280(1997). 4596CC -!- FUNCTION: Low-potential electron donor to a number of redox 4597CC enzymes. 4598CC -!- COFACTOR: FMN. 4599CC -!- SIMILARITY: Belongs to the flavodoxin family. 4600CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4601CC ----------------------------------------------------------------------- 4602CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4603CC Distributed under the Creative Commons Attribution-NoDerivs License 4604CC ----------------------------------------------------------------------- 4605DR PDB; 1FLA; X-ray; 1.90 A; A=1-138. 4606DR PDB; 1FLD; X-ray; 1.80 A; A=1-138. 4607DR PDB; 1FLN; X-ray; 1.90 A; A=1-138. 4608DR PDB; 1FVX; X-ray; 1.90 A; A=1-138. 4609DR PDB; 2FAX; X-ray; 1.80 A; A=1-136. 4610DR PDB; 2FDX; X-ray; 1.65 A; A=1-136. 4611DR PDB; 2FLV; X-ray; 1.80 A; A=1-138. 4612DR PDB; 2FOX; X-ray; 1.80 A; A=1-138. 4613DR PDB; 2FVX; X-ray; 1.80 A; A=1-138. 4614DR PDB; 3NLL; X-ray; 2.40 A; A=1-138. 4615DR PDB; 4NLL; X-ray; 1.90 A; A=1-138. 4616DR PDB; 4NUL; X-ray; 1.90 A; A=1-138. 4617DR PDB; 5NLL; X-ray; 1.75 A; A=1-138. 4618DR PDB; 5NUL; X-ray; 1.60 A; A=1-138. 4619DR PDB; 5ULL; X-ray; 1.80 A; A=1-138. 4620DR PDB; 6NUL; X-ray; 1.80 A; A=1-136. 4621DR PDBsum; 1FLA; -. 4622DR PDBsum; 1FLD; -. 4623DR PDBsum; 1FLN; -. 4624DR PDBsum; 1FVX; -. 4625DR PDBsum; 2FAX; -. 4626DR PDBsum; 2FDX; -. 4627DR PDBsum; 2FLV; -. 4628DR PDBsum; 2FOX; -. 4629DR PDBsum; 2FVX; -. 4630DR PDBsum; 3NLL; -. 4631DR PDBsum; 4NLL; -. 4632DR PDBsum; 4NUL; -. 4633DR PDBsum; 5NLL; -. 4634DR PDBsum; 5NUL; -. 4635DR PDBsum; 5ULL; -. 4636DR PDBsum; 6NUL; -. 4637DR ProteinModelPortal; P00322; -. 4638DR SMR; P00322; 1-138. 4639DR EvolutionaryTrace; P00322; -. 4640DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4641DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4642DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4643DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4644DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4645DR InterPro; IPR010087; Flav_short. 4646DR InterPro; IPR008254; Flavodoxin/NO_synth. 4647DR InterPro; IPR001226; Flavodoxin_CS. 4648DR Pfam; PF00258; Flavodoxin_1; 1. 4649DR TIGRFAMs; TIGR01753; Flav_short; 1. 4650DR PROSITE; PS00201; FLAVODOXIN; 1. 4651DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4652PE 1: Evidence at protein level; 4653KW 3D-structure; Direct protein sequencing; Electron transport; 4654KW Flavoprotein; FMN; Transport. 4655FT CHAIN 1 138 Flavodoxin. 4656FT /FTId=PRO_0000171613. 4657FT DOMAIN 1 136 Flavodoxin-like. 4658FT STRAND 2 6 4659FT STRAND 8 10 4660FT HELIX 11 25 4661FT STRAND 31 34 4662FT HELIX 35 37 4663FT HELIX 40 43 4664FT STRAND 47 53 4665FT TURN 57 59 4666FT TURN 63 65 4667FT HELIX 66 73 4668FT HELIX 74 76 4669FT STRAND 81 93 4670FT HELIX 94 105 4671FT STRAND 115 120 4672FT HELIX 122 124 4673FT HELIX 125 136 4674SQ SEQUENCE 138 AA; 15332 MW; 98BE3746EC000FF1 CRC64; 4675 MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV 4676 LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE 4677 PDEAEQDCIE FGKKIANI 4678// 4679ID FLAV_CLOSA Reviewed; 160 AA. 4680AC P18855; 4681DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. 4682DT 01-NOV-1990, sequence version 1. 4683DT 21-SEP-2011, entry version 50. 4684DE RecName: Full=Flavodoxin; 4685GN Name=floX; 4686OS Clostridium saccharobutylicum. 4687OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; 4688OC Clostridium. 4689OX NCBI_TaxID=169679; 4690RN [1] 4691RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4692RX MEDLINE=91123180; PubMed=1991710; 4693RA Santangelo J.D., Jones D.T., Woods D.R.; 4694RT "Metronidazole activation and isolation of Clostridium acetobutylicum 4695RT electron transport genes."; 4696RL J. Bacteriol. 173:1088-1095(1991). 4697CC -!- FUNCTION: Low-potential electron donor to a number of redox 4698CC enzymes. 4699CC -!- COFACTOR: FMN. 4700CC -!- SIMILARITY: Belongs to the flavodoxin family. 4701CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4702CC -!- CAUTION: Was originally thought to originate from 4703CC C.acetobutylicum. 4704CC ----------------------------------------------------------------------- 4705CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4706CC Distributed under the Creative Commons Attribution-NoDerivs License 4707CC ----------------------------------------------------------------------- 4708DR EMBL; M36770; AAA23238.1; -; Genomic_DNA. 4709DR ProteinModelPortal; P18855; -. 4710DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4711DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4712DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4713DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4714DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4715DR InterPro; IPR008254; Flavodoxin/NO_synth. 4716DR InterPro; IPR001226; Flavodoxin_CS. 4717DR Pfam; PF00258; Flavodoxin_1; 1. 4718DR PROSITE; PS00201; FLAVODOXIN; 1. 4719DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4720PE 3: Inferred from homology; 4721KW Electron transport; Flavoprotein; FMN; Transport. 4722FT CHAIN 1 160 Flavodoxin. 4723FT /FTId=PRO_0000171614. 4724FT DOMAIN 3 153 Flavodoxin-like. 4725SQ SEQUENCE 160 AA; 17763 MW; 6153F8A1F0BCDC8D CRC64; 4726 MKISILYSSK TGKTERVAKL IEEGVKRSGN IEVKTMNLDA VDKKFLQESE GIIFGTPTYY 4727 ANISWEMKKW IDESSEFNLE GKLGAAFSTA NSIAGGSDIA LLTILNHLMV KGMLVYSGGV 4728 AFGKPKTHLG YVHINEIQEN EDENARIFGE RIANKVKQIF 4729// 4730ID FLAV_DESDE Reviewed; 148 AA. 4731AC P26492; 4732DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. 4733DT 01-AUG-1992, sequence version 1. 4734DT 18-APR-2012, entry version 53. 4735DE RecName: Full=Flavodoxin; 4736OS Desulfovibrio desulfuricans. 4737OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; 4738OC Desulfovibrionaceae; Desulfovibrio. 4739OX NCBI_TaxID=876; 4740RN [1] 4741RP NUCLEOTIDE SEQUENCE [MRNA]. 4742RC STRAIN=ATCC 29577 / CIP 107039 / LMG 7529 / NCIB 8307 / VKM B-1799; 4743RX MEDLINE=91316149; PubMed=1859847; DOI=10.1016/0167-4781(91)90190-W; 4744RA Helms L.R., Swenson R.P.; 4745RT "Cloning and characterization of the flavodoxin gene from 4746RT Desulfovibrio desulfuricans."; 4747RL Biochim. Biophys. Acta 1089:417-419(1991). 4748CC -!- FUNCTION: Low-potential electron donor to a number of redox 4749CC enzymes. 4750CC -!- COFACTOR: FMN. 4751CC -!- SIMILARITY: Belongs to the flavodoxin family. 4752CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4753CC ----------------------------------------------------------------------- 4754CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4755CC Distributed under the Creative Commons Attribution-NoDerivs License 4756CC ----------------------------------------------------------------------- 4757DR EMBL; X59438; CAA42064.1; -; mRNA. 4758DR PIR; S17000; FXDVD. 4759DR PDB; 3F6R; X-ray; 2.00 A; A/B/C/D=1-148. 4760DR PDB; 3F6S; X-ray; 2.50 A; A/B/D/E/F/G/H/I=1-148. 4761DR PDB; 3F90; X-ray; 2.50 A; A/B/D/E/F/G/H/I=1-148. 4762DR PDBsum; 3F6R; -. 4763DR PDBsum; 3F6S; -. 4764DR PDBsum; 3F90; -. 4765DR ProteinModelPortal; P26492; -. 4766DR EvolutionaryTrace; P26492; -. 4767DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4768DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4769DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4770DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4771DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4772DR InterPro; IPR010087; Flav_short. 4773DR InterPro; IPR008254; Flavodoxin/NO_synth. 4774DR InterPro; IPR001226; Flavodoxin_CS. 4775DR Pfam; PF00258; Flavodoxin_1; 1. 4776DR TIGRFAMs; TIGR01753; Flav_short; 1. 4777DR PROSITE; PS00201; FLAVODOXIN; 1. 4778DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4779PE 1: Evidence at protein level; 4780KW 3D-structure; Electron transport; Flavoprotein; FMN; Transport. 4781FT CHAIN 1 148 Flavodoxin. 4782FT /FTId=PRO_0000171615. 4783FT DOMAIN 4 145 Flavodoxin-like. 4784FT STRAND 3 8 4785FT HELIX 15 27 4786FT STRAND 32 37 4787FT TURN 38 40 4788FT TURN 44 47 4789FT STRAND 52 55 4790FT HELIX 69 75 4791FT HELIX 76 80 4792FT STRAND 87 90 4793FT STRAND 98 100 4794FT HELIX 105 114 4795FT HELIX 130 132 4796FT HELIX 134 146 4797SQ SEQUENCE 148 AA; 15694 MW; 1CE35B4B79817459 CRC64; 4798 MSKVLIVFGS STGNTESIAQ KLEELIAAGG HEVTLLNAAD ASAENLADGY DAVLFGCSAW 4799 GMEDLEMQDD FLSLFEEFNR IGLAGRKVAA FASGDQEYEH FCGAVPAIEE RAKELGATII 4800 AEGLKMEGDA SNDPEAVASF AEDVLKQL 4801// 4802ID FLAV_DESGI Reviewed; 146 AA. 4803AC Q01095; 4804DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. 4805DT 01-APR-1993, sequence version 1. 4806DT 31-MAY-2011, entry version 56. 4807DE RecName: Full=Flavodoxin; 4808OS Desulfovibrio gigas. 4809OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; 4810OC Desulfovibrionaceae; Desulfovibrio. 4811OX NCBI_TaxID=879; 4812RN [1] 4813RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4814RC STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759; 4815RX MEDLINE=92329549; PubMed=1627649; DOI=10.1016/0167-4781(92)90034-W; 4816RA Helms L.R., Swenson R.P.; 4817RT "The primary structures of the flavodoxins from two strains of 4818RT Desulfovibrio gigas. Cloning and nucleotide sequence of the structural 4819RT genes."; 4820RL Biochim. Biophys. Acta 1131:325-328(1992). 4821CC -!- FUNCTION: Electron-transfer proteins that function in various 4822CC electron transport systems in micro-organisms. Functionally 4823CC interchangeable with ferredoxin. 4824CC -!- COFACTOR: FMN. 4825CC -!- SIMILARITY: Belongs to the flavodoxin family. 4826CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4827CC ----------------------------------------------------------------------- 4828CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4829CC Distributed under the Creative Commons Attribution-NoDerivs License 4830CC ----------------------------------------------------------------------- 4831DR EMBL; X64766; CAA46013.1; -; Genomic_DNA. 4832DR PIR; S24311; S24311. 4833DR ProteinModelPortal; Q01095; -. 4834DR SMR; Q01095; 2-146. 4835DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4836DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4837DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 4838DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4839DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4840DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4841DR InterPro; IPR010087; Flav_short. 4842DR InterPro; IPR001094; Flavdoxin. 4843DR InterPro; IPR008254; Flavodoxin/NO_synth. 4844DR InterPro; IPR001226; Flavodoxin_CS. 4845DR Pfam; PF00258; Flavodoxin_1; 1. 4846DR PRINTS; PR00369; FLAVODOXIN. 4847DR TIGRFAMs; TIGR01753; Flav_short; 1. 4848DR PROSITE; PS00201; FLAVODOXIN; 1. 4849DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4850PE 3: Inferred from homology; 4851KW Electron transport; Flavoprotein; FMN; Transport. 4852FT CHAIN 1 146 Flavodoxin. 4853FT /FTId=PRO_0000171617. 4854FT DOMAIN 4 143 Flavodoxin-like. 4855SQ SEQUENCE 146 AA; 15470 MW; 95D9E73B1FCF1403 CRC64; 4856 MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW 4857 GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV 4858 ASSLKIDGEP DSAEVLDWAR EVLARV 4859// 4860ID FLAV_DESAD Reviewed; 146 AA. 4861AC P18086; C6BZ47; 4862DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. 4863DT 01-NOV-1990, sequence version 1. 4864DT 16-MAY-2012, entry version 64. 4865DE RecName: Full=Flavodoxin; 4866GN OrderedLocusNames=Desal_0805; 4867OS Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / 4868OS VKM B-1763). 4869OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; 4870OC Desulfovibrionaceae; Desulfovibrio. 4871OX NCBI_TaxID=526222; 4872RN [1] 4873RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4874RX MEDLINE=90241257; PubMed=2334437; DOI=10.1016/0006-291X(90)92393-E; 4875RA Helms L.R., Krey G.D., Swenson R.P.; 4876RT "Identification, sequence determination, and expression of the 4877RT flavodoxin gene from Desulfovibrio salexigens."; 4878RL Biochem. Biophys. Res. Commun. 168:809-817(1990). 4879RN [2] 4880RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 4881RC STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763; 4882RG US DOE Joint Genome Institute; 4883RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., 4884RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., 4885RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., 4886RA Anderson I., Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., 4887RA Hazen T.C.; 4888RT "Complete sequence of Desulfovibrio salexigens DSM 2638."; 4889RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. 4890CC -!- FUNCTION: Low-potential electron donor to a number of redox 4891CC enzymes. 4892CC -!- COFACTOR: FMN. 4893CC -!- SIMILARITY: Belongs to the flavodoxin family. 4894CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 4895CC ----------------------------------------------------------------------- 4896CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 4897CC Distributed under the Creative Commons Attribution-NoDerivs License 4898CC ----------------------------------------------------------------------- 4899DR EMBL; M35475; AAA23368.1; -; Genomic_DNA. 4900DR EMBL; CP001649; ACS78871.1; -; Genomic_DNA. 4901DR PIR; A34640; A34640. 4902DR RefSeq; YP_002990410.1; NC_012881.1. 4903DR ProteinModelPortal; P18086; -. 4904DR SMR; P18086; 2-146. 4905DR STRING; P18086; -. 4906DR GeneID; 8091789; -. 4907DR GenomeReviews; CP001649_GR; Desal_0805. 4908DR KEGG; dsa:Desal_0805; -. 4909DR PATRIC; 21757061; VBIDesSal121003_0807. 4910DR eggNOG; COG0716; -. 4911DR HOGENOM; HOG000030540; -. 4912DR ProtClustDB; CLSK634549; -. 4913DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 4914DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 4915DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 4916DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 4917DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 4918DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 4919DR InterPro; IPR010087; Flav_short. 4920DR InterPro; IPR001094; Flavdoxin. 4921DR InterPro; IPR008254; Flavodoxin/NO_synth. 4922DR InterPro; IPR001226; Flavodoxin_CS. 4923DR Pfam; PF00258; Flavodoxin_1; 1. 4924DR PRINTS; PR00369; FLAVODOXIN. 4925DR TIGRFAMs; TIGR01753; Flav_short; 1. 4926DR PROSITE; PS00201; FLAVODOXIN; 1. 4927DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 4928PE 3: Inferred from homology; 4929KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 4930FT CHAIN 1 146 Flavodoxin. 4931FT /FTId=PRO_0000171619. 4932FT DOMAIN 4 143 Flavodoxin-like. 4933SQ SEQUENCE 146 AA; 15812 MW; BDE3651310E1F780 CRC64; 4934 MSKSLIVYGS TTGNTETAAE YVAEAFENKE IDVELKNVTD VSVADLGNGY DIVLFGCSTW 4935 GEEEIELQDD FIPLYDSLEN ADLKGKKVSV FGCGDSDYTY FCGAVDAIEE KLEKMGAVVI 4936 GDSLKIDGDP ERDEIVSWGS GIADKI 4937// 4938ID FLAV_DESVH Reviewed; 148 AA. 4939AC P00323; 4940DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 4941DT 01-NOV-1990, sequence version 2. 4942DT 16-MAY-2012, entry version 100. 4943DE RecName: Full=Flavodoxin; 4944GN OrderedLocusNames=DVU_2680; 4945OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 4946OS 8303). 4947OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; 4948OC Desulfovibrionaceae; Desulfovibrio. 4949OX NCBI_TaxID=882; 4950RN [1] 4951RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4952RX MEDLINE=89008444; PubMed=3170590; 4953RA Krey G.D., Vanin E.F., Swenson R.P.; 4954RT "Cloning, nucleotide sequence, and expression of the flavodoxin gene 4955RT from Desulfovibrio vulgaris (Hildenborough)."; 4956RL J. Biol. Chem. 263:15436-15443(1988). 4957RN [2] 4958RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 4959RA Curley G.P., Voordouw G.; 4960RT "Cloning and sequencing of the gene encoding flavodoxin from 4961RT Desulfovibrio vulgaris Hildenborough."; 4962RL FEMS Microbiol. Lett. 49:295-299(1988). 4963RN [3] 4964RP PROTEIN SEQUENCE. 4965RX MEDLINE=77118626; PubMed=402366; 4966RA Dubourdieu M., Fox J.L.; 4967RT "Amino acid sequence of Desulfovibrio vulgaris flavodoxin."; 4968RL J. Biol. Chem. 252:1453-1463(1977). 4969RN [4] 4970RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 4971RC STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303; 4972RX PubMed=15077118; DOI=10.1038/nbt959; 4973RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., 4974RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., 4975RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., 4976RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., 4977RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., 4978RA Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., 4979RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; 4980RT "The genome sequence of the anaerobic, sulfate-reducing bacterium 4981RT Desulfovibrio vulgaris Hildenborough."; 4982RL Nat. Biotechnol. 22:554-559(2004). 4983RN [5] 4984RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). 4985RX MEDLINE=91162643; PubMed=2002503; DOI=10.1016/0022-2836(91)90884-9; 4986RA Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.; 4987RT "Comparison of the crystal structures of a flavodoxin in its three 4988RT oxidation states at cryogenic temperatures."; 4989RL J. Mol. Biol. 218:195-208(1991). 4990RN [6] 4991RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). 4992RX MEDLINE=74087652; PubMed=4521211; DOI=10.1073/pnas.70.12.3857; 4993RA Watenpaugh K.D., Sieker L.C., Jensen L.H.; 4994RT "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin 4995RT at 2.0-A resolution."; 4996RL Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973). 4997RN [7] 4998RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). 4999RX MEDLINE=73044810; PubMed=4508313; DOI=10.1073/pnas.69.11.3185; 5000RA Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.; 5001RT "Structure of the oxidized form of a flavodoxin at 2.5-A resolution: 5002RT resolution of the phase ambiguity by anomalous scattering."; 5003RL Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972). 5004RN [8] 5005RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). 5006RX MEDLINE=99089597; PubMed=9874201; 5007RX DOI=10.1046/j.1432-1327.1998.2580362.x; 5008RA Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D., 5009RA Mayhew S.G., Higgins T.M.; 5010RT "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) 5011RT apoflavodoxin-riboflavin complex."; 5012RL Eur. J. Biochem. 258:362-371(1998). 5013RN [9] 5014RP STRUCTURE BY NMR. 5015RX MEDLINE=93238683; PubMed=8477691; 5016RX DOI=10.1111/j.1432-1033.1993.tb17746.x; 5017RA Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G., 5018RA Mueller F., Rueterjans H.; 5019RT "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio 5020RT vulgaris flavodoxin. Sequential assignments and identification of 5021RT secondary structure elements."; 5022RL Eur. J. Biochem. 213:167-184(1993). 5023RN [10] 5024RP STRUCTURE BY NMR. 5025RX MEDLINE=96283837; PubMed=8681954; 5026RX DOI=10.1111/j.1432-1033.1996.0423z.x; 5027RA Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.; 5028RT "NMR investigation of the solution conformation of oxidized flavodoxin 5029RT from Desulfovibrio vulgaris. Determination of the tertiary structure 5030RT and detection of protein-bound water molecules."; 5031RL Eur. J. Biochem. 238:423-434(1996). 5032RN [11] 5033RP STRUCTURE BY NMR. 5034RX MEDLINE=93237739; PubMed=8477184; DOI=10.1007/BF00178258; 5035RA Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A., 5036RA Swenson R.P.; 5037RT "1H and 15N resonance assignments and solution secondary structure of 5038RT oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear 5039RT three-dimensional NMR spectroscopy."; 5040RL J. Biomol. NMR 3:133-149(1993). 5041CC -!- FUNCTION: Low-potential electron donor to a number of redox 5042CC enzymes. 5043CC -!- COFACTOR: FMN. 5044CC -!- SIMILARITY: Belongs to the flavodoxin family. 5045CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5046CC ----------------------------------------------------------------------- 5047CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5048CC Distributed under the Creative Commons Attribution-NoDerivs License 5049CC ----------------------------------------------------------------------- 5050DR EMBL; J04033; AAA23367.1; -; Genomic_DNA. 5051DR EMBL; AE017285; AAS97152.1; -; Genomic_DNA. 5052DR PIR; A31991; FXDV. 5053DR RefSeq; YP_011892.1; NC_002937.3. 5054DR PDB; 1AKQ; X-ray; 1.90 A; A=2-148. 5055DR PDB; 1AKR; X-ray; 1.58 A; A=2-148. 5056DR PDB; 1AKT; X-ray; 1.80 A; A=2-148. 5057DR PDB; 1AKU; X-ray; 1.90 A; A=2-148. 5058DR PDB; 1AKV; X-ray; 2.00 A; A=2-148. 5059DR PDB; 1AKW; X-ray; 1.75 A; A=2-148. 5060DR PDB; 1AZL; X-ray; 1.80 A; A=2-148. 5061DR PDB; 1BU5; X-ray; 1.83 A; A/B=2-148. 5062DR PDB; 1C7E; X-ray; 2.25 A; A/B=2-148. 5063DR PDB; 1C7F; X-ray; 2.00 A; A/B=2-148. 5064DR PDB; 1F4P; X-ray; 1.30 A; A=2-148. 5065DR PDB; 1FX1; X-ray; 2.00 A; A=1-148. 5066DR PDB; 1I1O; X-ray; 2.00 A; A=3-148. 5067DR PDB; 1J8Q; X-ray; 1.35 A; A=3-148. 5068DR PDB; 1J9E; X-ray; 1.44 A; A=3-148. 5069DR PDB; 1J9G; X-ray; 2.40 A; A=3-148. 5070DR PDB; 1WSB; X-ray; 1.80 A; A=3-148. 5071DR PDB; 1WSW; X-ray; 1.69 A; A=3-148. 5072DR PDB; 1XT6; X-ray; 1.80 A; A=3-148. 5073DR PDB; 1XYV; X-ray; 1.79 A; A=3-148. 5074DR PDB; 1XYY; X-ray; 1.70 A; A=3-148. 5075DR PDB; 2FX2; X-ray; 1.90 A; A=3-148. 5076DR PDB; 3FX2; X-ray; 1.90 A; A=3-148. 5077DR PDB; 4FX2; X-ray; 1.90 A; A=3-148. 5078DR PDB; 5FX2; X-ray; 1.90 A; A=3-148. 5079DR PDBsum; 1AKQ; -. 5080DR PDBsum; 1AKR; -. 5081DR PDBsum; 1AKT; -. 5082DR PDBsum; 1AKU; -. 5083DR PDBsum; 1AKV; -. 5084DR PDBsum; 1AKW; -. 5085DR PDBsum; 1AZL; -. 5086DR PDBsum; 1BU5; -. 5087DR PDBsum; 1C7E; -. 5088DR PDBsum; 1C7F; -. 5089DR PDBsum; 1F4P; -. 5090DR PDBsum; 1FX1; -. 5091DR PDBsum; 1I1O; -. 5092DR PDBsum; 1J8Q; -. 5093DR PDBsum; 1J9E; -. 5094DR PDBsum; 1J9G; -. 5095DR PDBsum; 1WSB; -. 5096DR PDBsum; 1WSW; -. 5097DR PDBsum; 1XT6; -. 5098DR PDBsum; 1XYV; -. 5099DR PDBsum; 1XYY; -. 5100DR PDBsum; 2FX2; -. 5101DR PDBsum; 3FX2; -. 5102DR PDBsum; 4FX2; -. 5103DR PDBsum; 5FX2; -. 5104DR ProteinModelPortal; P00323; -. 5105DR SMR; P00323; 2-148. 5106DR STRING; P00323; -. 5107DR GeneID; 2795051; -. 5108DR GenomeReviews; AE017285_GR; DVU_2680. 5109DR KEGG; dvu:DVU2680; -. 5110DR PATRIC; 32064950; VBIDesVul119526_2425. 5111DR TIGR; DVU_2680; -. 5112DR eggNOG; COG0716; -. 5113DR OMA; HFCGAVD; -. 5114DR ProtClustDB; CLSK634549; -. 5115DR BioCyc; DVUL882:DVU_2680-MONOMER; -. 5116DR DrugBank; DB00140; Riboflavin. 5117DR EvolutionaryTrace; P00323; -. 5118DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5119DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5120DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 5121DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5122DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5123DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5124DR InterPro; IPR010087; Flav_short. 5125DR InterPro; IPR001094; Flavdoxin. 5126DR InterPro; IPR008254; Flavodoxin/NO_synth. 5127DR InterPro; IPR001226; Flavodoxin_CS. 5128DR Pfam; PF00258; Flavodoxin_1; 1. 5129DR PRINTS; PR00369; FLAVODOXIN. 5130DR TIGRFAMs; TIGR01753; Flav_short; 1. 5131DR PROSITE; PS00201; FLAVODOXIN; 1. 5132DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5133PE 1: Evidence at protein level; 5134KW 3D-structure; Complete proteome; Direct protein sequencing; 5135KW Electron transport; Flavoprotein; FMN; Reference proteome; Transport. 5136FT CHAIN 1 148 Flavodoxin. 5137FT /FTId=PRO_0000171620. 5138FT DOMAIN 4 145 Flavodoxin-like. 5139FT CONFLICT 28 28 D -> N (in Ref. 2). 5140FT STRAND 3 9 5141FT STRAND 11 13 5142FT HELIX 14 29 5143FT STRAND 32 37 5144FT HELIX 38 40 5145FT TURN 44 49 5146FT STRAND 51 57 5147FT STRAND 62 64 5148FT TURN 69 71 5149FT HELIX 72 76 5150FT HELIX 78 80 5151FT STRAND 87 94 5152FT STRAND 98 100 5153FT HELIX 103 114 5154FT STRAND 124 128 5155FT HELIX 130 133 5156FT HELIX 134 145 5157SQ SEQUENCE 148 AA; 15823 MW; E07630E7047ABD3F CRC64; 5158 MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW 5159 GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV 5160 QDGLRIDGDP RAARDDIVGW AHDVRGAI 5161// 5162ID FLAV_DESVM Reviewed; 148 AA. 5163AC P71165; B8DKD5; 5164DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 5165DT 14-APR-2009, sequence version 2. 5166DT 16-MAY-2012, entry version 61. 5167DE RecName: Full=Flavodoxin; 5168GN OrderedLocusNames=DvMF_1143; 5169OS Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637). 5170OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; 5171OC Desulfovibrionaceae; Desulfovibrio. 5172OX NCBI_TaxID=883; 5173RN [1] 5174RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. 5175RC STRAIN=Isolate F; 5176RX MEDLINE=98230696; PubMed=9562622; 5177RA Kitamura M., Sagara T., Taniguchi M., Ashida M., Ezoe K., Kohno K., 5178RA Kojima S., Ozawa K., Akutsu H., Kumagai I., Nakaya T.; 5179RT "Cloning and expression of the gene encoding flavodoxin from 5180RT Desulfovibrio vulgaris (Miyazaki F)."; 5181RL J. Biochem. 123:891-898(1998). 5182RN [2] 5183RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5184RC STRAIN=Miyazaki F / DSM 19637; 5185RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., 5186RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., 5187RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., 5188RA Mikhailova N., Hazen T.C., Richardson P.; 5189RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'."; 5190RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 5191CC -!- FUNCTION: Low-potential electron donor to a number of redox 5192CC enzymes. 5193CC -!- COFACTOR: FMN. 5194CC -!- SIMILARITY: Belongs to the flavodoxin family. 5195CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5196CC ----------------------------------------------------------------------- 5197CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5198CC Distributed under the Creative Commons Attribution-NoDerivs License 5199CC ----------------------------------------------------------------------- 5200DR EMBL; D88493; BAA13628.1; -; Genomic_DNA. 5201DR EMBL; CP001197; ACL08097.1; -; Genomic_DNA. 5202DR RefSeq; YP_002435565.1; NC_011769.1. 5203DR ProteinModelPortal; P71165; -. 5204DR STRING; P71165; -. 5205DR GeneID; 7173044; -. 5206DR GenomeReviews; CP001197_GR; DvMF_1143. 5207DR KEGG; dvm:DvMF_1143; -. 5208DR PATRIC; 21772357; VBIDesVul86729_1215. 5209DR eggNOG; COG0716; -. 5210DR HOGENOM; HOG000030540; -. 5211DR OMA; ARIICDS; -. 5212DR ProtClustDB; CLSK634549; -. 5213DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5214DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5215DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 5216DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5217DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5218DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5219DR InterPro; IPR010087; Flav_short. 5220DR InterPro; IPR001094; Flavdoxin. 5221DR InterPro; IPR008254; Flavodoxin/NO_synth. 5222DR InterPro; IPR001226; Flavodoxin_CS. 5223DR Pfam; PF00258; Flavodoxin_1; 1. 5224DR PRINTS; PR00369; FLAVODOXIN. 5225DR TIGRFAMs; TIGR01753; Flav_short; 1. 5226DR PROSITE; PS00201; FLAVODOXIN; 1. 5227DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5228PE 1: Evidence at protein level; 5229KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 5230FT CHAIN 1 148 Flavodoxin. 5231FT /FTId=PRO_0000171621. 5232FT DOMAIN 4 145 Flavodoxin-like. 5233FT CONFLICT 104 104 A -> P (in Ref. 1; BAA13628). 5234SQ SEQUENCE 148 AA; 15630 MW; 9D321268C4089DF1 CRC64; 5235 MANVLIVYGS TTGNTAWVAE TVGRDIAEAG HSVEIRDAGQ VEAEGLCEGR DLVLFGCSTW 5236 GDDEIELQDD FIHLYESLEA TGAGKGRAAC FGCGDSSYTY FCGAVDAIEE RLSGLGADIV 5237 ADSLKIDGDP RTMRDDVSAW AGRVVTAL 5238// 5239ID FLAV_ECO57 Reviewed; 176 AA. 5240AC P61951; P23243; 5241DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. 5242DT 23-JAN-2007, sequence version 2. 5243DT 16-MAY-2012, entry version 51. 5244DE RecName: Full=Flavodoxin-1; 5245GN Name=fldA; OrderedLocusNames=Z0832, ECs0715; 5246OS Escherichia coli O157:H7. 5247OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 5248OC Enterobacteriaceae; Escherichia. 5249OX NCBI_TaxID=83334; 5250RN [1] 5251RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5252RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; 5253RX MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089; 5254RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., 5255RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., 5256RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., 5257RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., 5258RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., 5259RA Welch R.A., Blattner F.R.; 5260RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; 5261RL Nature 409:529-533(2001). 5262RN [2] 5263RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5264RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; 5265RX MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11; 5266RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., 5267RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., 5268RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., 5269RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; 5270RT "Complete genome sequence of enterohemorrhagic Escherichia coli 5271RT O157:H7 and genomic comparison with a laboratory strain K-12."; 5272RL DNA Res. 8:11-22(2001). 5273CC -!- FUNCTION: Low-potential electron donor to a number of redox 5274CC enzymes (Potential). Involved in the reactivation of inactive 5275CC cob(II)alamin in methionine synthase (By similarity). 5276CC -!- COFACTOR: FMN (By similarity). 5277CC -!- SIMILARITY: Belongs to the flavodoxin family. 5278CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5279CC ----------------------------------------------------------------------- 5280CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5281CC Distributed under the Creative Commons Attribution-NoDerivs License 5282CC ----------------------------------------------------------------------- 5283DR EMBL; AE005174; AAG55007.1; -; Genomic_DNA. 5284DR EMBL; BA000007; BAB34138.1; -; Genomic_DNA. 5285DR PIR; C85568; C85568. 5286DR PIR; C90718; C90718. 5287DR RefSeq; NP_286399.1; NC_002655.2. 5288DR RefSeq; NP_308742.1; NC_002695.1. 5289DR ProteinModelPortal; P61951; -. 5290DR SMR; P61951; 2-176. 5291DR EnsemblBacteria; EBESCT00000027406; EBESCP00000026299; EBESCG00000026458. 5292DR EnsemblBacteria; EBESCT00000055801; EBESCP00000053629; EBESCG00000054849. 5293DR GeneID; 917084; -. 5294DR GeneID; 957759; -. 5295DR GenomeReviews; AE005174_GR; Z0832. 5296DR GenomeReviews; BA000007_GR; ECs0715. 5297DR KEGG; ece:Z0832; -. 5298DR KEGG; ecs:ECs0715; -. 5299DR PATRIC; 18350446; VBIEscCol44059_0734. 5300DR eggNOG; COG0716; -. 5301DR HOGENOM; HOG000030543; -. 5302DR KO; K03839; -. 5303DR OMA; DDKHFVG; -. 5304DR ProtClustDB; PRK09267; -. 5305DR BioCyc; ECOL83334:ECS0715-MONOMER; -. 5306DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5307DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5308DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5309DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5310DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5311DR InterPro; IPR008254; Flavodoxin/NO_synth. 5312DR InterPro; IPR001226; Flavodoxin_CS. 5313DR InterPro; IPR010086; Flavodoxin_lc. 5314DR Pfam; PF00258; Flavodoxin_1; 1. 5315DR TIGRFAMs; TIGR01752; Flav_long; 1. 5316DR PROSITE; PS00201; FLAVODOXIN; 1. 5317DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5318PE 3: Inferred from homology; 5319KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 5320FT INIT_MET 1 1 Removed (By similarity). 5321FT CHAIN 2 176 Flavodoxin-1. 5322FT /FTId=PRO_0000171624. 5323FT DOMAIN 4 165 Flavodoxin-like. 5324SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; 5325 MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG 5326 EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW 5327 PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA 5328// 5329ID FLAV_ECOL6 Reviewed; 176 AA. 5330AC P61950; P23243; 5331DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. 5332DT 23-JAN-2007, sequence version 2. 5333DT 13-JUN-2012, entry version 51. 5334DE RecName: Full=Flavodoxin-1; 5335GN Name=fldA; OrderedLocusNames=c0771; 5336OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). 5337OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 5338OC Enterobacteriaceae; Escherichia. 5339OX NCBI_TaxID=199310; 5340RN [1] 5341RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5342RC STRAIN=CFT073 / ATCC 700928 / UPEC; 5343RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; 5344RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., 5345RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., 5346RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., 5347RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; 5348RT "Extensive mosaic structure revealed by the complete genome sequence 5349RT of uropathogenic Escherichia coli."; 5350RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). 5351CC -!- FUNCTION: Low-potential electron donor to a number of redox 5352CC enzymes (Potential). Involved in the reactivation of inactive 5353CC cob(II)alamin in methionine synthase (By similarity). 5354CC -!- COFACTOR: FMN (By similarity). 5355CC -!- SIMILARITY: Belongs to the flavodoxin family. 5356CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5357CC -!- SEQUENCE CAUTION: 5358CC Sequence=AAN79244.1; Type=Erroneous initiation; 5359CC ----------------------------------------------------------------------- 5360CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5361CC Distributed under the Creative Commons Attribution-NoDerivs License 5362CC ----------------------------------------------------------------------- 5363DR EMBL; AE014075; AAN79244.1; ALT_INIT; Genomic_DNA. 5364DR RefSeq; NP_752701.2; NC_004431.1. 5365DR ProteinModelPortal; P61950; -. 5366DR SMR; P61950; 2-176. 5367DR EnsemblBacteria; EBESCT00000041388; EBESCP00000039737; EBESCG00000040438. 5368DR GeneID; 1035998; -. 5369DR GenomeReviews; AE014075_GR; c0771. 5370DR KEGG; ecc:c0771; -. 5371DR PATRIC; 18279597; VBIEscCol75197_0735. 5372DR HOGENOM; HOG000030543; -. 5373DR KO; K03839; -. 5374DR OMA; DDKHFVG; -. 5375DR ProtClustDB; PRK09267; -. 5376DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5377DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5378DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5379DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5380DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5381DR InterPro; IPR008254; Flavodoxin/NO_synth. 5382DR InterPro; IPR001226; Flavodoxin_CS. 5383DR InterPro; IPR010086; Flavodoxin_lc. 5384DR Pfam; PF00258; Flavodoxin_1; 1. 5385DR TIGRFAMs; TIGR01752; Flav_long; 1. 5386DR PROSITE; PS00201; FLAVODOXIN; 1. 5387DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5388PE 3: Inferred from homology; 5389KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 5390FT INIT_MET 1 1 Removed (By similarity). 5391FT CHAIN 2 176 Flavodoxin-1. 5392FT /FTId=PRO_0000171623. 5393FT DOMAIN 4 165 Flavodoxin-like. 5394SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; 5395 MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG 5396 EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW 5397 PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA 5398// 5399ID FLAV_ECOLI Reviewed; 176 AA. 5400AC P61949; P23243; 5401DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. 5402DT 23-JAN-2007, sequence version 2. 5403DT 16-MAY-2012, entry version 81. 5404DE RecName: Full=Flavodoxin-1; 5405GN Name=fldA; OrderedLocusNames=b0684, JW0671; 5406OS Escherichia coli (strain K12). 5407OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 5408OC Enterobacteriaceae; Escherichia. 5409OX NCBI_TaxID=83333; 5410RN [1] 5411RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15. 5412RX MEDLINE=91154129; PubMed=1999390; 5413RA Osborne C., Chen L.-M., Matthews R.G.; 5414RT "Isolation, cloning, mapping, and nucleotide sequencing of the gene 5415RT encoding flavodoxin in Escherichia coli."; 5416RL J. Bacteriol. 173:1729-1737(1991). 5417RN [2] 5418RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5419RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 5420RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137; 5421RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., 5422RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., 5423RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., 5424RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., 5425RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., 5426RA Yano M., Horiuchi T.; 5427RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome 5428RT corresponding to the 12.7-28.0 min region on the linkage map."; 5429RL DNA Res. 3:137-155(1996). 5430RN [3] 5431RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5432RC STRAIN=K12 / MG1655 / ATCC 47076; 5433RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; 5434RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., 5435RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., 5436RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., 5437RA Mau B., Shao Y.; 5438RT "The complete genome sequence of Escherichia coli K-12."; 5439RL Science 277:1453-1474(1997). 5440RN [4] 5441RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5442RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 5443RX PubMed=16738553; DOI=10.1038/msb4100049; 5444RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., 5445RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; 5446RT "Highly accurate genome sequences of Escherichia coli K-12 strains 5447RT MG1655 and W3110."; 5448RL Mol. Syst. Biol. 2:E1-E5(2006). 5449RN [5] 5450RP PROTEIN SEQUENCE OF 2-11. 5451RX MEDLINE=95050480; PubMed=7961651; 5452RA Jenkins C.M., Waterman M.R.; 5453RT "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli 5454RT support bovine cytochrome P450c17 hydroxylase activities."; 5455RL J. Biol. Chem. 269:27401-27408(1994). 5456RN [6] 5457RP FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN. 5458RX PubMed=9730838; DOI=10.1021/bi9808565; 5459RA Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.; 5460RT "The mechanism of adenosylmethionine-dependent activation of 5461RT methionine synthase: a rapid kinetic analysis of intermediates in 5462RT reductive methylation of Cob(II)alamin enzyme."; 5463RL Biochemistry 37:12649-12658(1998). 5464RN [7] 5465RP STRUCTURE BY NMR. 5466RX MEDLINE=97234567; PubMed=9119004; 5467RX DOI=10.1111/j.1432-1033.1997.00384.x; 5468RA Ponstingl H., Otting G.; 5469RT "NMR assignments, secondary structure and hydration of oxidized 5470RT Escherichia coli flavodoxin."; 5471RL Eur. J. Biochem. 244:384-399(1997). 5472RN [8] 5473RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). 5474RX MEDLINE=98078562; PubMed=9416602; 5475RA Hoover D.M., Ludwig M.L.; 5476RT "A flavodoxin that is required for enzyme activation: the structure of 5477RT oxidized flavodoxin from Escherichia coli at 1.8-A resolution."; 5478RL Protein Sci. 6:2525-2537(1997). 5479CC -!- FUNCTION: Low-potential electron donor to a number of redox 5480CC enzymes (Potential). Involved in the reactivation of inactive 5481CC cob(II)alamin in methionine synthase. 5482CC -!- COFACTOR: FMN. 5483CC -!- SIMILARITY: Belongs to the flavodoxin family. 5484CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5485CC ----------------------------------------------------------------------- 5486CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5487CC Distributed under the Creative Commons Attribution-NoDerivs License 5488CC ----------------------------------------------------------------------- 5489DR EMBL; M59426; AAA23789.1; -; Genomic_DNA. 5490DR EMBL; U00096; AAC73778.1; -; Genomic_DNA. 5491DR EMBL; AP009048; BAA35333.1; -; Genomic_DNA. 5492DR PIR; A37319; A37319. 5493DR RefSeq; NP_415210.1; NC_000913.2. 5494DR PDB; 1AG9; X-ray; 1.80 A; A/B=2-176. 5495DR PDB; 1AHN; X-ray; 2.60 A; A=2-176. 5496DR PDBsum; 1AG9; -. 5497DR PDBsum; 1AHN; -. 5498DR ProteinModelPortal; P61949; -. 5499DR SMR; P61949; 2-176. 5500DR DIP; DIP-48242N; -. 5501DR IntAct; P61949; 19. 5502DR MINT; MINT-1239730; -. 5503DR ECO2DBASE; A019.0; 6TH EDITION. 5504DR EnsemblBacteria; EBESCT00000004622; EBESCP00000004622; EBESCG00000003770. 5505DR EnsemblBacteria; EBESCT00000015811; EBESCP00000015102; EBESCG00000014871. 5506DR GeneID; 945293; -. 5507DR GenomeReviews; AP009048_GR; JW0671. 5508DR GenomeReviews; U00096_GR; b0684. 5509DR KEGG; eco:b0684; -. 5510DR PATRIC; 32116561; VBIEscCol129921_0713. 5511DR EchoBASE; EB0314; -. 5512DR EcoGene; EG10318; fldA. 5513DR eggNOG; COG0716; -. 5514DR HOGENOM; HOG000030543; -. 5515DR KO; K03839; -. 5516DR OMA; DDKHFVG; -. 5517DR ProtClustDB; PRK09267; -. 5518DR BioCyc; EcoCyc:FLAVODOXIN1-MONOMER; -. 5519DR EvolutionaryTrace; P61949; -. 5520DR Genevestigator; P61949; -. 5521DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki. 5522DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5523DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5524DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5525DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5526DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5527DR InterPro; IPR008254; Flavodoxin/NO_synth. 5528DR InterPro; IPR001226; Flavodoxin_CS. 5529DR InterPro; IPR010086; Flavodoxin_lc. 5530DR Pfam; PF00258; Flavodoxin_1; 1. 5531DR TIGRFAMs; TIGR01752; Flav_long; 1. 5532DR PROSITE; PS00201; FLAVODOXIN; 1. 5533DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5534PE 1: Evidence at protein level; 5535KW 3D-structure; Complete proteome; Direct protein sequencing; 5536KW Electron transport; Flavoprotein; FMN; Reference proteome; Transport. 5537FT INIT_MET 1 1 Removed. 5538FT CHAIN 2 176 Flavodoxin-1. 5539FT /FTId=PRO_0000171622. 5540FT DOMAIN 4 165 Flavodoxin-like. 5541FT STRAND 4 8 5542FT STRAND 11 13 5543FT HELIX 14 26 5544FT TURN 28 30 5545FT STRAND 31 35 5546FT HELIX 36 38 5547FT HELIX 41 45 5548FT STRAND 48 53 5549FT TURN 58 60 5550FT HELIX 64 73 5551FT STRAND 82 88 5552FT TURN 91 96 5553FT HELIX 100 109 5554FT TURN 110 113 5555FT STRAND 133 135 5556FT STRAND 138 144 5557FT TURN 146 148 5558FT TURN 150 152 5559FT HELIX 153 168 5560FT HELIX 170 173 5561SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; 5562 MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG 5563 EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW 5564 PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA 5565// 5566ID FLAV_ENTAG Reviewed; 177 AA. 5567AC P28579; 5568DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. 5569DT 01-DEC-1992, sequence version 1. 5570DT 21-SEP-2011, entry version 56. 5571DE RecName: Full=Flavodoxin; 5572GN Name=nifF; 5573OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans). 5574OG Plasmid pEA3. 5575OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 5576OC Enterobacteriaceae; Pantoea. 5577OX NCBI_TaxID=549; 5578RN [1] 5579RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 5580RC STRAIN=333; 5581RX MEDLINE=91217003; PubMed=1708766; 5582RA Kreutzer R., Dayananda S., Klingmueller W.; 5583RT "Cotranscription of the electron transport protein genes nifJ and nifF 5584RT in Enterobacter agglomerans 333."; 5585RL J. Bacteriol. 173:3252-3256(1991). 5586RN [2] 5587RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. 5588RC STRAIN=333; 5589RA Schwickerath O.; 5590RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. 5591CC -!- FUNCTION: Low-potential electron donor to a number of redox 5592CC enzymes. NifF is the electron donor to nitrogenase. 5593CC -!- COFACTOR: FMN. 5594CC -!- SIMILARITY: Belongs to the flavodoxin family. 5595CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5596CC ----------------------------------------------------------------------- 5597CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5598CC Distributed under the Creative Commons Attribution-NoDerivs License 5599CC ----------------------------------------------------------------------- 5600DR EMBL; M38221; AAA23385.1; -; Genomic_DNA. 5601DR EMBL; X99694; CAA68010.1; -; Genomic_DNA. 5602DR EMBL; X78558; CAA55301.1; -; Genomic_DNA. 5603DR PIR; A39414; A39414. 5604DR ProteinModelPortal; P28579; -. 5605DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5606DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5607DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 5608DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5609DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5610DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW. 5611DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5612DR InterPro; IPR001094; Flavdoxin. 5613DR InterPro; IPR008254; Flavodoxin/NO_synth. 5614DR InterPro; IPR001226; Flavodoxin_CS. 5615DR InterPro; IPR010086; Flavodoxin_lc. 5616DR Pfam; PF00258; Flavodoxin_1; 1. 5617DR PRINTS; PR00369; FLAVODOXIN. 5618DR TIGRFAMs; TIGR01752; Flav_long; 1. 5619DR PROSITE; PS00201; FLAVODOXIN; 1. 5620DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5621PE 3: Inferred from homology; 5622KW Electron transport; Flavoprotein; FMN; Nitrogen fixation; Plasmid; 5623KW Transport. 5624FT CHAIN 1 177 Flavodoxin. 5625FT /FTId=PRO_0000171631. 5626FT DOMAIN 4 173 Flavodoxin-like. 5627SQ SEQUENCE 177 AA; 19581 MW; 3D54F95F7EC60B41 CRC64; 5628 MATIGIFFGS DTGQTRKVAK LIHQKLDGIA DAPLDVRRAT REQFLSYPVL LLGTPTLGDG 5629 ELPGVEAGSQ YDSWQEFTNT LSEADLTGKT VALFGLGDQL NYSKNFVSAM RILYDLVIAR 5630 GACVVGNWPR EGYKFSFSAA LLENNEFVGL PLDQENQYDL TEERIDSWLE KLKPAVL 5631// 5632ID FLAV_HAEIN Reviewed; 174 AA. 5633AC P44562; 5634DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. 5635DT 23-JAN-2007, sequence version 2. 5636DT 16-MAY-2012, entry version 81. 5637DE RecName: Full=Flavodoxin; 5638GN Name=fldA; OrderedLocusNames=HI_0191; 5639OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). 5640OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; 5641OC Pasteurellaceae; Haemophilus. 5642OX NCBI_TaxID=71421; 5643RN [1] 5644RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5645RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; 5646RX MEDLINE=95350630; PubMed=7542800; DOI=10.1126/science.7542800; 5647RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., 5648RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., 5649RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., 5650RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., 5651RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., 5652RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., 5653RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., 5654RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., 5655RA Venter J.C.; 5656RT "Whole-genome random sequencing and assembly of Haemophilus influenzae 5657RT Rd."; 5658RL Science 269:496-512(1995). 5659CC -!- FUNCTION: Low-potential electron donor to a number of redox 5660CC enzymes (By similarity). 5661CC -!- COFACTOR: FMN (By similarity). 5662CC -!- SIMILARITY: Belongs to the flavodoxin family. 5663CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5664CC ----------------------------------------------------------------------- 5665CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5666CC Distributed under the Creative Commons Attribution-NoDerivs License 5667CC ----------------------------------------------------------------------- 5668DR EMBL; L42023; AAC21860.1; -; Genomic_DNA. 5669DR PIR; C64053; C64053. 5670DR RefSeq; NP_438360.1; NC_000907.1. 5671DR ProteinModelPortal; P44562; -. 5672DR SMR; P44562; 2-173. 5673DR GeneID; 951101; -. 5674DR GenomeReviews; L42023_GR; HI_0191. 5675DR KEGG; hin:HI0191; -. 5676DR PATRIC; 20188879; VBIHaeInf48452_0196. 5677DR TIGR; HI_0191; -. 5678DR eggNOG; COG0716; -. 5679DR KO; K03839; -. 5680DR OMA; DDKHFVG; -. 5681DR ProtClustDB; PRK09267; -. 5682DR BioCyc; HINF71421:HI_0191-MONOMER; -. 5683DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5684DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5685DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5686DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5687DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5688DR InterPro; IPR008254; Flavodoxin/NO_synth. 5689DR InterPro; IPR001226; Flavodoxin_CS. 5690DR InterPro; IPR010086; Flavodoxin_lc. 5691DR Pfam; PF00258; Flavodoxin_1; 1. 5692DR TIGRFAMs; TIGR01752; Flav_long; 1. 5693DR PROSITE; PS00201; FLAVODOXIN; 1. 5694DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5695PE 3: Inferred from homology; 5696KW Complete proteome; Electron transport; Flavoprotein; FMN; 5697KW Reference proteome; Transport. 5698FT INIT_MET 1 1 Removed (By similarity). 5699FT CHAIN 2 174 Flavodoxin. 5700FT /FTId=PRO_0000171633. 5701FT DOMAIN 4 165 Flavodoxin-like. 5702SQ SEQUENCE 174 AA; 19627 MW; 5E95E895F04BF3F8 CRC64; 5703 MAIVGLFYGS DTGNTENIAK QIQKQLGSDL IDIRDIAKSS KEDIEAYDFL LFGIPTWYYG 5704 EAQADWDDFF PTLEEIDFTD KLVGIFGCGD QEDYADYFCD AIGTVRDIIE PHGAIVVGNW 5705 PTEGYNFEAS KALLEDGTFI GLCIDEDRQP ELTAERVEKW CKQIYDEMCL AELA 5706// 5707ID FLAV_HELPY Reviewed; 164 AA. 5708AC O25776; 5709DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 5710DT 01-JAN-1998, sequence version 1. 5711DT 16-MAY-2012, entry version 78. 5712DE RecName: Full=Flavodoxin; 5713GN Name=fldA; OrderedLocusNames=HP_1161; 5714OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter 5715OS pylori). 5716OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; 5717OC Helicobacteraceae; Helicobacter. 5718OX NCBI_TaxID=85962; 5719RN [1] 5720RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 5721RC STRAIN=ATCC 700392 / 26695; 5722RX MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483; 5723RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., 5724RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., 5725RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., 5726RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., 5727RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., 5728RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., 5729RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., 5730RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., 5731RA Smith H.O., Fraser C.M., Venter J.C.; 5732RT "The complete genome sequence of the gastric pathogen Helicobacter 5733RT pylori."; 5734RL Nature 388:539-547(1997). 5735CC -!- FUNCTION: Low-potential electron donor to a number of redox 5736CC enzymes (By similarity). 5737CC -!- COFACTOR: FMN (By similarity). 5738CC -!- SIMILARITY: Belongs to the flavodoxin family. 5739CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5740CC ----------------------------------------------------------------------- 5741CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5742CC Distributed under the Creative Commons Attribution-NoDerivs License 5743CC ----------------------------------------------------------------------- 5744DR EMBL; AE000511; AAD08207.1; -; Genomic_DNA. 5745DR PIR; A64665; A64665. 5746DR RefSeq; NP_207952.1; NC_000915.1. 5747DR PDB; 2BMV; X-ray; 2.11 A; A=1-164. 5748DR PDB; 2W5U; X-ray; 2.62 A; A/B=1-164. 5749DR PDBsum; 2BMV; -. 5750DR PDBsum; 2W5U; -. 5751DR ProteinModelPortal; O25776; -. 5752DR SMR; O25776; 2-164. 5753DR GeneID; 899921; -. 5754DR GenomeReviews; AE000511_GR; HP_1161. 5755DR KEGG; hpy:HP1161; -. 5756DR PATRIC; 20593673; VBIHelPyl33062_1215. 5757DR TIGR; HP_1161; -. 5758DR eggNOG; COG0716; -. 5759DR KO; K03839; -. 5760DR OMA; DDKHFVG; -. 5761DR ProtClustDB; PRK09267; -. 5762DR EvolutionaryTrace; O25776; -. 5763DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5764DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5765DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5766DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5767DR InterPro; IPR008254; Flavodoxin/NO_synth. 5768DR InterPro; IPR010086; Flavodoxin_lc. 5769DR Pfam; PF00258; Flavodoxin_1; 1. 5770DR TIGRFAMs; TIGR01752; Flav_long; 1. 5771DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. 5772DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5773PE 1: Evidence at protein level; 5774KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; 5775KW FMN; Reference proteome; Transport. 5776FT CHAIN 1 164 Flavodoxin. 5777FT /FTId=PRO_0000171634. 5778FT DOMAIN 4 160 Flavodoxin-like. 5779FT STRAND 4 8 5780FT STRAND 11 13 5781FT HELIX 14 26 5782FT STRAND 28 33 5783FT HELIX 34 36 5784FT HELIX 39 42 5785FT STRAND 46 55 5786FT TURN 56 58 5787FT HELIX 62 68 5788FT HELIX 74 77 5789FT STRAND 79 86 5790FT TURN 89 91 5791FT TURN 96 98 5792FT HELIX 99 107 5793FT STRAND 110 112 5794FT STRAND 116 118 5795FT STRAND 133 139 5796FT TURN 141 143 5797FT HELIX 145 147 5798FT HELIX 148 159 5799FT TURN 160 162 5800SQ SEQUENCE 164 AA; 17492 MW; EBAD44D97964608C CRC64; 5801 MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VVDVAKASKE QFNSFTKVIL VAPTAGAGDL 5802 QTDWEDFLGT LEASDFATKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG 5803 YHFEASKAVE GGKFVGLVID EDNQDDLTDE RISKWVEQVK GSFA 5804// 5805ID FLAV_KLEPN Reviewed; 176 AA. 5806AC O07026; 5807DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 5808DT 15-JUL-1999, sequence version 2. 5809DT 31-MAY-2011, entry version 47. 5810DE RecName: Full=Flavodoxin; 5811GN Name=fldA; 5812OS Klebsiella pneumoniae. 5813OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 5814OC Enterobacteriaceae; Klebsiella. 5815OX NCBI_TaxID=573; 5816RN [1] 5817RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. 5818RC STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / 5819RC NCTC 9633; 5820RX MEDLINE=97417492; PubMed=9272865; DOI=10.1016/S0378-1119(97)00168-6; 5821RA Achenbach L.A., Genova E.G.; 5822RT "Transcriptional regulation of a second flavodoxin gene from 5823RT Klebsiella pneumoniae."; 5824RL Gene 194:235-240(1997). 5825RN [2] 5826RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-176. 5827RC STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 / 5828RC NCTC 9633; 5829RX MEDLINE=97208874; PubMed=9055816; DOI=10.1016/S0378-1119(96)00642-7; 5830RA Achenbach L.A., Yang W.; 5831RT "The fur gene from Klebsiella pneumoniae: characterization, genomic 5832RT organization and phylogenetic analysis."; 5833RL Gene 185:201-207(1997). 5834CC -!- FUNCTION: Low-potential electron donor to a number of redox 5835CC enzymes (By similarity). 5836CC -!- COFACTOR: FMN (By similarity). 5837CC -!- INDUCTION: By low iron conditions and by heat shock. Iron 5838CC regulation is mediated through the fur protein. 5839CC -!- SIMILARITY: Belongs to the flavodoxin family. 5840CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5841CC ----------------------------------------------------------------------- 5842CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5843CC Distributed under the Creative Commons Attribution-NoDerivs License 5844CC ----------------------------------------------------------------------- 5845DR EMBL; U67169; AAB65080.1; -; Genomic_DNA. 5846DR EMBL; L23871; AAB51076.1; -; Genomic_DNA. 5847DR ProteinModelPortal; O07026; -. 5848DR SMR; O07026; 2-176. 5849DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5850DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5851DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5852DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5853DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5854DR InterPro; IPR008254; Flavodoxin/NO_synth. 5855DR InterPro; IPR001226; Flavodoxin_CS. 5856DR InterPro; IPR010086; Flavodoxin_lc. 5857DR Pfam; PF00258; Flavodoxin_1; 1. 5858DR TIGRFAMs; TIGR01752; Flav_long; 1. 5859DR PROSITE; PS00201; FLAVODOXIN; 1. 5860DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5861PE 2: Evidence at transcript level; 5862KW Electron transport; Flavoprotein; FMN; Transport. 5863FT CHAIN 1 176 Flavodoxin. 5864FT /FTId=PRO_0000171636. 5865FT DOMAIN 4 165 Flavodoxin-like. 5866SQ SEQUENCE 176 AA; 19765 MW; C40E5F80287D3636 CRC64; 5867 MAIIGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAHDIL LLGIPTWYYG 5868 EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW 5869 PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTNERVEKW VKQVAEELHL EEIKNA 5870// 5871ID FLAV_MEGEL Reviewed; 137 AA. 5872AC P00321; 5873DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 5874DT 21-JUL-1986, sequence version 1. 5875DT 18-APR-2012, entry version 66. 5876DE RecName: Full=Flavodoxin; 5877OS Megasphaera elsdenii. 5878OC Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae; 5879OC Megasphaera. 5880OX NCBI_TaxID=907; 5881RN [1] 5882RP PROTEIN SEQUENCE. 5883RC STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927; 5884RX MEDLINE=73197809; PubMed=4711610; 5885RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.; 5886RT "The primary structure of Peptostreptococcus elsdenii flavodoxin."; 5887RL J. Biol. Chem. 248:4354-4366(1973). 5888RN [2] 5889RP SEQUENCE REVISION TO 78-82. 5890RX MEDLINE=74277393; PubMed=4843143; 5891RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.; 5892RT "Correction of the amino acid sequence of Peptostreptococcus elsdenii 5893RT flavodoxin."; 5894RL J. Biol. Chem. 249:4397-4397(1974). 5895RN [3] 5896RP PROTEIN SEQUENCE OF 1-41 AND 136-137. 5897RC STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927; 5898RX MEDLINE=72062407; PubMed=5126921; DOI=10.1021/bi00792a009; 5899RA Tanaka M., Haniu M., Matsueda G., Yasunobu K.T., Mayhew S., Massey V.; 5900RT "Amino- and carboxyl-terminal amino acid sequences of the 5901RT Peptostreptococcus eisdenii and Clostridium pasteurianum 5902RT flavodoxins."; 5903RL Biochemistry 10:3041-3046(1971). 5904RN [4] 5905RP STRUCTURE BY NMR. 5906RX MEDLINE=90276429; PubMed=2161759; 5907RX DOI=10.1111/j.1432-1033.1990.tb15527.x; 5908RA van Mierlo C.P.M., Mueller F., Vervoort J.; 5909RT "Secondary and tertiary structure characteristics of Megasphaera 5910RT elsdenii flavodoxin in the reduced state as determined by two- 5911RT dimensional 1H NMR."; 5912RL Eur. J. Biochem. 189:589-600(1990). 5913RN [5] 5914RP STRUCTURE BY NMR. 5915RX MEDLINE=91071190; PubMed=2253614; 5916RX DOI=10.1111/j.1432-1033.1990.tb19444.x; 5917RA van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F., 5918RA Berendsen H.J.C., de Vlieg J.; 5919RT "Tertiary structure of two-electron reduced Megasphaera elsdenii 5920RT flavodoxin and some implications, as determined by two-dimensional 1H- 5921RT NMR and restrained molecular dynamics."; 5922RL Eur. J. Biochem. 194:185-198(1990). 5923CC -!- FUNCTION: Low-potential electron donor to a number of redox 5924CC enzymes. 5925CC -!- COFACTOR: FMN. 5926CC -!- SIMILARITY: Belongs to the flavodoxin family. 5927CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5928CC ----------------------------------------------------------------------- 5929CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5930CC Distributed under the Creative Commons Attribution-NoDerivs License 5931CC ----------------------------------------------------------------------- 5932DR PIR; A92137; FXME. 5933DR PDB; 2FZ5; NMR; -; A=1-137. 5934DR PDBsum; 2FZ5; -. 5935DR ProteinModelPortal; P00321; -. 5936DR SMR; P00321; 1-137. 5937DR EvolutionaryTrace; P00321; -. 5938DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 5939DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 5940DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 5941DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 5942DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 5943DR InterPro; IPR010087; Flav_short. 5944DR InterPro; IPR008254; Flavodoxin/NO_synth. 5945DR InterPro; IPR001226; Flavodoxin_CS. 5946DR Pfam; PF00258; Flavodoxin_1; 1. 5947DR TIGRFAMs; TIGR01753; Flav_short; 1. 5948DR PROSITE; PS00201; FLAVODOXIN; 1. 5949DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 5950PE 1: Evidence at protein level; 5951KW 3D-structure; Direct protein sequencing; Electron transport; 5952KW Flavoprotein; FMN; Transport. 5953FT CHAIN 1 137 Flavodoxin. 5954FT /FTId=PRO_0000171639. 5955FT DOMAIN 2 137 Flavodoxin-like. 5956FT STRAND 2 6 5957FT STRAND 9 11 5958FT HELIX 12 26 5959FT STRAND 31 35 5960FT HELIX 41 45 5961FT STRAND 48 53 5962FT TURN 58 60 5963FT HELIX 64 74 5964FT HELIX 75 77 5965FT STRAND 82 91 5966FT HELIX 95 106 5967FT STRAND 110 123 5968FT HELIX 126 135 5969SQ SEQUENCE 137 AA; 14550 MW; 86BD744412D6F869 CRC64; 5970 MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE 5971 ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM 5972 PDNAPECKEL GEAAAKA 5973// 5974ID FLAV_NOSSM Reviewed; 35 AA. 5975AC P35707; 5976DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. 5977DT 01-JUN-1994, sequence version 1. 5978DT 19-JAN-2010, entry version 39. 5979DE RecName: Full=Flavodoxin; 5980DE Flags: Fragment; 5981OS Nostoc sp. (strain MAC). 5982OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. 5983OX NCBI_TaxID=35822; 5984RN [1] 5985RP PROTEIN SEQUENCE. 5986RA Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.; 5987RT "N-terminal amino acid sequences of flavodoxins from Chondrus crispus 5988RT and Nostoc strain MAC."; 5989RL Phytochemistry 25:2113-2115(1986). 5990CC -!- FUNCTION: Low-potential electron donor to a number of redox 5991CC enzymes. 5992CC -!- COFACTOR: FMN. 5993CC -!- SIMILARITY: Belongs to the flavodoxin family. 5994CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 5995CC ----------------------------------------------------------------------- 5996CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 5997CC Distributed under the Creative Commons Attribution-NoDerivs License 5998CC ----------------------------------------------------------------------- 5999DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6000DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6001DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6002DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6003DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6004DR InterPro; IPR008254; Flavodoxin/NO_synth. 6005DR InterPro; IPR001226; Flavodoxin_CS. 6006DR PROSITE; PS00201; FLAVODOXIN; 1. 6007DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6008PE 1: Evidence at protein level; 6009KW Direct protein sequencing; Electron transport; Flavoprotein; FMN; 6010KW Transport. 6011FT CHAIN 1 >35 Flavodoxin. 6012FT /FTId=PRO_0000171640. 6013FT DOMAIN 4 >35 Flavodoxin-like. 6014FT NON_TER 35 35 6015SQ SEQUENCE 35 AA; 3820 MW; B6EEB5CA7A45DDA6 CRC64; 6016 SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID 6017// 6018ID FLAV_RHOCB Reviewed; 182 AA. 6019AC P52967; D5AT59; 6020DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 6021DT 28-JUN-2011, sequence version 3. 6022DT 16-MAY-2012, entry version 62. 6023DE RecName: Full=Flavodoxin; 6024GN Name=nifF; Synonyms=fldA; OrderedLocusNames=RCAP_rcc01421; 6025OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). 6026OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; 6027OC Rhodobacteraceae; Rhodobacter. 6028OX NCBI_TaxID=272942; 6029RN [1] 6030RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 6031RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; 6032RX MEDLINE=96272272; PubMed=8682802; 6033RA Gennaro G., Huebner P., Sandmeier U., Yakunin A.F., Hallenbeck P.C.; 6034RT "Cloning, characterization, and regulation of nifF from Rhodobacter 6035RT capsulatus."; 6036RL J. Bacteriol. 178:3949-3952(1996). 6037RN [2] 6038RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6039RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; 6040RX PubMed=20418398; DOI=10.1128/JB.00366-10; 6041RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., 6042RA Haselkorn R.; 6043RT "Complete genome sequence of the photosynthetic purple nonsulfur 6044RT bacterium Rhodobacter capsulatus SB 1003."; 6045RL J. Bacteriol. 192:3545-3546(2010). 6046CC -!- FUNCTION: Low-potential electron donor to a number of redox 6047CC enzymes. NifF is the electron donor to nitrogenase. 6048CC -!- COFACTOR: FMN. 6049CC -!- SIMILARITY: Belongs to the flavodoxin family. 6050CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6051CC ----------------------------------------------------------------------- 6052CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6053CC Distributed under the Creative Commons Attribution-NoDerivs License 6054CC ----------------------------------------------------------------------- 6055DR EMBL; L42290; AAC05792.1; -; Genomic_DNA. 6056DR EMBL; CP001312; ADE85166.1; -; Genomic_DNA. 6057DR RefSeq; YP_003577573.1; NC_014034.1. 6058DR PDB; 2WC1; X-ray; 2.17 A; A=1-182. 6059DR PDBsum; 2WC1; -. 6060DR ProteinModelPortal; P52967; -. 6061DR GeneID; 9004244; -. 6062DR KEGG; rcp:RCAP_rcc01421; -. 6063DR PATRIC; 35502944; VBIRhoCap134200_1432. 6064DR HOGENOM; HOG000030543; -. 6065DR KO; K03839; -. 6066DR EvolutionaryTrace; P52967; -. 6067DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6068DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6069DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 6070DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6071DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6072DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW. 6073DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6074DR InterPro; IPR001094; Flavdoxin. 6075DR InterPro; IPR008254; Flavodoxin/NO_synth. 6076DR InterPro; IPR001226; Flavodoxin_CS. 6077DR InterPro; IPR010086; Flavodoxin_lc. 6078DR Pfam; PF00258; Flavodoxin_1; 1. 6079DR PRINTS; PR00369; FLAVODOXIN. 6080DR TIGRFAMs; TIGR01752; Flav_long; 1. 6081DR PROSITE; PS00201; FLAVODOXIN; 1. 6082DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6083PE 1: Evidence at protein level; 6084KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; 6085KW FMN; Nitrogen fixation; Transport. 6086FT INIT_MET 1 1 Removed (By similarity). 6087FT CHAIN 2 182 Flavodoxin. 6088FT /FTId=PRO_0000171641. 6089FT DOMAIN 4 173 Flavodoxin-like. 6090FT CONFLICT 124 125 KL -> NV (in Ref. 1; AAC05792). 6091FT STRAND 6 8 6092FT HELIX 15 23 6093FT TURN 28 30 6094FT STRAND 31 36 6095FT HELIX 37 39 6096FT HELIX 42 47 6097FT STRAND 49 53 6098FT HELIX 75 78 6099FT HELIX 79 82 6100FT STRAND 91 94 6101FT TURN 100 102 6102FT TURN 107 109 6103FT HELIX 110 119 6104FT STRAND 124 126 6105FT TURN 154 156 6106FT HELIX 158 160 6107FT HELIX 161 165 6108FT TURN 169 175 6109SQ SEQUENCE 182 AA; 19848 MW; 955F326BBF27213E CRC64; 6110 MAKIGLFFGS DTGTTRKIAK QIKDMFDDEV MAKPLNVNRA DVADFMAYDF LILGTPTLGD 6111 GQLPGLSANA ASESWEEFLP RIADQDFSGK TIALFGLGDQ VTYPLEFVNA LFFLHEFFSD 6112 RGAKLVGRWP AKGYGFEDSL AVVEGEFLGL ALDQDNQAAL TPERLKGWLS LIAADFGLVL 6113 PA 6114// 6115ID FLAV_SYNE7 Reviewed; 170 AA. 6116AC P10340; Q31MZ8; 6117DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. 6118DT 23-JAN-2007, sequence version 3. 6119DT 16-MAY-2012, entry version 97. 6120DE RecName: Full=Flavodoxin; 6121GN Name=isiB; OrderedLocusNames=Synpcc7942_1541; 6122OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2). 6123OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. 6124OX NCBI_TaxID=1140; 6125RN [1] 6126RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 6127RX MEDLINE=88086879; PubMed=3121586; 6128RA Laudenbach D.E., Reith M.E., Straus N.A.; 6129RT "Isolation, sequence analysis, and transcriptional studies of the 6130RT flavodoxin gene from Anacystis nidulans R2."; 6131RL J. Bacteriol. 170:258-265(1988). 6132RN [2] 6133RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6134RC STRAIN=PCC 7942; 6135RG US DOE Joint Genome Institute; 6136RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., 6137RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., 6138RA Kyrpides N., Lykidis A., Richardson P.; 6139RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 6140RT 7942."; 6141RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. 6142RN [3] 6143RP PROTEIN SEQUENCE OF 2-56, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). 6144RX MEDLINE=83216115; PubMed=6406674; DOI=10.1016/S0022-2836(83)80277-0; 6145RA Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D., 6146RA Tanaka M., Yasunobu K.T.; 6147RT "Structure of oxidized flavodoxin from Anacystis nidulans."; 6148RL J. Mol. Biol. 165:737-753(1983). 6149RN [4] 6150RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). 6151RX MEDLINE=20079529; PubMed=10610791; DOI=10.1006/jmbi.1999.3151; 6152RA Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M., 6153RA Ludwig M.L.; 6154RT "Refined structures of oxidized flavodoxin from Anacystis nidulans."; 6155RL J. Mol. Biol. 294:711-724(1999). 6156RN [5] 6157RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS). 6158RX MEDLINE=20079530; PubMed=10610792; DOI=10.1006/jmbi.1999.3152; 6159RA Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H., 6160RA Pattridge K.A., Ludwig M.L.; 6161RT "Comparisons of wild-type and mutant flavodoxins from Anacystis 6162RT nidulans. Structural determinants of the redox potentials."; 6163RL J. Mol. Biol. 294:725-743(1999). 6164RN [6] 6165RP STRUCTURE BY NMR. 6166RX MEDLINE=91329335; PubMed=1907844; DOI=10.1021/bi00245a008; 6167RA Clubb R.T., Thanabal V., Osborne C., Wagner G.; 6168RT "1H and 15N resonance assignments of oxidized flavodoxin from 6169RT Anacystis nidulans with 3D NMR."; 6170RL Biochemistry 30:7718-7730(1991). 6171CC -!- FUNCTION: Low-potential electron donor to a number of redox 6172CC enzymes. 6173CC -!- COFACTOR: FMN. 6174CC -!- INDUCTION: By iron stress. 6175CC -!- SIMILARITY: Belongs to the flavodoxin family. 6176CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6177CC ----------------------------------------------------------------------- 6178CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6179CC Distributed under the Creative Commons Attribution-NoDerivs License 6180CC ----------------------------------------------------------------------- 6181DR EMBL; M19116; AAA22050.1; -; Genomic_DNA. 6182DR EMBL; CP000100; ABB57571.1; -; Genomic_DNA. 6183DR RefSeq; YP_170711.1; NC_006576.1. 6184DR RefSeq; YP_400558.1; NC_007604.1. 6185DR PDB; 1CZH; X-ray; 1.86 A; A=2-170. 6186DR PDB; 1CZK; X-ray; 1.90 A; A=2-170. 6187DR PDB; 1CZL; X-ray; 1.80 A; A=2-170. 6188DR PDB; 1CZN; X-ray; 1.70 A; A=2-170. 6189DR PDB; 1CZO; X-ray; 1.85 A; A=2-170. 6190DR PDB; 1CZR; X-ray; 1.90 A; A=2-170. 6191DR PDB; 1CZU; X-ray; 2.00 A; A=2-170. 6192DR PDB; 1D03; X-ray; 1.85 A; A=2-170. 6193DR PDB; 1D04; X-ray; 1.85 A; A=2-170. 6194DR PDB; 1OFV; X-ray; 1.70 A; A=2-170. 6195DR PDBsum; 1CZH; -. 6196DR PDBsum; 1CZK; -. 6197DR PDBsum; 1CZL; -. 6198DR PDBsum; 1CZN; -. 6199DR PDBsum; 1CZO; -. 6200DR PDBsum; 1CZR; -. 6201DR PDBsum; 1CZU; -. 6202DR PDBsum; 1D03; -. 6203DR PDBsum; 1D04; -. 6204DR PDBsum; 1OFV; -. 6205DR ProteinModelPortal; P10340; -. 6206DR SMR; P10340; 2-170. 6207DR STRING; P10340; -. 6208DR GeneID; 3199676; -. 6209DR GeneID; 3774965; -. 6210DR GenomeReviews; CP000100_GR; Synpcc7942_1541. 6211DR KEGG; syc:syc0001_c; -. 6212DR KEGG; syf:Synpcc7942_1541; -. 6213DR PATRIC; 23788451; VBISynElo51371_1750. 6214DR eggNOG; COG0716; -. 6215DR HOGENOM; HOG000030543; -. 6216DR KO; K03839; -. 6217DR ProtClustDB; PRK09267; -. 6218DR BioCyc; SYNEL:SYNPCC7942_1541-MONOMER; -. 6219DR EvolutionaryTrace; P10340; -. 6220DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6221DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6222DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6223DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6224DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. 6225DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6226DR InterPro; IPR008254; Flavodoxin/NO_synth. 6227DR InterPro; IPR001226; Flavodoxin_CS. 6228DR InterPro; IPR010086; Flavodoxin_lc. 6229DR Pfam; PF00258; Flavodoxin_1; 1. 6230DR TIGRFAMs; TIGR01752; Flav_long; 1. 6231DR PROSITE; PS00201; FLAVODOXIN; 1. 6232DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6233PE 1: Evidence at protein level; 6234KW 3D-structure; Complete proteome; Direct protein sequencing; 6235KW Electron transport; Flavoprotein; FMN; Stress response; Transport. 6236FT INIT_MET 1 1 Removed. 6237FT CHAIN 2 170 Flavodoxin. 6238FT /FTId=PRO_0000171644. 6239FT DOMAIN 4 165 Flavodoxin-like. 6240FT CONFLICT 55 55 C -> S (in Ref. 3; AA sequence). 6241FT STRAND 4 8 6242FT STRAND 11 13 6243FT HELIX 14 26 6244FT TURN 29 31 6245FT STRAND 32 36 6246FT HELIX 37 39 6247FT HELIX 42 47 6248FT STRAND 49 54 6249FT TURN 59 61 6250FT HELIX 65 70 6251FT HELIX 71 76 6252FT STRAND 83 89 6253FT TURN 92 97 6254FT HELIX 101 111 6255FT TURN 112 114 6256FT STRAND 121 123 6257FT STRAND 138 144 6258FT TURN 146 148 6259FT HELIX 150 152 6260FT HELIX 153 168 6261SQ SEQUENCE 170 AA; 18778 MW; 7291AEF23DCA0345 CRC64; 6262 MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY LIIGCPTWNV 6263 GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ DAMGILEEKI SSLGSQTVGY 6264 WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP DLTKNRIKTW VSQLKSEFGL 6265// 6266ID FLAV_SYNP2 Reviewed; 170 AA. 6267AC P31158; B1XL33; 6268DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. 6269DT 23-JAN-2007, sequence version 2. 6270DT 16-MAY-2012, entry version 69. 6271DE RecName: Full=Flavodoxin; 6272GN Name=isiB; OrderedLocusNames=SYNPCC7002_A1291; 6273OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum 6274OS quadruplicatum). 6275OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. 6276OX NCBI_TaxID=32049; 6277RN [1] 6278RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 6279RX MEDLINE=92407507; PubMed=1527503; 6280RA Leonhardt K.G., Straus N.A.; 6281RT "An iron stress operon involved in photosynthetic electron transport 6282RT in the marine cyanobacterium Synechococcus sp. PCC 7002."; 6283RL J. Gen. Microbiol. 138:1613-1621(1992). 6284RN [2] 6285RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6286RC STRAIN=ATCC 27264 / PCC 7002 / PR-6; 6287RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., 6288RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., 6289RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.; 6290RT "Complete sequence of Synechococcus sp. PCC 7002."; 6291RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 6292CC -!- FUNCTION: Low-potential electron donor to a number of redox 6293CC enzymes. 6294CC -!- COFACTOR: FMN. 6295CC -!- INDUCTION: By iron stress. 6296CC -!- SIMILARITY: Belongs to the flavodoxin family. 6297CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6298CC ----------------------------------------------------------------------- 6299CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6300CC Distributed under the Creative Commons Attribution-NoDerivs License 6301CC ----------------------------------------------------------------------- 6302DR EMBL; M88253; AAA27318.1; -; Genomic_DNA. 6303DR EMBL; CP000951; ACA99288.1; -; Genomic_DNA. 6304DR RefSeq; YP_001734544.1; NC_010475.1. 6305DR ProteinModelPortal; P31158; -. 6306DR SMR; P31158; 2-170. 6307DR STRING; P31158; -. 6308DR GeneID; 6055593; -. 6309DR GenomeReviews; CP000951_GR; SYNPCC7002_A1291. 6310DR KEGG; syp:SYNPCC7002_A1291; -. 6311DR PATRIC; 23817150; VBISynSp37135_1525. 6312DR eggNOG; COG0716; -. 6313DR HOGENOM; HOG000030543; -. 6314DR KO; K03839; -. 6315DR OMA; FTETAGY; -. 6316DR ProtClustDB; PRK09267; -. 6317DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6318DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6319DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6320DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6321DR GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW. 6322DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6323DR InterPro; IPR008254; Flavodoxin/NO_synth. 6324DR InterPro; IPR001226; Flavodoxin_CS. 6325DR InterPro; IPR010086; Flavodoxin_lc. 6326DR Pfam; PF00258; Flavodoxin_1; 1. 6327DR TIGRFAMs; TIGR01752; Flav_long; 1. 6328DR PROSITE; PS00201; FLAVODOXIN; 1. 6329DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6330PE 2: Evidence at transcript level; 6331KW Complete proteome; Electron transport; Flavoprotein; FMN; 6332KW Stress response; Transport. 6333FT INIT_MET 1 1 Removed (By similarity). 6334FT CHAIN 2 170 Flavodoxin. 6335FT /FTId=PRO_0000171643. 6336FT DOMAIN 4 165 Flavodoxin-like. 6337SQ SEQUENCE 170 AA; 18479 MW; FFBB605F69E701BA CRC64; 6338 MSKIGLFFGT QTGNTEELAQ AIQAAFGGSD IVELFDVAEV DIEALRDFDQ LIIGCPTWNV 6339 GELQSDWEAL YDDLDDVDFS GKTIAYFGAG DQVGYADNFQ DAMGVLEEKI TSLGGKTVGQ 6340 WPTAGYDHSE SKAERDGKFV GLAIDEDNQP ELTAERIQAW VAQLKPAFGL 6341// 6342ID FLAV_SYNY3 Reviewed; 170 AA. 6343AC P27319; 6344DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. 6345DT 01-JUN-1994, sequence version 2. 6346DT 13-JUN-2012, entry version 88. 6347DE RecName: Full=Flavodoxin; 6348GN Name=isiB; OrderedLocusNames=sll0248; 6349OS Synechocystis sp. (strain PCC 6803 / Kazusa). 6350OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. 6351OX NCBI_TaxID=1111708; 6352RN [1] 6353RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 6354RX MEDLINE=94320780; PubMed=8045418; DOI=10.1016/0378-1119(94)90342-5; 6355RA Poncelet M.G.M., Cassier-Chauvat C.J.S., Chauvat F.R.L.; 6356RT "Sequence of the flavodoxin-encoding gene from the cyanobacterium 6357RT Synechocystis PCC6803."; 6358RL Gene 145:153-154(1994). 6359RN [2] 6360RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6361RC STRAIN=PCC 6803 / Kazusa; 6362RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109; 6363RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., 6364RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., 6365RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., 6366RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., 6367RA Tabata S.; 6368RT "Sequence analysis of the genome of the unicellular cyanobacterium 6369RT Synechocystis sp. strain PCC6803. II. Sequence determination of the 6370RT entire genome and assignment of potential protein-coding regions."; 6371RL DNA Res. 3:109-136(1996). 6372RN [3] 6373RP PROTEIN SEQUENCE OF 1-42. 6374RX MEDLINE=92338182; PubMed=1633177; DOI=10.1016/0167-4838(92)90465-P; 6375RA Bottin H., Lagoutte B.; 6376RT "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp 6377RT PCC 6803."; 6378RL Biochim. Biophys. Acta 1101:48-56(1992). 6379CC -!- FUNCTION: Low-potential electron donor to a number of redox 6380CC enzymes. 6381CC -!- COFACTOR: FMN. 6382CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 6383CC Redox potential: 6384CC E(0) are -433 mV and -238 mV; 6385CC -!- SIMILARITY: Belongs to the flavodoxin family. 6386CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6387CC ----------------------------------------------------------------------- 6388CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6389CC Distributed under the Creative Commons Attribution-NoDerivs License 6390CC ----------------------------------------------------------------------- 6391DR EMBL; Z27091; CAA81614.1; -; Genomic_DNA. 6392DR EMBL; L25881; AAA27288.1; -; Genomic_DNA. 6393DR EMBL; BA000022; BAA17947.1; -; Genomic_DNA. 6394DR PIR; S38632; S38632. 6395DR RefSeq; NP_441267.1; NC_000911.1. 6396DR RefSeq; YP_005651324.1; NC_017277.1. 6397DR ProteinModelPortal; P27319; -. 6398DR SMR; P27319; 3-165. 6399DR STRING; P27319; -. 6400DR GeneID; 12255742; -. 6401DR GeneID; 954609; -. 6402DR GenomeReviews; BA000022_GR; sll0248. 6403DR KEGG; syn:sll0248; -. 6404DR PATRIC; 23839886; VBISynSp132158_1504. 6405DR eggNOG; COG0716; -. 6406DR HOGENOM; HOG000030543; -. 6407DR KO; K03839; -. 6408DR OMA; DDKHFVG; -. 6409DR ProtClustDB; PRK09267; -. 6410DR BioCyc; SSP1148:SLL0248-MONOMER; -. 6411DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6412DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6413DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6414DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6415DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6416DR InterPro; IPR008254; Flavodoxin/NO_synth. 6417DR InterPro; IPR001226; Flavodoxin_CS. 6418DR InterPro; IPR010086; Flavodoxin_lc. 6419DR Pfam; PF00258; Flavodoxin_1; 1. 6420DR TIGRFAMs; TIGR01752; Flav_long; 1. 6421DR PROSITE; PS00201; FLAVODOXIN; 1. 6422DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6423PE 1: Evidence at protein level; 6424KW Complete proteome; Direct protein sequencing; Electron transport; 6425KW Flavoprotein; FMN; Reference proteome; Transport. 6426FT CHAIN 1 170 Flavodoxin. 6427FT /FTId=PRO_0000171645. 6428FT DOMAIN 4 165 Flavodoxin-like. 6429FT CONFLICT 2 2 Missing (in Ref. 3; AA sequence). 6430FT CONFLICT 40 40 A -> AA (in Ref. 3; AA sequence). 6431SQ SEQUENCE 170 AA; 18822 MW; B2937F347796BBD9 CRC64; 6432 MTKIGLFYGT QTGNTETIAE LIQKEMGGDS VVDMMDISQA DVDDFRQYSC LIIGCPTWNV 6433 GELQSDWEGF YDQLDEIDFN GKKVAYFGAG DQVGYADNFQ DAMGILEEKI SGLGGKTVGF 6434 WPTAGYDFDE SKAVKNGKFV GLALDEDNQP ELTELRVKTW VSEIKPILQS 6435// 6436ID FLAV_TREPA Reviewed; 146 AA. 6437AC O83895; 6438DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 6439DT 01-NOV-1998, sequence version 1. 6440DT 16-MAY-2012, entry version 67. 6441DE RecName: Full=Flavodoxin; 6442GN Name=fldA; OrderedLocusNames=TP_0925; 6443OS Treponema pallidum (strain Nichols). 6444OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. 6445OX NCBI_TaxID=243276; 6446RN [1] 6447RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6448RC STRAIN=Nichols; 6449RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; 6450RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., 6451RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., 6452RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., 6453RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., 6454RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., 6455RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., 6456RA Weidman J.F., Smith H.O., Venter J.C.; 6457RT "Complete genome sequence of Treponema pallidum, the syphilis 6458RT spirochete."; 6459RL Science 281:375-388(1998). 6460CC -!- FUNCTION: Low-potential electron donor to a number of redox 6461CC enzymes (By similarity). 6462CC -!- COFACTOR: FMN (By similarity). 6463CC -!- SIMILARITY: Belongs to the flavodoxin family. 6464CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6465CC ----------------------------------------------------------------------- 6466CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6467CC Distributed under the Creative Commons Attribution-NoDerivs License 6468CC ----------------------------------------------------------------------- 6469DR EMBL; AE000520; AAC65882.1; -; Genomic_DNA. 6470DR PIR; F71263; F71263. 6471DR RefSeq; NP_219360.1; NC_000919.1. 6472DR ProteinModelPortal; O83895; -. 6473DR IntAct; O83895; 2. 6474DR GeneID; 2611211; -. 6475DR GenomeReviews; AE000520_GR; TP_0925. 6476DR KEGG; tpa:TP0925; -. 6477DR PATRIC; 20531963; VBITrePal57110_0977. 6478DR TIGR; TP_0925; -. 6479DR eggNOG; COG0716; -. 6480DR OMA; FGSYDWG; -. 6481DR ProtClustDB; CLSK218926; -. 6482DR BioCyc; TPAL243276:TP_0925-MONOMER; -. 6483DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. 6484DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6485DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6486DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6487DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6488DR InterPro; IPR010087; Flav_short. 6489DR InterPro; IPR008254; Flavodoxin/NO_synth. 6490DR InterPro; IPR001226; Flavodoxin_CS. 6491DR Pfam; PF00258; Flavodoxin_1; 1. 6492DR TIGRFAMs; TIGR01753; Flav_short; 1. 6493DR PROSITE; PS00201; FLAVODOXIN; 1. 6494DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6495PE 3: Inferred from homology; 6496KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 6497FT CHAIN 1 146 Flavodoxin. 6498FT /FTId=PRO_0000171646. 6499FT DOMAIN 4 145 Flavodoxin-like. 6500SQ SEQUENCE 146 AA; 15793 MW; 398A7D7C8530F2CE CRC64; 6501 MAKVAVIFWS GTGHTETMAR CIVEGLNVGG AKADLFSVMD FDVGTFDSYD RFAFGCSAAG 6502 SEELESSEFE PFFTSIEGRL SGKKVALFGS YEWAGEGEGG EWMVNWVERC KAAGADVFEG 6503 KGEIAYDDPS EEAQASCKAF GERFAR 6504// 6505ID FLAV_TRIEI Reviewed; 171 AA. 6506AC O52659; Q114Y7; 6507DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 6508DT 28-NOV-2006, sequence version 2. 6509DT 16-MAY-2012, entry version 63. 6510DE RecName: Full=Flavodoxin; 6511GN Name=fld; OrderedLocusNames=Tery_1666; 6512OS Trichodesmium erythraeum (strain IMS101). 6513OC Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium. 6514OX NCBI_TaxID=203124; 6515RN [1] 6516RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6517RC STRAIN=IMS101; 6518RG US DOE Joint Genome Institute; 6519RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., 6520RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., 6521RA Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., 6522RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., 6523RA Kyrpides N., Kim E., Richardson P.; 6524RT "Complete sequence of Trichodesmium erythraeum IMS101."; 6525RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 6526RN [2] 6527RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-146. 6528RA Lin S., Carpenter E.J.; 6529RT "Identification of a gene encoding flavodoxin in the marine 6530RT cyanobacterium Trichodesmium."; 6531RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. 6532CC -!- FUNCTION: Low-potential electron donor to a number of redox 6533CC enzymes (By similarity). 6534CC -!- COFACTOR: FMN (By similarity). 6535CC -!- SIMILARITY: Belongs to the flavodoxin family. 6536CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. 6537CC ----------------------------------------------------------------------- 6538CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6539CC Distributed under the Creative Commons Attribution-NoDerivs License 6540CC ----------------------------------------------------------------------- 6541DR EMBL; CP000393; ABG50937.1; -; Genomic_DNA. 6542DR EMBL; AF044318; AAC02683.1; -; Genomic_DNA. 6543DR RefSeq; YP_721410.1; NC_008312.1. 6544DR ProteinModelPortal; O52659; -. 6545DR SMR; O52659; 3-171. 6546DR GeneID; 4245460; -. 6547DR GenomeReviews; CP000393_GR; Tery_1666. 6548DR KEGG; ter:Tery_1666; -. 6549DR PATRIC; 23987341; VBITriEry99848_2106. 6550DR eggNOG; COG0716; -. 6551DR HOGENOM; HOG000030543; -. 6552DR KO; K03839; -. 6553DR OMA; DDKHFVG; -. 6554DR ProtClustDB; PRK09267; -. 6555DR BioCyc; TERY203124:TERY_1666-MONOMER; -. 6556DR GO; GO:0010181; F:FMN binding; IEA:InterPro. 6557DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 6558DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. 6559DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. 6560DR InterPro; IPR008254; Flavodoxin/NO_synth. 6561DR InterPro; IPR010086; Flavodoxin_lc. 6562DR Pfam; PF00258; Flavodoxin_1; 1. 6563DR TIGRFAMs; TIGR01752; Flav_long; 1. 6564DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. 6565DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. 6566PE 3: Inferred from homology; 6567KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. 6568FT CHAIN 1 171 Flavodoxin. 6569FT /FTId=PRO_0000171647. 6570FT DOMAIN 4 166 Flavodoxin-like. 6571FT CONFLICT 4 4 I -> M (in Ref. 2; AAC02683). 6572FT CONFLICT 8 8 V -> F (in Ref. 2; AAC02683). 6573FT CONFLICT 130 130 E -> V (in Ref. 2; AAC02683). 6574SQ SEQUENCE 171 AA; 18742 MW; 677F643438653126 CRC64; 6575 MSKIGLFVGT TTGKTEEAAE KIKEEFGGDD VVTIHDISEA SPEDFDGYQN VIIGCPTWDV 6576 GELQSDWSGF YSEELDNVKF TGKKVAYFGT GDQIGYADNF QDAMGILEEK ITGLGGTTIG 6577 SWSTEGYDHE DSKAVKNGKF VGLALDDDNQ ADLTDERIKE WVKQLKTEFG V 6578// 6579ID FLS1_ARATH Reviewed; 336 AA. 6580AC Q96330; O04730; O04731; O04732; O04830; O04831; O04832; 6581DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. 6582DT 01-FEB-1997, sequence version 1. 6583DT 13-JUN-2012, entry version 91. 6584DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase; 6585DE EC=1.14.11.23; 6586DE EC=1.14.11.9; 6587DE AltName: Full=FLS 1; 6588GN Name=FLS1; Synonyms=FLS; OrderedLocusNames=At5g08640; 6589GN ORFNames=MAH20.20; 6590OS Arabidopsis thaliana (Mouse-ear cress). 6591OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; 6592OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 6593OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. 6594OX NCBI_TaxID=3702; 6595RN [1] 6596RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY LIGHT. 6597RC STRAIN=cv. Landsberg erecta; 6598RX MEDLINE=97267154; PubMed=9112784; DOI=10.1104/pp.113.4.1437; 6599RA Pelletier M.K., Murrell J.R., Shirley B.W.; 6600RT "Characterization of flavonol synthase and leucoanthocyanidin 6601RT dioxygenase genes in Arabidopsis. Further evidence for differential 6602RT regulation of 'early' and 'late' genes."; 6603RL Plant Physiol. 113:1437-1445(1997). 6604RN [2] 6605RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INDUCTION BY 6606RP LIGHT, AND DISRUPTION PHENOTYPE. 6607RC STRAIN=cv. Columbia, and cv. Landsberg erecta; 6608RX MEDLINE=98445388; PubMed=9770503; DOI=10.1073/pnas.95.21.12432; 6609RA Wisman E., Hartmann U., Sagasser M., Baumann E., Palme K., 6610RA Hahlbrock K., Saedler H., Weisshaar B.; 6611RT "Knock-out mutants from an En-1 mutagenized Arabidopsis thaliana 6612RT population generate phenylpropanoid biosynthesis phenotypes."; 6613RL Proc. Natl. Acad. Sci. U.S.A. 95:12432-12437(1998). 6614RN [3] 6615RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 6616RC STRAIN=cv. Columbia; 6617RX MEDLINE=98069011; PubMed=9405937; DOI=10.1093/dnares/4.4.291; 6618RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., 6619RA Tabata S.; 6620RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. 6621RT Sequence features of the regions of 1,044,062 bp covered by thirteen 6622RT physically assigned P1 clones."; 6623RL DNA Res. 4:291-300(1997). 6624RN [4] 6625RP GENOME REANNOTATION. 6626RC STRAIN=cv. Columbia; 6627RG The Arabidopsis Information Resource (TAIR); 6628RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 6629RN [5] 6630RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 6631RC STRAIN=cv. Columbia; 6632RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; 6633RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., 6634RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., 6635RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., 6636RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., 6637RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., 6638RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., 6639RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., 6640RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., 6641RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., 6642RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., 6643RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., 6644RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; 6645RT "Empirical analysis of transcriptional activity in the Arabidopsis 6646RT genome."; 6647RL Science 302:842-846(2003). 6648RN [6] 6649RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 6650RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., 6651RA Feldmann K.A.; 6652RT "Full-length cDNA from Arabidopsis thaliana."; 6653RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. 6654RN [7] 6655RP TISSUE SPECIFICITY. 6656RX PubMed=10394944; 6657RA Pelletier M.K., Burbulis I.E., Winkel-Shirley B.; 6658RT "Disruption of specific flavonoid genes enhances the accumulation of 6659RT flavonoid enzymes and end-products in Arabidopsis seedlings."; 6660RL Plant Mol. Biol. 40:45-54(1999). 6661RN [8] 6662RP FUNCTION, AND CATALYTIC ACTIVITY. 6663RX PubMed=12126705; 6664RA Prescott A.G., Stamford N.P., Wheeler G., Firmin J.L.; 6665RT "In vitro properties of a recombinant flavonol synthase from 6666RT Arabidopsis thaliana."; 6667RL Phytochemistry 60:589-593(2002). 6668RN [9] 6669RP FUNCTION, AND CATALYTIC ACTIVITY. 6670RX PubMed=16153644; DOI=10.1016/j.febslet.2005.08.033; 6671RA Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J., 6672RA Schofield C.J.; 6673RT "Incorporation of oxygen into the succinate co-product of iron(II) and 6674RT 2-oxoglutarate dependent oxygenases from bacteria, plants and 6675RT humans."; 6676RL FEBS Lett. 579:5170-5174(2005). 6677RN [10] 6678RP TISSUE SPECIFICITY, AND INDUCTION. 6679RX PubMed=15821875; DOI=10.1007/s11103-004-6910-0; 6680RA Hartmann U., Sagasser M., Mehrtens F., Stracke R., Weisshaar B.; 6681RT "Differential combinatorial interactions of cis-acting elements 6682RT recognized by R2R3-MYB, BZIP, and BHLH factors control light- 6683RT responsive and tissue-specific activation of phenylpropanoid 6684RT biosynthesis genes."; 6685RL Plant Mol. Biol. 57:155-171(2005). 6686RN [11] 6687RP FUNCTION, AND MUTAGENESIS OF HIS-132 AND LYS-329. 6688RX PubMed=16106293; DOI=10.1039/b507153d; 6689RA Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C., 6690RA Schofield C.J.; 6691RT "Structural and mechanistic studies on anthocyanidin synthase 6692RT catalysed oxidation of flavanone substrates: the effect of C-2 6693RT stereochemistry on product selectivity and mechanism."; 6694RL Org. Biomol. Chem. 3:3117-3126(2005). 6695RN [12] 6696RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-132; 6697RP PHE-134; LYS-202; HIS-221; ASP-223; HIS-277; ARG-287; SER-289; PHE-293 6698RP AND GLU-295. 6699RX PubMed=17719613; DOI=10.1016/j.phytochem.2007.07.006; 6700RA Chua C.S., Biermann D., Goo K.S., Sim T.S.; 6701RT "Elucidation of active site residues of Arabidopsis thaliana flavonol 6702RT synthase provides a molecular platform for engineering flavonols."; 6703RL Phytochemistry 69:66-75(2008). 6704RN [13] 6705RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND 6706RP DISRUPTION PHENOTYPE. 6707RC STRAIN=cv. Wassilewskija; 6708RX PubMed=18467451; DOI=10.1104/pp.108.117457; 6709RA Owens D.K., Alerding A.B., Crosby K.C., Bandara A.B., Westwood J.H., 6710RA Winkel B.S.; 6711RT "Functional analysis of a predicted flavonol synthase gene family in 6712RT Arabidopsis."; 6713RL Plant Physiol. 147:1046-1061(2008). 6714RN [14] 6715RP FUNCTION. 6716RX PubMed=19433090; DOI=10.1016/j.febslet.2009.05.006; 6717RA Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., 6718RA Martens S.; 6719RT "Arabidopsis thaliana expresses a second functional flavonol 6720RT synthase."; 6721RL FEBS Lett. 583:1981-1986(2009). 6722RN [15] 6723RP FUNCTION, AND DISRUPTION PHENOTYPE. 6724RC STRAIN=cv. No-0; 6725RX PubMed=18998159; DOI=10.1007/s00425-008-0841-y; 6726RA Stracke R., De Vos R.C., Bartelniewoehner L., Ishihara H., 6727RA Sagasser M., Martens S., Weisshaar B.; 6728RT "Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis 6729RT thaliana support the in vivo involvement of leucoanthocyanidin 6730RT dioxygenase."; 6731RL Planta 229:427-445(2009). 6732RN [16] 6733RP INDUCTION. 6734RX PubMed=21427279; DOI=10.1104/pp.111.172502; 6735RA Lewis D.R., Ramirez M.V., Miller N.D., Vallabhaneni P., Ray W.K., 6736RA Helm R.F., Winkel B.S., Muday G.K.; 6737RT "Auxin and ethylene induce flavonol accumulation through distinct 6738RT transcriptional networks."; 6739RL Plant Physiol. 156:144-164(2011). 6740RN [17] 6741RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. 6742RX PubMed=21502189; DOI=10.1104/pp.111.175976; 6743RA Kuhn B.M., Geisler M., Bigler L., Ringli C.; 6744RT "Flavonols accumulate asymmetrically and affect auxin transport in 6745RT Arabidopsis."; 6746RL Plant Physiol. 156:585-595(2011). 6747CC -!- FUNCTION: Catalyzes the formation of flavonols from 6748CC dihydroflavonols. It can act on dihydrokaempferol to produce 6749CC kaempferol, on dihydroquercetin to produce quercitin and on 6750CC dihydromyricetin to produce myricetin. In vitro catalyzes the 6751CC oxidation of both enantiomers of naringenin to give both cis- and 6752CC trans-dihydrokaempferol. 6753CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a 6754CC flavonol + succinate + CO(2) + H(2)O. 6755CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a 6756CC dihydroflavonol + succinate + CO(2). 6757CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. 6758CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. 6759CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 6760CC Kinetic parameters: 6761CC KM=59 uM for dihydroquercetin.; 6762CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid 6763CC biosynthesis. 6764CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. 6765CC -!- TISSUE SPECIFICITY: Expressed in young seedlings (at protein 6766CC level). Expressed in roots, emerging leaves, shoot-root transition 6767CC zone, trichomes, flowers and siliques. In cotyledons, expressed 6768CC mostly on the adaxial side and only in guard cells on the abaxial 6769CC side. 6770CC -!- INDUCTION: By light, auxin and 1-aminocyclopropane-1-carboxylic 6771CC acid (ACC). 6772CC -!- DISRUPTION PHENOTYPE: Accumulation of anthocyanins and 6773CC glycosylated forms of dihydroflavonols, and drastic reduction of 6774CC kaempferol, quercitin and favonol glycosides. 6775CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 6776CC family. 6777CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. 6778CC ----------------------------------------------------------------------- 6779CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6780CC Distributed under the Creative Commons Attribution-NoDerivs License 6781CC ----------------------------------------------------------------------- 6782DR EMBL; U72631; AAB17393.1; -; Genomic_DNA. 6783DR EMBL; U84258; AAC69362.1; -; Genomic_DNA. 6784DR EMBL; U84259; AAC69363.1; -; mRNA. 6785DR EMBL; U84260; AAB41504.1; -; mRNA. 6786DR EMBL; AB006697; BAB10013.1; -; Genomic_DNA. 6787DR EMBL; CP002688; AED91332.1; -; Genomic_DNA. 6788DR EMBL; CP002688; AED91333.1; -; Genomic_DNA. 6789DR EMBL; AY058068; AAL24176.1; -; mRNA. 6790DR EMBL; BT000494; AAN18063.1; -; mRNA. 6791DR EMBL; AY086328; AAM64397.1; -; mRNA. 6792DR IPI; IPI00532962; -. 6793DR RefSeq; NP_001190266.1; NM_001203337.1. 6794DR RefSeq; NP_196481.1; NM_120951.2. 6795DR UniGene; At.8771; -. 6796DR ProteinModelPortal; Q96330; -. 6797DR SMR; Q96330; 2-334. 6798DR IntAct; Q96330; 3. 6799DR STRING; Q96330; -. 6800DR PRIDE; Q96330; -. 6801DR ProMEX; Q96330; -. 6802DR EnsemblPlants; AT5G08640; AT5G08640; AT5G08640. 6803DR GeneID; 830765; -. 6804DR GenomeReviews; BA000015_GR; AT5G08640. 6805DR KEGG; ath:AT5G08640; -. 6806DR TAIR; At5g08640; -. 6807DR eggNOG; COG3491; -. 6808DR InParanoid; Q96330; -. 6809DR KO; K05278; -. 6810DR OMA; EWGLFQV; -. 6811DR PhylomeDB; Q96330; -. 6812DR ProtClustDB; PLN02704; -. 6813DR ArrayExpress; Q96330; -. 6814DR Genevestigator; Q96330; -. 6815DR GermOnline; AT5G08640; Arabidopsis thaliana. 6816DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 6817DR GO; GO:0045431; F:flavonol synthase activity; IDA:TAIR. 6818DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. 6819DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 6820DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. 6821DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. 6822DR GO; GO:0009733; P:response to auxin stimulus; IEP:TAIR. 6823DR GO; GO:0080167; P:response to karrikin; IEP:TAIR. 6824DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. 6825DR Pfam; PF03171; 2OG-FeII_Oxy; 1. 6826DR PROSITE; PS51471; FE2OG_OXY; 1. 6827PE 1: Evidence at protein level; 6828KW Complete proteome; Cytoplasm; Dioxygenase; Flavonoid biosynthesis; 6829KW Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome; 6830KW Vitamin C. 6831FT CHAIN 1 336 Flavonol synthase/flavanone 3- 6832FT hydroxylase. 6833FT /FTId=PRO_0000067291. 6834FT DOMAIN 196 296 Fe2OG dioxygenase. 6835FT REGION 204 206 2-oxoglutarate binding (By similarity). 6836FT REGION 287 289 2-oxoglutarate binding (Probable). 6837FT METAL 221 221 Iron; catalytic (Probable). 6838FT METAL 223 223 Iron; catalytic (Probable). 6839FT METAL 277 277 Iron; catalytic (Probable). 6840FT MUTAGEN 132 132 H->F: Slightly increases activity. 6841FT MUTAGEN 132 132 H->Y: Slightly decreases activity. 6842FT MUTAGEN 134 134 F->A: Reduces activity 7-fold. 6843FT MUTAGEN 134 134 F->L: Reduces activity 2-fold. 6844FT MUTAGEN 202 202 K->M: Reduces activity 25-fold. 6845FT MUTAGEN 202 202 K->R: Reduces activity 8-fold. 6846FT MUTAGEN 221 221 H->W: Loss of activity. 6847FT MUTAGEN 223 223 D->E: Loss of activity. 6848FT MUTAGEN 277 277 H->F: Loss of activity. 6849FT MUTAGEN 287 287 R->K: Loss of activity. 6850FT MUTAGEN 289 289 S->T: Reduces activity 2-fold. 6851FT MUTAGEN 293 293 F->A,L: Reduces activity 12-fold. 6852FT MUTAGEN 295 295 E->L: Reduces activity 15-fold. 6853FT MUTAGEN 295 295 E->Q: Reduces activity 2-fold. 6854FT MUTAGEN 329 329 K->N: Reduces activity 4-fold. 6855SQ SEQUENCE 336 AA; 38282 MW; 3283E3AFE603D2A9 CRC64; 6856 MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV 6857 VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ 6858 KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG 6859 LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV 6860 FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK 6861 IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD 6862// 6863ID FLS_MATIN Reviewed; 291 AA. 6864AC O04395; 6865DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. 6866DT 01-JUL-1997, sequence version 1. 6867DT 13-JUN-2012, entry version 63. 6868DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase; 6869DE Short=FLS; 6870DE EC=1.14.11.23; 6871DE EC=1.14.11.9; 6872DE Flags: Fragment; 6873OS Matthiola incana (Common stock) (Cheiranthus incanus). 6874OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; 6875OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 6876OC rosids; malvids; Brassicales; Brassicaceae; Anchonieae; Matthiola. 6877OX NCBI_TaxID=3724; 6878RN [1] 6879RP NUCLEOTIDE SEQUENCE [MRNA]. 6880RC TISSUE=Flower bud, and Petal; 6881RA Henkel J., Forkmann G.; 6882RT "Cloning and expression of a flavonol synthase gene from common stock 6883RT (Matthiola incana)."; 6884RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. 6885CC -!- FUNCTION: Catalyzes the formation of flavonols from 6886CC dihydroflavonols. It can act on dihydrokaempferol to produce 6887CC kaempferol, on dihydroquercetin to produce quercitin and on 6888CC dihydromyricetin to produce myricetin. 6889CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a 6890CC flavonol + succinate + CO(2) + H(2)O. 6891CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a 6892CC dihydroflavonol + succinate + CO(2). 6893CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. 6894CC -!- COFACTOR: Binds 1 iron ion per subunit. 6895CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid 6896CC biosynthesis. 6897CC -!- SUBCELLULAR LOCATION: Cytoplasm. 6898CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 6899CC family. 6900CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. 6901CC ----------------------------------------------------------------------- 6902CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6903CC Distributed under the Creative Commons Attribution-NoDerivs License 6904CC ----------------------------------------------------------------------- 6905DR EMBL; AF001391; AAB58800.1; -; mRNA. 6906DR ProteinModelPortal; O04395; -. 6907DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 6908DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. 6909DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. 6910DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 6911DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. 6912DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. 6913DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. 6914DR Pfam; PF03171; 2OG-FeII_Oxy; 1. 6915DR PROSITE; PS51471; FE2OG_OXY; 1. 6916PE 2: Evidence at transcript level; 6917KW Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; 6918KW Oxidoreductase; Vitamin C. 6919FT CHAIN <1 291 Flavonol synthase/flavanone 3- 6920FT hydroxylase. 6921FT /FTId=PRO_0000067295. 6922FT DOMAIN 151 250 Fe2OG dioxygenase. 6923FT METAL 175 175 Iron (By similarity). 6924FT METAL 177 177 Iron (By similarity). 6925FT METAL 231 231 Iron (By similarity). 6926FT NON_TER 1 1 6927SQ SEQUENCE 291 AA; 33430 MW; 6B8E4E3D2834720A CRC64; 6928 QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR 6929 SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA 6930 RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING 6931 LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT 6932 RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S 6933// 6934ID FLS_PETHY Reviewed; 348 AA. 6935AC Q07512; 6936DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 6937DT 01-OCT-1996, sequence version 1. 6938DT 13-JUN-2012, entry version 66. 6939DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase; 6940DE Short=FLS; 6941DE EC=1.14.11.23; 6942DE EC=1.14.11.9; 6943GN Name=FL; 6944OS Petunia hybrida (Petunia). 6945OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; 6946OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 6947OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia. 6948OX NCBI_TaxID=4102; 6949RN [1] 6950RP NUCLEOTIDE SEQUENCE [MRNA]. 6951RC STRAIN=cv. Old Glory Blue; TISSUE=Petal; 6952RX MEDLINE=94108485; PubMed=7904213; 6953RX DOI=10.1046/j.1365-313X.1993.04061003.x; 6954RA Holton T.A., Brugliera F., Tanaka Y.; 6955RT "Cloning and expression of flavonol synthase from Petunia hybrida."; 6956RL Plant J. 4:1003-1010(1993). 6957CC -!- FUNCTION: Catalyzes the formation of flavonols from 6958CC dihydroflavonols. It can act on dihydrokaempferol to produce 6959CC kaempferol, on dihydroquercetin to produce quercitin and on 6960CC dihydromyricetin to produce myricetin. 6961CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a 6962CC flavonol + succinate + CO(2) + H(2)O. 6963CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a 6964CC dihydroflavonol + succinate + CO(2). 6965CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. 6966CC -!- COFACTOR: Binds 1 iron ion per subunit. 6967CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid 6968CC biosynthesis. 6969CC -!- SUBCELLULAR LOCATION: Cytoplasm. 6970CC -!- DEVELOPMENTAL STAGE: Expressed at highest level during the first 6971CC stage of flower development. 6972CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 6973CC family. 6974CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. 6975CC ----------------------------------------------------------------------- 6976CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 6977CC Distributed under the Creative Commons Attribution-NoDerivs License 6978CC ----------------------------------------------------------------------- 6979DR EMBL; Z22543; CAA80264.1; -; mRNA. 6980DR PIR; S33510; S33510. 6981DR ProteinModelPortal; Q07512; -. 6982DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 6983DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. 6984DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 6985DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. 6986DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. 6987DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. 6988DR InterPro; IPR002283; Isopenicillin-N_synthase. 6989DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. 6990DR Pfam; PF03171; 2OG-FeII_Oxy; 1. 6991DR PRINTS; PR00682; IPNSYNTHASE. 6992DR PROSITE; PS51471; FE2OG_OXY; 1. 6993PE 2: Evidence at transcript level; 6994KW Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; 6995KW Oxidoreductase; Vitamin C. 6996FT CHAIN 1 348 Flavonol synthase/flavanone 3- 6997FT hydroxylase. 6998FT /FTId=PRO_0000067296. 6999FT DOMAIN 209 309 Fe2OG dioxygenase. 7000FT METAL 234 234 Iron (By similarity). 7001FT METAL 236 236 Iron (By similarity). 7002FT METAL 290 290 Iron (By similarity). 7003SQ SEQUENCE 348 AA; 39427 MW; B39E1E4381DE6379 CRC64; 7004 MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL 7005 RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP 7006 GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR 7007 EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI 7008 TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR 7009 MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ 7010// 7011ID FLS_SOLTU Reviewed; 349 AA. 7012AC Q41452; 7013DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 7014DT 01-NOV-1997, sequence version 1. 7015DT 13-JUN-2012, entry version 66. 7016DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase; 7017DE Short=FLS; 7018DE EC=1.14.11.23; 7019DE EC=1.14.11.9; 7020OS Solanum tuberosum (Potato). 7021OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; 7022OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; 7023OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; 7024OC Solanum. 7025OX NCBI_TaxID=4113; 7026RN [1] 7027RP NUCLEOTIDE SEQUENCE [MRNA]. 7028RC TISSUE=Pistil; 7029RX MEDLINE=97177800; PubMed=9025306; 7030RX DOI=10.1046/j.1365-313X.1997.11010105.x; 7031RA van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A., 7032RA Schrauwen J.A.M., Wullems G.J.; 7033RT "Regulation of flavonol biosynthesis during anther and pistil 7034RT development, and during pollen tube growth in Solanum tuberosum."; 7035RL Plant J. 11:105-113(1997). 7036CC -!- FUNCTION: Catalyzes the formation of flavonols from 7037CC dihydroflavonols. It can act on dihydrokaempferol to produce 7038CC kaempferol, on dihydroquercetin to produce quercitin and on 7039CC dihydromyricetin to produce myricetin. 7040CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a 7041CC flavonol + succinate + CO(2) + H(2)O. 7042CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a 7043CC dihydroflavonol + succinate + CO(2). 7044CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). 7045CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity). 7046CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid 7047CC biosynthesis. 7048CC -!- SUBCELLULAR LOCATION: Cytoplasm. 7049CC -!- DEVELOPMENTAL STAGE: Temporally expressed during flower 7050CC development. 7051CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase 7052CC family. 7053CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. 7054CC ----------------------------------------------------------------------- 7055CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 7056CC Distributed under the Creative Commons Attribution-NoDerivs License 7057CC ----------------------------------------------------------------------- 7058DR EMBL; X92178; CAA63092.1; -; mRNA. 7059DR PIR; T07373; T07373. 7060DR ProteinModelPortal; Q41452; -. 7061DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 7062DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. 7063DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. 7064DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 7065DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. 7066DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. 7067DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. 7068DR Pfam; PF03171; 2OG-FeII_Oxy; 1. 7069DR PROSITE; PS51471; FE2OG_OXY; 1. 7070PE 2: Evidence at transcript level; 7071KW Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; 7072KW Oxidoreductase; Vitamin C. 7073FT CHAIN 1 349 Flavonol synthase/flavanone 3- 7074FT hydroxylase. 7075FT /FTId=PRO_0000067297. 7076FT DOMAIN 213 310 Fe2OG dioxygenase. 7077FT METAL 238 238 Iron (By similarity). 7078FT METAL 240 240 Iron (By similarity). 7079FT METAL 291 291 Iron (By similarity). 7080SQ SEQUENCE 349 AA; 39728 MW; ADBBC3F6B10A0E05 CRC64; 7081 MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI 7082 DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI 7083 AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA 7084 KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD 7085 MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT 7086 RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ 7087// 7088ID FOS_TAKRU Reviewed; 376 AA. 7089AC P53450; 7090DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 7091DT 01-OCT-1996, sequence version 1. 7092DT 16-MAY-2012, entry version 67. 7093DE RecName: Full=Proto-oncogene c-Fos; 7094DE AltName: Full=Cellular oncogene fos; 7095GN Name=fos; 7096OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 7097OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 7098OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 7099OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 7100OC Tetradontoidea; Tetraodontidae; Takifugu. 7101OX NCBI_TaxID=31033; 7102RN [1] 7103RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 7104RX MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366; 7105RA Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., 7106RA Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., 7107RA Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.; 7108RT "Conservation of synteny between the genome of the pufferfish (Fugu 7109RT rubripes) and the region on human chromosome 14 (14q24.3) associated 7110RT with familial Alzheimer disease (AD3 locus)."; 7111RL Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996). 7112CC -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non- 7113CC covalently linked complex with the JUN/AP-1 transcription factor. 7114CC FOS has a critical function in regulating the development of cells 7115CC destined to form and maintain the skeleton. It is thought to have 7116CC an important role in signal transduction, cell proliferation and 7117CC differentiation (By similarity). 7118CC -!- SUBUNIT: Heterodimer (By similarity). 7119CC -!- SUBCELLULAR LOCATION: Nucleus. 7120CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. 7121CC -!- SIMILARITY: Contains 1 bZIP domain. 7122CC ----------------------------------------------------------------------- 7123CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 7124CC Distributed under the Creative Commons Attribution-NoDerivs License 7125CC ----------------------------------------------------------------------- 7126DR EMBL; U40757; AAC59778.1; -; Genomic_DNA. 7127DR ProteinModelPortal; P53450; -. 7128DR SMR; P53450; 123-182. 7129DR STRING; P53450; -. 7130DR eggNOG; NOG258795; -. 7131DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 7132DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. 7133DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. 7134DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. 7135DR InterPro; IPR004827; bZIP. 7136DR InterPro; IPR011616; bZIP_1. 7137DR InterPro; IPR000837; Leuzip_Fos. 7138DR Pfam; PF00170; bZIP_1; 1. 7139DR PRINTS; PR00042; LEUZIPPRFOS. 7140DR SMART; SM00338; BRLZ; 1. 7141DR PROSITE; PS50217; BZIP; 1. 7142DR PROSITE; PS00036; BZIP_BASIC; 1. 7143PE 3: Inferred from homology; 7144KW Complete proteome; DNA-binding; Nucleus; Phosphoprotein; 7145KW Proto-oncogene; Reference proteome. 7146FT CHAIN 1 376 Proto-oncogene c-Fos. 7147FT /FTId=PRO_0000076473. 7148FT DOMAIN 149 177 Leucine-zipper. 7149FT DNA_BIND 123 144 Basic motif. 7150SQ SEQUENCE 376 AA; 40826 MW; BFC28534431DB491 CRC64; 7151 MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT 7152 AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE 7153 EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI 7154 LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN 7155 SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA 7156 AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS 7157 NDQSSDSLSS PTLLAL 7158// 7159ID G6PD_TAKRU Reviewed; 530 AA. 7160AC P54996; 7161DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 7162DT 01-OCT-1996, sequence version 1. 7163DT 16-MAY-2012, entry version 76. 7164DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase; 7165DE Short=G6PD; 7166DE EC=1.1.1.49; 7167GN Name=g6pd; 7168OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 7169OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 7170OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 7171OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 7172OC Tetradontoidea; Tetraodontidae; Takifugu. 7173OX NCBI_TaxID=31033; 7174RN [1] 7175RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 7176RX MEDLINE=95331796; PubMed=7607684; DOI=10.1016/0888-7543(95)80179-P; 7177RA Mason P.J., Stevens D.J., Luzzatto L., Brenner S., Aparicio S.; 7178RT "Genomic structure and sequence of the Fugu rubripes glucose-6- 7179RT phosphate dehydrogenase gene (G6PD)."; 7180RL Genomics 26:587-591(1995). 7181CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D- 7182CC glucono-1,5-lactone + NADPH. 7183CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- 7184CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): 7185CC step 1/3. 7186CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase 7187CC family. 7188CC ----------------------------------------------------------------------- 7189CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 7190CC Distributed under the Creative Commons Attribution-NoDerivs License 7191CC ----------------------------------------------------------------------- 7192DR EMBL; X83611; CAA58590.2; -; Genomic_DNA. 7193DR PIR; A56841; A56841. 7194DR ProteinModelPortal; P54996; -. 7195DR SMR; P54996; 43-530. 7196DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC. 7197DR GO; GO:0050661; F:NADP binding; IEA:InterPro. 7198DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. 7199DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. 7200DR InterPro; IPR001282; G6P_DH. 7201DR InterPro; IPR019796; G6P_DH_AS. 7202DR InterPro; IPR022675; G6P_DH_C. 7203DR InterPro; IPR022674; G6P_DH_NAD-bd. 7204DR InterPro; IPR016040; NAD(P)-bd_dom. 7205DR PANTHER; PTHR23429; G6PDH; 1. 7206DR Pfam; PF02781; G6PD_C; 1. 7207DR Pfam; PF00479; G6PD_N; 1. 7208DR PIRSF; PIRSF000110; G6PD; 1. 7209DR PRINTS; PR00079; G6PDHDRGNASE. 7210DR TIGRFAMs; TIGR00871; Zwf; 1. 7211DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. 7212PE 3: Inferred from homology; 7213KW Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP; 7214KW Oxidoreductase; Reference proteome. 7215FT CHAIN 1 530 Glucose-6-phosphate 1-dehydrogenase. 7216FT /FTId=PRO_0000068088. 7217FT ACT_SITE 278 278 Proton acceptor (By similarity). 7218FT BINDING 55 55 NADP (By similarity). 7219FT BINDING 87 87 NADP (By similarity). 7220FT BINDING 216 216 Substrate (By similarity). 7221FT BINDING 220 220 Substrate (By similarity). 7222SQ SEQUENCE 530 AA; 60469 MW; FC73FB53D834EF29 CRC64; 7223 MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK 7224 KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN 7225 SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN 7226 RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW 7227 NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR 7228 DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH 7229 NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM 7230 SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF 7231 TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL 7232// 7233ID GCN4_YEAST Reviewed; 281 AA. 7234AC P03069; D3DLN9; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0; 7235AC Q96UT3; 7236DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 7237DT 21-JUL-1986, sequence version 1. 7238DT 13-JUN-2012, entry version 139. 7239DE RecName: Full=General control protein GCN4; 7240DE AltName: Full=Amino acid biosynthesis regulatory protein; 7241GN Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C; 7242OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 7243OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; 7244OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. 7245OX NCBI_TaxID=559292; 7246RN [1] 7247RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 7248RX MEDLINE=85038531; PubMed=6387704; DOI=10.1073/pnas.81.20.6442; 7249RA Hinnebusch A.G.; 7250RT "Evidence for translational regulation of the activator of general 7251RT amino acid control in yeast."; 7252RL Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984). 7253RN [2] 7254RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 7255RX MEDLINE=84298088; PubMed=6433345; DOI=10.1073/pnas.81.16.5096; 7256RA Thireos G., Penn M.D., Greer H.; 7257RT "5' untranslated sequences are required for the translational control 7258RT of a yeast regulatory gene."; 7259RL Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984). 7260RN [3] 7261RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62; 7262RP ALA-82; ALA-91; ALA-125 AND GLU-196. 7263RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, 7264RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17; 7265RX PubMed=15087486; DOI=10.1093/nar/gkh529; 7266RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S., 7267RA Souciet J.-L.; 7268RT "Differential evolution of the Saccharomyces cerevisiae DUP240 7269RT paralogs and implication of recombination in phylogeny."; 7270RL Nucleic Acids Res. 32:2069-2078(2004). 7271RN [4] 7272RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 7273RC STRAIN=ATCC 204511 / S288c / AB972; 7274RX MEDLINE=97313264; PubMed=9169868; 7275RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., 7276RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., 7277RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., 7278RA Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., 7279RA Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., 7280RA Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., 7281RA Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.; 7282RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; 7283RL Nature 387:78-81(1997). 7284RN [5] 7285RP GENOME REANNOTATION. 7286RC STRAIN=ATCC 204508 / S288c; 7287RG Saccharomyces Genome Database; 7288RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. 7289RN [6] 7290RP NUCLEOTIDE SEQUENCE [MRNA] OF 249-281. 7291RX PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x; 7292RA Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.; 7293RT "Construction of dimeric F(ab) useful in blood group serology."; 7294RL Transfusion 42:257-264(2002). 7295RN [7] 7296RP DOMAINS. 7297RX MEDLINE=87002456; PubMed=3530496; DOI=10.1016/0092-8674(86)90070-X; 7298RA Hope I.A., Struhl K.; 7299RT "Functional dissection of a eukaryotic transcriptional activator 7300RT protein, GCN4 of yeast."; 7301RL Cell 46:885-894(1986). 7302RN [8] 7303RP DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113 7304RP AND 120-TRP--PHE-124. 7305RX PubMed=7862116; 7306RA Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H., 7307RA Hinnebusch A.G.; 7308RT "The transcriptional activator GCN4 contains multiple activation 7309RT domains that are critically dependent on hydrophobic amino acids."; 7310RL Mol. Cell. Biol. 15:1220-1233(1995). 7311RN [9] 7312RP PHOSPHORYLATION AT THR-165. 7313RX PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002; 7314RA Shemer R., Meimoun A., Holtzman T., Kornitzer D.; 7315RT "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5."; 7316RL Mol. Cell. Biol. 22:5395-5404(2002). 7317RN [10] 7318RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-165 AND SER-218, 7319RP AND MASS SPECTROMETRY. 7320RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; 7321RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; 7322RT "A multidimensional chromatography technology for in-depth 7323RT phosphoproteome analysis."; 7324RL Mol. Cell. Proteomics 7:1389-1396(2008). 7325RN [11] 7326RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281. 7327RX MEDLINE=92054531; PubMed=1948029; DOI=10.1126/science.1948029; 7328RA O'Shea E.K., Klemm J.D., Kim P.S., Alber T.; 7329RT "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel 7330RT coiled coil."; 7331RL Science 254:539-544(1991). 7332RN [12] 7333RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281. 7334RX MEDLINE=93113690; PubMed=1473154; DOI=10.1016/S0092-8674(05)80070-4; 7335RA Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.; 7336RT "The GCN4 basic region leucine zipper binds DNA as a dimer of 7337RT uninterrupted alpha helices: crystal structure of the protein-DNA 7338RT complex."; 7339RL Cell 71:1223-1237(1992). 7340RN [13] 7341RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281. 7342RX MEDLINE=99057965; PubMed=9837709; DOI=10.1006/jmbi.1998.2214; 7343RA Eckert D.M., Malashkevich V.N., Kim P.S.; 7344RT "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried 7345RT polar residues."; 7346RL J. Mol. Biol. 284:859-865(1998). 7347RN [14] 7348RP STRUCTURE BY NMR OF 237-281. 7349RX MEDLINE=91367802; PubMed=1891459; DOI=10.1093/protein/4.5.519; 7350RA Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H., 7351RA Gibson T.; 7352RT "The solution structure of a leucine-zipper motif peptide."; 7353RL Protein Eng. 4:519-529(1991). 7354CC -!- FUNCTION: Is a transcription factor that is responsible for the 7355CC activation of more than 30 genes required for amino acid or for 7356CC purine biosynthesis in response to amino acid or purine 7357CC starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA- 7358CC 3'. 7359CC -!- SUBUNIT: Binds DNA as a dimer. 7360CC -!- SUBCELLULAR LOCATION: Nucleus. 7361CC -!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal 7362CC activation domain (NTAD) and the central acidic activation domain 7363CC (CAAD) respectively, which can function independently to promote 7364CC high-level transcription of the target genes. 7365CC -!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation 7366CC of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase 7367CC complex SCF(Cdc4). 7368CC -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. 7369CC -!- SIMILARITY: Contains 1 bZIP domain. 7370CC ----------------------------------------------------------------------- 7371CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 7372CC Distributed under the Creative Commons Attribution-NoDerivs License 7373CC ----------------------------------------------------------------------- 7374DR EMBL; K02205; AAA34640.1; -; Genomic_DNA. 7375DR EMBL; K02649; AAA65521.1; -; Genomic_DNA. 7376DR EMBL; AJ585686; CAE52206.1; -; Genomic_DNA. 7377DR EMBL; AJ585687; CAE52207.1; -; Genomic_DNA. 7378DR EMBL; AJ585688; CAE52208.1; -; Genomic_DNA. 7379DR EMBL; AJ585689; CAE52209.1; -; Genomic_DNA. 7380DR EMBL; AJ585690; CAE52210.1; -; Genomic_DNA. 7381DR EMBL; AJ585691; CAE52211.1; -; Genomic_DNA. 7382DR EMBL; AJ585692; CAE52212.1; -; Genomic_DNA. 7383DR EMBL; AJ585693; CAE52213.1; -; Genomic_DNA. 7384DR EMBL; AJ585694; CAE52214.1; -; Genomic_DNA. 7385DR EMBL; AJ585695; CAE52215.1; -; Genomic_DNA. 7386DR EMBL; AJ585696; CAE52216.1; -; Genomic_DNA. 7387DR EMBL; AJ585697; CAE52217.1; -; Genomic_DNA. 7388DR EMBL; AJ585698; CAE52218.1; -; Genomic_DNA. 7389DR EMBL; AJ585699; CAE52219.1; -; Genomic_DNA. 7390DR EMBL; AJ585700; CAE52220.1; -; Genomic_DNA. 7391DR EMBL; AJ585701; CAE52221.1; -; Genomic_DNA. 7392DR EMBL; AJ585702; CAE52222.1; -; Genomic_DNA. 7393DR EMBL; AJ585703; CAE52223.1; -; Genomic_DNA. 7394DR EMBL; AJ585704; CAE52224.1; -; Genomic_DNA. 7395DR EMBL; AF416613; AAL09032.1; -; mRNA. 7396DR EMBL; U18530; AAB64486.1; -; Genomic_DNA. 7397DR EMBL; BK006939; DAA07643.1; -; Genomic_DNA. 7398DR PIR; A03605; RGBYA2. 7399DR RefSeq; NP_010907.1; NM_001178824.1. 7400DR PDB; 1CE9; X-ray; 1.80 A; A/B/C/D=253-281. 7401DR PDB; 1DGC; X-ray; 3.00 A; A=220-281. 7402DR PDB; 1ENV; X-ray; 2.60 A; A=254-280. 7403DR PDB; 1FAV; X-ray; 3.00 A; A=254-280. 7404DR PDB; 1FMH; NMR; -; A/B=249-279. 7405DR PDB; 1GCL; X-ray; 2.10 A; A/B/C/D=249-281. 7406DR PDB; 1GCM; X-ray; 1.80 A; A/B/C=249-281. 7407DR PDB; 1GK6; X-ray; 1.90 A; A/B=249-279. 7408DR PDB; 1GZL; X-ray; 1.80 A; A/B=249-276. 7409DR PDB; 1IHQ; NMR; -; A/B=264-281. 7410DR PDB; 1IJ0; X-ray; 1.86 A; A/B/C=249-281. 7411DR PDB; 1IJ1; X-ray; 1.86 A; A/B/C=249-281. 7412DR PDB; 1IJ2; X-ray; 1.70 A; A/B/C=249-281. 7413DR PDB; 1IJ3; X-ray; 1.80 A; A/B/C=249-281. 7414DR PDB; 1KQL; X-ray; 2.70 A; A/B=255-278. 7415DR PDB; 1LD4; EM; 11.40 A; E/F/G/H/I/J/K/L=225-281. 7416DR PDB; 1LLM; X-ray; 1.50 A; C/D=253-281. 7417DR PDB; 1NKN; X-ray; 2.50 A; A/B/C/D=250-281. 7418DR PDB; 1PIQ; X-ray; 1.80 A; A=249-277. 7419DR PDB; 1RB4; X-ray; 1.90 A; A/B/C=249-281. 7420DR PDB; 1RB5; X-ray; 1.90 A; A/B/C=249-281. 7421DR PDB; 1RB6; X-ray; 1.90 A; A/B/C=249-281. 7422DR PDB; 1SWI; X-ray; 2.60 A; A/B/C=249-281. 7423DR PDB; 1TMZ; NMR; -; A/B=264-281. 7424DR PDB; 1UNT; X-ray; 2.07 A; A/B=249-281. 7425DR PDB; 1UNU; X-ray; 2.07 A; A/B=249-281. 7426DR PDB; 1UNV; X-ray; 2.14 A; A/B=249-281. 7427DR PDB; 1UNW; X-ray; 2.20 A; A/B=249-281. 7428DR PDB; 1UNX; X-ray; 2.40 A; A/B=249-281. 7429DR PDB; 1UNY; X-ray; 2.30 A; A/B=249-281. 7430DR PDB; 1UNZ; X-ray; 2.30 A; A/B=249-281. 7431DR PDB; 1UO0; X-ray; 2.40 A; A/B=249-281. 7432DR PDB; 1UO1; X-ray; 2.50 A; A/B=249-281. 7433DR PDB; 1UO2; X-ray; 1.99 A; A/B=249-281. 7434DR PDB; 1UO3; X-ray; 1.92 A; A/B=249-281. 7435DR PDB; 1UO4; X-ray; 1.70 A; A/B=249-281. 7436DR PDB; 1UO5; X-ray; 2.07 A; A/B=249-281. 7437DR PDB; 1W5G; X-ray; 2.16 A; A/B=249-281. 7438DR PDB; 1W5H; X-ray; 2.50 A; A/B=249-281. 7439DR PDB; 1W5I; X-ray; 2.30 A; A/B=249-281. 7440DR PDB; 1W5J; X-ray; 2.20 A; A/B/C/D=249-273. 7441DR PDB; 1W5K; X-ray; 1.92 A; A/B/C/D=249-263. 7442DR PDB; 1W5L; X-ray; 2.17 A; A/B=249-281. 7443DR PDB; 1YSA; X-ray; 2.90 A; C/D=226-281. 7444DR PDB; 1ZII; X-ray; 1.80 A; A/B=249-281. 7445DR PDB; 1ZIJ; X-ray; 2.00 A; A/B/C=249-281. 7446DR PDB; 1ZIK; X-ray; 1.80 A; A/B=249-281. 7447DR PDB; 1ZIL; X-ray; 2.25 A; A/B=249-281. 7448DR PDB; 1ZIM; X-ray; 2.00 A; A/B/C=249-281. 7449DR PDB; 1ZTA; NMR; -; A=247-281. 7450DR PDB; 2AHP; X-ray; 2.00 A; A/B=249-281. 7451DR PDB; 2B1F; X-ray; 1.50 A; A/B/C/D=251-281. 7452DR PDB; 2B22; X-ray; 2.00 A; A=251-281. 7453DR PDB; 2BNI; X-ray; 1.50 A; A/B/C/D=249-281. 7454DR PDB; 2CCE; X-ray; 1.90 A; A/B=249-281. 7455DR PDB; 2CCF; X-ray; 1.70 A; A/B=249-281. 7456DR PDB; 2CCN; X-ray; 1.60 A; A/B=249-281. 7457DR PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=254-277. 7458DR PDB; 2DGC; X-ray; 2.20 A; A=220-281. 7459DR PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=249-277. 7460DR PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=249-277. 7461DR PDB; 2G9J; NMR; -; A/B=264-281. 7462DR PDB; 2HY6; X-ray; 1.25 A; A/B/C/D/E/F/G=251-281. 7463DR PDB; 2IPZ; X-ray; 1.35 A; A/B/C/D=251-281. 7464DR PDB; 2LPB; NMR; -; B=101-134. 7465DR PDB; 2NRN; X-ray; 1.40 A; A/B/C/D=251-281. 7466DR PDB; 2O7H; X-ray; 1.86 A; A/B/C/D/E/F=249-281. 7467DR PDB; 2OVN; NMR; -; A=264-280. 7468DR PDB; 2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272. 7469DR PDB; 2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272. 7470DR PDB; 2WPY; X-ray; 1.75 A; A=249-281. 7471DR PDB; 2WPZ; X-ray; 1.25 A; A/B/C=249-281. 7472DR PDB; 2WQ0; X-ray; 1.12 A; A=249-281. 7473DR PDB; 2WQ1; X-ray; 1.08 A; A=249-281. 7474DR PDB; 2WQ2; X-ray; 1.36 A; A=249-281. 7475DR PDB; 2WQ3; X-ray; 1.22 A; A=249-281. 7476DR PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=259-278, I=267-278. 7477DR PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=259-278, I/J=267-278. 7478DR PDB; 2ZTA; X-ray; 1.80 A; A/B=249-281. 7479DR PDB; 3AZD; X-ray; 0.98 A; A/B=264-281. 7480DR PDB; 3BAS; X-ray; 2.30 A; A/B=250-281. 7481DR PDB; 3BAT; X-ray; 2.30 A; A/B/C/D=250-281. 7482DR PDB; 3CK4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=251-281. 7483DR PDB; 3CRP; X-ray; 1.70 A; A/B/C/D/E=251-281. 7484DR PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=258-263. 7485DR PDB; 3GJP; X-ray; 2.00 A; A/B/C=249-281. 7486DR PDB; 3I1G; X-ray; 1.60 A; A=249-281. 7487DR PDB; 3I5C; X-ray; 1.94 A; A/B=249-278. 7488DR PDB; 3K7Z; X-ray; 1.90 A; A/B/C=249-281. 7489DR PDB; 3M48; X-ray; 1.45 A; A=249-281. 7490DR PDB; 3P8M; X-ray; 2.90 A; C/D=250-281. 7491DR PDBsum; 1CE9; -. 7492DR PDBsum; 1DGC; -. 7493DR PDBsum; 1ENV; -. 7494DR PDBsum; 1FAV; -. 7495DR PDBsum; 1FMH; -. 7496DR PDBsum; 1GCL; -. 7497DR PDBsum; 1GCM; -. 7498DR PDBsum; 1GK6; -. 7499DR PDBsum; 1GZL; -. 7500DR PDBsum; 1IHQ; -. 7501DR PDBsum; 1IJ0; -. 7502DR PDBsum; 1IJ1; -. 7503DR PDBsum; 1IJ2; -. 7504DR PDBsum; 1IJ3; -. 7505DR PDBsum; 1KQL; -. 7506DR PDBsum; 1LD4; -. 7507DR PDBsum; 1LLM; -. 7508DR PDBsum; 1NKN; -. 7509DR PDBsum; 1PIQ; -. 7510DR PDBsum; 1RB4; -. 7511DR PDBsum; 1RB5; -. 7512DR PDBsum; 1RB6; -. 7513DR PDBsum; 1SWI; -. 7514DR PDBsum; 1TMZ; -. 7515DR PDBsum; 1UNT; -. 7516DR PDBsum; 1UNU; -. 7517DR PDBsum; 1UNV; -. 7518DR PDBsum; 1UNW; -. 7519DR PDBsum; 1UNX; -. 7520DR PDBsum; 1UNY; -. 7521DR PDBsum; 1UNZ; -. 7522DR PDBsum; 1UO0; -. 7523DR PDBsum; 1UO1; -. 7524DR PDBsum; 1UO2; -. 7525DR PDBsum; 1UO3; -. 7526DR PDBsum; 1UO4; -. 7527DR PDBsum; 1UO5; -. 7528DR PDBsum; 1W5G; -. 7529DR PDBsum; 1W5H; -. 7530DR PDBsum; 1W5I; -. 7531DR PDBsum; 1W5J; -. 7532DR PDBsum; 1W5K; -. 7533DR PDBsum; 1W5L; -. 7534DR PDBsum; 1YSA; -. 7535DR PDBsum; 1ZII; -. 7536DR PDBsum; 1ZIJ; -. 7537DR PDBsum; 1ZIK; -. 7538DR PDBsum; 1ZIL; -. 7539DR PDBsum; 1ZIM; -. 7540DR PDBsum; 1ZTA; -. 7541DR PDBsum; 2AHP; -. 7542DR PDBsum; 2B1F; -. 7543DR PDBsum; 2B22; -. 7544DR PDBsum; 2BNI; -. 7545DR PDBsum; 2CCE; -. 7546DR PDBsum; 2CCF; -. 7547DR PDBsum; 2CCN; -. 7548DR PDBsum; 2D3E; -. 7549DR PDBsum; 2DGC; -. 7550DR PDBsum; 2EFR; -. 7551DR PDBsum; 2EFS; -. 7552DR PDBsum; 2G9J; -. 7553DR PDBsum; 2HY6; -. 7554DR PDBsum; 2IPZ; -. 7555DR PDBsum; 2LPB; -. 7556DR PDBsum; 2NRN; -. 7557DR PDBsum; 2O7H; -. 7558DR PDBsum; 2OVN; -. 7559DR PDBsum; 2WG5; -. 7560DR PDBsum; 2WG6; -. 7561DR PDBsum; 2WPY; -. 7562DR PDBsum; 2WPZ; -. 7563DR PDBsum; 2WQ0; -. 7564DR PDBsum; 2WQ1; -. 7565DR PDBsum; 2WQ2; -. 7566DR PDBsum; 2WQ3; -. 7567DR PDBsum; 2Z5H; -. 7568DR PDBsum; 2Z5I; -. 7569DR PDBsum; 2ZTA; -. 7570DR PDBsum; 3AZD; -. 7571DR PDBsum; 3BAS; -. 7572DR PDBsum; 3BAT; -. 7573DR PDBsum; 3CK4; -. 7574DR PDBsum; 3CRP; -. 7575DR PDBsum; 3G9R; -. 7576DR PDBsum; 3GJP; -. 7577DR PDBsum; 3I1G; -. 7578DR PDBsum; 3I5C; -. 7579DR PDBsum; 3K7Z; -. 7580DR PDBsum; 3M48; -. 7581DR PDBsum; 3P8M; -. 7582DR DisProt; DP00083; -. 7583DR ProteinModelPortal; P03069; -. 7584DR SMR; P03069; 101-134, 229-277. 7585DR DIP; DIP-591N; -. 7586DR IntAct; P03069; 5. 7587DR MINT; MINT-395967; -. 7588DR STRING; P03069; -. 7589DR EnsemblFungi; YEL009C; YEL009C; YEL009C. 7590DR GeneID; 856709; -. 7591DR KEGG; sce:YEL009C; -. 7592DR CYGD; YEL009c; -. 7593DR SGD; S000000735; GCN4. 7594DR eggNOG; NOG329891; -. 7595DR KO; K09464; -. 7596DR OMA; ARKLQRM; -. 7597DR OrthoDB; EOG46QB3F; -. 7598DR EvolutionaryTrace; P03069; -. 7599DR NextBio; 982781; -. 7600DR ArrayExpress; P03069; -. 7601DR Genevestigator; P03069; -. 7602DR GermOnline; YEL009C; Saccharomyces cerevisiae. 7603DR GO; GO:0005634; C:nucleus; IDA:SGD. 7604DR GO; GO:0003682; F:chromatin binding; IDA:SGD. 7605DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. 7606DR GO; GO:0001191; F:RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription; IPI:SGD. 7607DR GO; GO:0001190; F:RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription; IMP:SGD. 7608DR GO; GO:0001135; F:RNA polymerase II transcription factor recruiting transcription factor activity; IMP:SGD. 7609DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD. 7610DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IMP:SGD. 7611DR GO; GO:0001084; F:TFIID-class binding transcription factor activity; IPI:SGD. 7612DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW. 7613DR GO; GO:0010691; P:negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels; IMP:SGD. 7614DR GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD. 7615DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:SGD. 7616DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD. 7617DR Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1. 7618DR InterPro; IPR004827; bZIP. 7619DR InterPro; IPR011616; bZIP_1. 7620DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. 7621DR Pfam; PF00170; bZIP_1; 1. 7622DR SMART; SM00338; BRLZ; 1. 7623DR PROSITE; PS50217; BZIP; 1. 7624DR PROSITE; PS00036; BZIP_BASIC; 1. 7625PE 1: Evidence at protein level; 7626KW 3D-structure; Activator; Amino-acid biosynthesis; Complete proteome; 7627KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; 7628KW Transcription; Transcription regulation. 7629FT CHAIN 1 281 General control protein GCN4. 7630FT /FTId=PRO_0000076490. 7631FT DOMAIN 253 274 Leucine-zipper. 7632FT DNA_BIND 231 249 Basic motif. 7633FT REGION 89 100 Required for transcriptional activation. 7634FT REGION 106 125 Required for transcriptional activation. 7635FT MOD_RES 17 17 Phosphoserine. 7636FT MOD_RES 165 165 Phosphothreonine; by PHO85. 7637FT MOD_RES 218 218 Phosphoserine. 7638FT VARIANT 24 24 S -> P (in strain: CLIB 219). 7639FT VARIANT 62 62 P -> S (in strain: CLIB 630 haplotype 7640FT Ha2). 7641FT VARIANT 82 82 T -> A (in strain: CLIB 556 haplotype 7642FT Ha1). 7643FT VARIANT 91 91 D -> A (in strain: CLIB 95, CLIB 219, 7644FT CLIB 382, CLIB 388, CLIB 410, CLIB 413, 7645FT CLIB 556, CLIB 630, K1, R12, R13 7646FT haplotype Ha2, Sigma 1278B haplotype Ha1, 7647FT YIIc12 and YIIc17). 7648FT VARIANT 125 125 D -> A (in strain: CLIB 556 haplotype 7649FT Ha1). 7650FT VARIANT 196 196 D -> E (in strain: CLIB 388, CLIB 410, 7651FT CLIB 413, CLIB 630 haplotype Ha1, K1, 7652FT YIIc12 haplotype Ha2 and YIIc17 haplotype 7653FT Ha1). 7654FT MUTAGEN 97 98 FF->AA: Reduces transcriptional 7655FT activation activity; when associated with 7656FT A-107; A-110; A-113; A-120; A-123 and A- 7657FT 124. 7658FT MUTAGEN 107 107 M->A: Reduces transcriptional activation 7659FT activity; when associated with A-97; A- 7660FT 98; A-110; A-113; A-120; A-123 and A-124. 7661FT MUTAGEN 110 110 Y->A: Reduces transcriptional activation 7662FT activity; when associated with A-97; A- 7663FT 98; A-107; A-113; A-120; A-123 and A-124. 7664FT MUTAGEN 113 113 L->A: Reduces transcriptional activation 7665FT activity; when associated with A-97; A- 7666FT 98; A-107; A-110; A-120; A-123 and A-124. 7667FT MUTAGEN 120 124 WTSLF->ATSAA: Reduces transcriptional 7668FT activation activity; when associated with 7669FT A-97; A-98; A-107; A-110 and A-113. 7670FT CONFLICT 239 281 ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG 7671FT ER -> PGVLVRESCKE (in Ref. 2; AAA65521). 7672FT HELIX 230 248 7673FT HELIX 251 280 7674SQ SEQUENCE 281 AA; 31310 MW; 2ED1B8E35D509578 CRC64; 7675 MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD 7676 TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW 7677 TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK 7678 KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR 7679 RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R 7680// 7681ID HBA_HUMAN Reviewed; 142 AA. 7682AC P69905; P01922; Q1HDT5; Q3MIF5; Q53F97; Q96KF1; Q9NYR7; Q9UCM0; 7683DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 7684DT 23-JAN-2007, sequence version 2. 7685DT 13-JUN-2012, entry version 108. 7686DE RecName: Full=Hemoglobin subunit alpha; 7687DE AltName: Full=Alpha-globin; 7688DE AltName: Full=Hemoglobin alpha chain; 7689GN Name=HBA1; 7690GN and 7691GN Name=HBA2; 7692OS Homo sapiens (Human). 7693OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 7694OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 7695OC Catarrhini; Hominidae; Homo. 7696OX NCBI_TaxID=9606; 7697RN [1] 7698RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1). 7699RX MEDLINE=81088339; PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5; 7700RA Michelson A.M., Orkin S.H.; 7701RT "The 3' untranslated regions of the duplicated human alpha-globin 7702RT genes are unexpectedly divergent."; 7703RL Cell 22:371-377(1980). 7704RN [2] 7705RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2). 7706RX MEDLINE=80137531; PubMed=6244294; 7707RA Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K., 7708RA Deriel J.K., Forget B.G., Weissman S.M.; 7709RT "Nucleotide sequence of the coding portion of human alpha globin 7710RT messenger RNA."; 7711RL J. Biol. Chem. 255:2807-2815(1980). 7712RN [3] 7713RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2). 7714RX MEDLINE=81175088; PubMed=6452630; DOI=10.1073/pnas.77.12.7054; 7715RA Liebhaber S.A., Goossens M.J., Kan Y.W.; 7716RT "Cloning and complete nucleotide sequence of human 5'-alpha-globin 7717RT gene."; 7718RL Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980). 7719RN [4] 7720RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 7721RX PubMed=6946451; DOI=10.1073/pnas.78.8.5041; 7722RA Orkin S.H., Goff S.C., Hechtman R.L.; 7723RT "Mutation in an intervening sequence splice junction in man."; 7724RL Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981). 7725RN [5] 7726RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32. 7727RX MEDLINE=21303311; PubMed=11410421; 7728RA Zhao Y., Xu X.; 7729RT "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha- 7730RT thalassemia in a Chinese family with HbH disease."; 7731RL Haematologica 86:541-542(2001). 7732RN [6] 7733RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1). 7734RX MEDLINE=21295668; PubMed=11402454; 7735RA Zhao Y., Zhong M., Liu Z., Xu X.; 7736RT "Rapid detection of the common alpha-thalassemia-2 determinants by PCR 7737RT assay."; 7738RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001). 7739RN [7] 7740RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2). 7741RX PubMed=16728641; DOI=10.1126/science.1126431; 7742RA De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J., 7743RA Ayyub H., Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P., 7744RA Cheng J.-F., Rubin E.M., Wood W.G., Bowden D., Higgs D.R.; 7745RT "A regulatory SNP causes a human genetic disease by creating a new 7746RT transcriptional promoter."; 7747RL Science 312:1215-1217(2006). 7748RN [8] 7749RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2). 7750RC TISSUE=Blood; 7751RA Kutlar F., Leithner C., Kutlar A.; 7752RT "Rapid sequencing of mRNA of the human alpha two globin, directly 7753RT isolated from reticulocytes in whole blood."; 7754RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. 7755RN [9] 7756RP NUCLEOTIDE SEQUENCE [MRNA] (HBA1). 7757RC TISSUE=Blood; 7758RA Kutlar F., Leithner C., Kutlar A.; 7759RT "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated 7760RT region is different than alpha two globin."; 7761RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. 7762RN [10] 7763RP NUCLEOTIDE SEQUENCE [MRNA]. 7764RC TISSUE=Blood; 7765RA Kutlar F., Holley L., Leithner C., Kutlar A.; 7766RT "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)' 7767RT mutation was detected on the alpha-1 globin mRNA by sequencing of 7768RT cDNA."; 7769RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. 7770RN [11] 7771RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63. 7772RC TISSUE=Blood; 7773RA Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.; 7774RT "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2 7775RT globin gene of an Hispanic girl."; 7776RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. 7777RN [12] 7778RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT G-PHILADELPHIA 7779RP LYS-69. 7780RA Kutlar F., Davis D.H., Nechtman J., Elam D.; 7781RT "Hb G-Philadelphia (Alpha,Codon 68;AAC>AAG/Asn>Lys)in black is 7782RT detected on a chromosome that carries alpha 3.7 kb deletion showed 7783RT completely normal alpha-2 globin gene sequence."; 7784RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. 7785RN [13] 7786RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 7787RC TISSUE=Thymus; 7788RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; 7789RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. 7790RN [14] 7791RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2). 7792RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; 7793RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., 7794RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., 7795RA Higgs D.R.; 7796RT "Sequence, structure and pathology of the fully annotated terminal 2 7797RT Mb of the short arm of human chromosome 16."; 7798RL Hum. Mol. Genet. 10:339-352(2001). 7799RN [15] 7800RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2). 7801RX PubMed=15616553; DOI=10.1038/nature03187; 7802RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., 7803RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., 7804RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., 7805RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., 7806RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., 7807RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., 7808RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., 7809RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., 7810RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., 7811RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., 7812RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., 7813RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., 7814RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., 7815RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., 7816RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., 7817RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., 7818RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., 7819RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., 7820RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., 7821RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., 7822RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., 7823RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., 7824RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., 7825RA Rubin E.M., Pennacchio L.A.; 7826RT "The sequence and analysis of duplication-rich human chromosome 16."; 7827RL Nature 432:988-994(2004). 7828RN [16] 7829RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HBA1 AND HBA2). 7830RC TISSUE=Bone marrow, Brain, Lung, and Spleen; 7831RX PubMed=15489334; DOI=10.1101/gr.2596504; 7832RG The MGC Project Team; 7833RT "The status, quality, and expansion of the NIH full-length cDNA 7834RT project: the Mammalian Gene Collection (MGC)."; 7835RL Genome Res. 14:2121-2127(2004). 7836RN [17] 7837RP PROTEIN SEQUENCE OF 2-142. 7838RX PubMed=13872627; 7839RA Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G., 7840RA Rudloff V., Wittmann-Liebold B.; 7841RT "The constitution of normal adult human haemoglobin."; 7842RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961). 7843RN [18] 7844RP PROTEIN SEQUENCE OF 2-142. 7845RX PubMed=13954546; 7846RA Hill R.J., Konigsberg W.; 7847RT "The structure of human hemoglobin: IV. The chymotryptic digestion of 7848RT the alpha chain of human hemoglobin."; 7849RL J. Biol. Chem. 237:3151-3156(1962). 7850RN [19] 7851RP PROTEIN SEQUENCE OF 2-142. 7852RX PubMed=14093912; DOI=10.1021/bi00906a030; 7853RA Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.; 7854RT "The amino acid sequence of the alpha chain of human fetal 7855RT hemoglobin."; 7856RL Biochemistry 2:1353-1357(1963). 7857RN [20] 7858RP PROTEIN SEQUENCE OF 2-32. 7859RC TISSUE=Platelet; 7860RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; 7861RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., 7862RA Thomas G.R., Vandekerckhove J.; 7863RT "Exploring proteomes and analyzing protein processing by mass 7864RT spectrometric identification of sorted N-terminal peptides."; 7865RL Nat. Biotechnol. 21:566-569(2003). 7866RN [21] 7867RP PROTEIN SEQUENCE OF 128-142, AND VARIANT ETHIOPIA HIS-141. 7868RC TISSUE=Umbilical cord blood; 7869RX MEDLINE=93053735; PubMed=1428951; 7870RA Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J.; 7871RT "Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2."; 7872RL Hemoglobin 16:441-443(1992). 7873RN [22] 7874RP GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, AND LACK OF GLYCATION 7875RP AT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100. 7876RX PubMed=7358733; 7877RA Shapiro R., McManus M.J., Zalut C., Bunn H.F.; 7878RT "Sites of nonenzymatic glycosylation of human hemoglobin A."; 7879RL J. Biol. Chem. 255:3120-3127(1980). 7880RN [23] 7881RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-43, AND MASS 7882RP SPECTROMETRY. 7883RC TISSUE=Lung carcinoma; 7884RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; 7885RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., 7886RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., 7887RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., 7888RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., 7889RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; 7890RT "Global survey of phosphotyrosine signaling identifies oncogenic 7891RT kinases in lung cancer."; 7892RL Cell 131:1190-1203(2007). 7893RN [24] 7894RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 7895RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; 7896RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., 7897RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; 7898RT "Initial characterization of the human central proteome."; 7899RL BMC Syst. Biol. 5:17-17(2011). 7900RN [25] 7901RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN. 7902RX MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4; 7903RA Fermi G.; 7904RT "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5- 7905RT A resolution: refinement of the atomic model."; 7906RL J. Mol. Biol. 97:237-256(1975). 7907RN [26] 7908RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). 7909RX PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3; 7910RA Baldwin J.M.; 7911RT "The structure of human carbonmonoxy haemoglobin at 2.7-A 7912RT resolution."; 7913RL J. Mol. Biol. 136:103-128(1980). 7914RN [27] 7915RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE. 7916RX MEDLINE=92381041; PubMed=1512262; 7917RA Silva M.M., Rogers P.H., Arnone A.; 7918RT "A third quaternary structure of human hemoglobin A at 1.7-A 7919RT resolution."; 7920RL J. Biol. Chem. 267:17248-17256(1992). 7921RN [28] 7922RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2. 7923RX MEDLINE=98332748; PubMed=9665850; DOI=10.1006/jmbi.1998.1868; 7924RA Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., 7925RA Baker E.N.; 7926RT "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy 7927RT form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution."; 7928RL J. Mol. Biol. 280:475-484(1998). 7929RN [29] 7930RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 7931RP INS. 7932RX MEDLINE=93192190; PubMed=8448109; DOI=10.1021/bi00061a007; 7933RA Kavanaugh J.S., Moo-Penn W.F., Arnone A.; 7934RT "Accommodation of insertions in helices: the mutation in hemoglobin 7935RT Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha 7936RT bulge."; 7937RL Biochemistry 32:2509-2513(1993). 7938RN [30] 7939RP VARIANT AL-AIN ABU DHABI ASP-19. 7940RX MEDLINE=93053723; PubMed=1428941; 7941RA Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y., 7942RA Kister J., Galacteros F., Wajcman H.; 7943RT "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin 7944RT variant discovered in an Emiratee family."; 7945RL Hemoglobin 16:355-362(1992). 7946RN [31] 7947RP VARIANT ATAGO TYR-86. 7948RX MEDLINE=72030550; PubMed=5115619; 7949RA Fujiwara N., Maekawa T., Matsuda G.; 7950RT "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human 7951RT hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and 7952RT myoglobins. VI."; 7953RL Int. J. Protein Res. 3:35-39(1971). 7954RN [32] 7955RP VARIANT AUCKLAND ASN-88. 7956RX MEDLINE=97463291; PubMed=9322075; 7957RA Brennan S.O., Matthews J.R.; 7958RT "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal 7959RT histidine identified by electrospray mass spectrometry."; 7960RL Hemoglobin 21:393-403(1997). 7961RN [33] 7962RP VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75. 7963RA Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J., 7964RA Jones R.T.; 7965RT "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) 7966RT Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn)."; 7967RL Biochim. Biophys. Acta 336:344-360(1974). 7968RN [34] 7969RP VARIANT CEMENELUM TRP-93. 7970RX PubMed=8148419; DOI=10.1007/BF01715134; 7971RA Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.; 7972RT "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the 7973RT alpha 1/beta 2 interface that displays a moderate increase in oxygen 7974RT affinity."; 7975RL Ann. Hematol. 68:73-76(1994). 7976RN [35] 7977RP VARIANTS CHONGQING ARG-3 AND HARBIN MET-17. 7978RX MEDLINE=85130255; PubMed=6526652; 7979RA Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C., 7980RA Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z., 7981RA Duan Y.-Q., Zhang G.-Y.; 7982RT "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin 7983RT [alpha 16(A14)Lys-->Met] found in China."; 7984RL Hemoglobin 8:569-581(1984). 7985RN [36] 7986RP VARIANT CLINIC LYS-61 DEL. 7987RX PubMed=10206681; 7988RX DOI=10.1002/(SICI)1098-1004(1998)11:5<412::AID-HUMU14>3.3.CO;2-I; 7989RA Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.; 7990RT "Alpha-thalassaemia due to a single codon deletion in the alpha 1- 7991RT globin gene. Computational structural analysis of the new alpha-chain 7992RT variant."; 7993RL Hum. Mutat. 11:412-412(1998). 7994RN [37] 7995RP VARIANT DAVENPORT HIS-79. 7996RX MEDLINE=91331854; PubMed=2101836; 7997RA Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K., 7998RA Huisman T.H.J.; 7999RT "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2."; 8000RL Hemoglobin 14:599-605(1990). 8001RN [38] 8002RP VARIANT EVANS MET-63. 8003RX MEDLINE=90109650; PubMed=2606724; 8004RA Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C., 8005RA Lutcher C.L., Felice A.E., Huisman T.H.J.; 8006RT "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin 8007RT causing a mild hemolytic anemia."; 8008RL Hemoglobin 13:557-566(1989). 8009RN [39] 8010RP VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46. 8011RX MEDLINE=89323437; PubMed=2752146; 8012RA Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.; 8013RT "Locus assignment of two alpha-globin structural mutants from the 8014RT Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish 8015RT Town (alpha 27 Val)."; 8016RL Blood 74:833-835(1989). 8017RN [40] 8018RP VARIANT GODAVARI THR-96. 8019RX MEDLINE=98153063; PubMed=9494044; 8020RA Wajcman H., Kister J., Riou J., Galacteros F., Girot R., 8021RA Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.; 8022RT "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid 8023RT substitution in the alpha 1 beta 2 interface that modifies the 8024RT electrophoretic mobility of hemoglobin."; 8025RL Hemoglobin 22:11-22(1998). 8026RN [41] 8027RP VARIANT GRADY GLU-PHE-THR-119 INS. 8028RX MEDLINE=75010592; PubMed=4528583; DOI=10.1073/pnas.71.8.3270; 8029RA Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.; 8030RT "Hemoglobin Grady: the first example of a variant with elongated 8031RT chains due to an insertion of residues."; 8032RL Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974). 8033RN [42] 8034RP VARIANT HANAMAKI GLU-140. 8035RX MEDLINE=92340291; PubMed=1634363; 8036RA Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.; 8037RT "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu 8038RT beta 2, found in a Japanese family."; 8039RL Hemoglobin 16:67-71(1992). 8040RN [43] 8041RP VARIANT HANDA MET-91. 8042RX MEDLINE=83056269; PubMed=6815131; 8043RA Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.; 8044RT "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and 8045RT biosynthesis of a new slightly higher oxygen affinity variant."; 8046RL Hemoglobin 6:379-389(1982). 8047RN [44] 8048RP VARIANT HASHARON HIS-48. 8049RX MEDLINE=69165810; PubMed=5780195; DOI=10.1172/JCI106041; 8050RA Charache S., Mondzac A.M., Gessner U.; 8051RT "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found 8052RT in low concentration."; 8053RL J. Clin. Invest. 48:834-847(1969). 8054RN [45] 8055RP VARIANT HOBART ARG-21. 8056RX MEDLINE=88006902; PubMed=3654264; 8057RA Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D., 8058RA Jupe D.M.D., Baikie M.J.; 8059RT "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain 8060RT hemoglobin variant."; 8061RL Hemoglobin 11:211-220(1987). 8062RN [46] 8063RP VARIANT INKSTER VAL-86. 8064RX MEDLINE=74302151; PubMed=4212045; 8065RX DOI=10.1111/j.1365-2141.1974.tb00489.x; 8066RA Reed R.E., Winter W.P., Rucknagel D.L.; 8067RT "Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2) 8068RT coexisting with beta-thalassaemia in a Caucasian family."; 8069RL Br. J. Haematol. 26:475-484(1974). 8070RN [47] 8071RP VARIANT KANAGAWA MET-41. 8072RX MEDLINE=92340282; PubMed=1634355; 8073RA Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., 8074RA Harano K., Imai K.; 8075RT "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with 8076RT an increased oxygen affinity."; 8077RL Hemoglobin 16:1-10(1992). 8078RN [48] 8079RP VARIANT KURDISTAN TYR-48. 8080RX MEDLINE=94252883; PubMed=8195005; 8081RA Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C., 8082RA Heister J.G.A.M., Amons R., Bernini L.F.; 8083RT "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in 8084RT combination with beta (0)-thalassemia."; 8085RL Hemoglobin 18:11-18(1994). 8086RN [49] 8087RP VARIANT KUROSAKI GLU-8. 8088RX MEDLINE=96031515; PubMed=7558876; 8089RA Harano T., Harano K., Imai K., Murakami T., Matsubara H.; 8090RT "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found 8091RT in a Japanese woman."; 8092RL Hemoglobin 19:197-201(1995). 8093RN [50] 8094RP VARIANT J-MEERUT/J-BIRMINGHAM GLU-121. 8095RX MEDLINE=95229430; PubMed=7713747; 8096RA Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.; 8097RT "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 8098RT 120(H3)Ala-->Glu]."; 8099RL Hemoglobin 18:433-435(1994). 8100RN [51] 8101RP VARIANT MELUSINE SER-115. 8102RX MEDLINE=94124250; PubMed=8294199; 8103RA Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.; 8104RT "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin 8105RT variant."; 8106RL Hemoglobin 17:397-405(1993). 8107RN [52] 8108RP VARIANT MONTGOMERY ARG-49. 8109RX MEDLINE=75109326; PubMed=1115799; 8110RA Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., 8111RA Atkins R.; 8112RT "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) 8113RT and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."; 8114RL Biochim. Biophys. Acta 379:28-32(1975). 8115RN [53] 8116RP VARIANT PETAH TIKVA ASP-111. 8117RX MEDLINE=81134478; PubMed=7470621; 8118RA Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., 8119RA Kirschman C.; 8120RT "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new 8121RT unstable variant with alpha-thalassemia-like expression."; 8122RL Blood 57:705-711(1981). 8123RN [54] 8124RP VARIANT PHNOM PENH ILE-118 INS. 8125RX MEDLINE=98112407; PubMed=9452028; 8126RA Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D., 8127RA Galacteros F.; 8128RT "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence 8129RT for a hotspot for insertion of residues in the third exon of the 8130RT alpha1-globin gene."; 8131RL Hum. Mutat. Suppl. 1:S20-S22(1998). 8132RN [55] 8133RP VARIANT PORT HURON ARG-57. 8134RX MEDLINE=92202056; PubMed=1802882; 8135RA Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.; 8136RT "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant."; 8137RL Hemoglobin 15:381-391(1991). 8138RN [56] 8139RP VARIANT SAWARA ALA-7. 8140RX MEDLINE=74008827; PubMed=4744335; 8141RA Sumida I., Ohta Y., Imamura T., Yanase T.; 8142RT "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine."; 8143RL Biochim. Biophys. Acta 322:23-26(1973). 8144RN [57] 8145RP VARIANT SHENYANG GLU-27. 8146RX MEDLINE=83135048; PubMed=7161109; 8147RA Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.; 8148RT "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable 8149RT variant found in China."; 8150RL Hemoglobin 6:625-628(1982). 8151RN [58] 8152RP VARIANT SUAN-DOK ARG-110. 8153RX MEDLINE=80006169; PubMed=478977; 8154RA Sanguansermsri T., Matragoon S., Changloah L., Flatz G.; 8155RT "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): 8156RT an unstable variant associated with alpha-thalassemia."; 8157RL Hemoglobin 3:161-174(1979). 8158RN [59] 8159RP INVOLVEMENT IN HEIBAN, AND VARIANT TOYAMA ARG-137. 8160RX PubMed=2833478; 8161RA Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T.; 8162RT "Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]: 8163RT detection and identification by in vitro biosynthesis with radioactive 8164RT amino acids."; 8165RL Hemoglobin 11:539-556(1987). 8166RN [60] 8167RP VARIANT SUN PRAIRIE PRO-131. 8168RX MEDLINE=91177710; PubMed=2079430; 8169RA Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B., 8170RA Webber B.B., Codrington J.F., Huisman T.H.J.; 8171RT "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable 8172RT variant occurring in low quantities."; 8173RL Hemoglobin 14:479-489(1990). 8174RN [61] 8175RP VARIANT SWAN RIVER GLY-7. 8176RX MEDLINE=96351655; PubMed=8745434; 8177RA Harano T., Harano K., Imai K., Terunuma S.; 8178RT "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man."; 8179RL Hemoglobin 20:75-78(1996). 8180RN [62] 8181RP VARIANT THIONVILLE GLU-2. 8182RX MEDLINE=92316953; PubMed=1618774; 8183RA Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S., 8184RA Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C., 8185RA Rosa J., Wajcman H.; 8186RT "Hemoglobin Thionville. An alpha-chain variant with a substitution of 8187RT a glutamate for valine at NA-1 and having an acetylated methionine NH2 8188RT terminus."; 8189RL J. Biol. Chem. 267:12682-12691(1992). 8190RN [63] 8191RP VARIANT TUNIS-BIZERTE PRO-130. 8192RX MEDLINE=95306384; PubMed=7786798; 8193RX DOI=10.1111/j.1365-2141.1995.tb03382.x; 8194RA Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.; 8195RT "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro 8196RT unstable variant with thalassaemic phenotype."; 8197RL Br. J. Haematol. 90:71-76(1995). 8198RN [64] 8199RP VARIANT TURRIFF GLU-100. 8200RX MEDLINE=92340284; PubMed=1634357; 8201RA Langdown J.V., Davidson R.J., Williamson D.; 8202RT "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the 8203RT interference of abnormal hemoglobins in Hb A1c determination."; 8204RL Hemoglobin 16:11-17(1992). 8205RN [65] 8206RP VARIANT VAL DE MARNE ARG-134. 8207RX MEDLINE=94124251; PubMed=8294200; 8208RA Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.; 8209RT "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant 8210RT with moderate increase in oxygen affinity."; 8211RL Hemoglobin 17:407-417(1993). 8212RN [66] 8213RP VARIANT WESTMEAD GLN-123. 8214RX MEDLINE=92155975; PubMed=1686260; 8215RA Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.; 8216RT "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase 8217RT chain reaction and Stu I cleavage."; 8218RL Hemoglobin 15:291-295(1991). 8219RN [67] 8220RP VARIANT WOODVILLE TYR-7. 8221RX MEDLINE=86167529; PubMed=3754246; 8222RA Como P.F., Barber S., Sage R.E., Kronenberg H.; 8223RT "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine."; 8224RL Hemoglobin 10:135-141(1986). 8225RN [68] 8226RP VARIANT YUDA ASP-131. 8227RX MEDLINE=93053734; PubMed=1428950; 8228RA Fujisawa K., Hattori Y., Ohba Y., Ando S.; 8229RT "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with 8230RT low oxygen affinity."; 8231RL Hemoglobin 16:435-439(1992). 8232RN [69] 8233RP VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS. 8234RX MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961; 8235RA Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., 8236RA Melevendi C., Rasore A., Galacteros F.; 8237RT "Two new human hemoglobin variants caused by unusual mutational 8238RT events: Hb Zaire contains a five residue repetition within the alpha- 8239RT chain and Hb Duino has two residues substituted in the beta-chain."; 8240RL Hum. Genet. 89:676-680(1992). 8241RN [70] 8242RP VARIANT HBH VAL-63 DEL. 8243RX PubMed=10569720; 8244RA Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C., 8245RA Kattamis C., Bernini L.F.; 8246RT "Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame' 8247RT deletion causing alpha-thalassemia."; 8248RL Hemoglobin 23:317-324(1999). 8249RN [71] 8250RP VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104. 8251RX PubMed=10569723; 8252RA Lacan P., Francina A., Souillet G., Aubry M., Couprie N., 8253RA Dementhon L., Becchi M.; 8254RT "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln, 8255RT alpha2], a variant on the distal histidine, and Hb CHarolles 8256RT [alpha103(G10)His-Tyr, alpha1]."; 8257RL Hemoglobin 23:345-352(1999). 8258RN [72] 8259RP VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127. 8260RX PubMed=14576901; DOI=10.1590/S0100-879X2003001100004; 8261RA Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.; 8262RT "Screening for mutations in human alpha-globin genes by nonradioactive 8263RT single-strand conformation polymorphism."; 8264RL Braz. J. Med. Biol. Res. 36:1471-1474(2003). 8265RN [73] 8266RP VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT 8267RP ALA-95. 8268RX PubMed=15495251; DOI=10.1002/ajh.20184; 8269RA Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E., 8270RA Lakka V., Santacroce R., Abraham D.J., Asakura T.; 8271RT "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant 8272RT with very low oxygen affinity."; 8273RL Am. J. Hematol. 77:268-276(2004). 8274RN [74] 8275RP VARIANT PLASENCIA ARG-126. 8276RX PubMed=15921163; DOI=10.1081/HEM-200058578; 8277RA Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M., 8278RA Mateo M., Salvador M., Benavente C.; 8279RT "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia: 8280RT Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2)."; 8281RL Hemoglobin 29:113-117(2005). 8282CC -!- FUNCTION: Involved in oxygen transport from the lung to the 8283CC various peripheral tissues. 8284CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 8285CC adult hemoglobin A (HbA); two alpha chains and two delta chains in 8286CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon 8287CC chains in early embryonic hemoglobin Gower-2; two alpha chains and 8288CC two gamma chains in fetal hemoglobin F (HbF). 8289CC -!- INTERACTION: 8290CC P68871:HBB; NbExp=19; IntAct=EBI-714680, EBI-715554; 8291CC -!- TISSUE SPECIFICITY: Red blood cells. 8292CC -!- PTM: The initiator Met is not cleaved in variant Thionville and is 8293CC acetylated. 8294CC -!- DISEASE: Defects in HBA1 may be a cause of Heinz body anemias 8295CC (HEIBAN) [MIM:140700]. This is a form of non-spherocytic hemolytic 8296CC anemia of Dacie type 1. After splenectomy, which has little 8297CC benefit, basophilic inclusions called Heinz bodies are 8298CC demonstrable in the erythrocytes. Before splenectomy, diffuse or 8299CC punctate basophilia may be evident. Most of these cases are 8300CC probably instances of hemoglobinopathy. The hemoglobin 8301CC demonstrates heat lability. Heinz bodies are observed also with 8302CC the Ivemark syndrome (asplenia with cardiovascular anomalies) and 8303CC with glutathione peroxidase deficiency. 8304CC -!- DISEASE: Defects in HBA1 are the cause of alpha-thalassemia (A- 8305CC THAL) [MIM:604131]. The thalassemias are the most common monogenic 8306CC diseases and occur mostly in Mediterranean and Southeast Asian 8307CC populations. The hallmark of alpha-thalassemia is an imbalance in 8308CC globin-chain production in the adult HbA molecule. The level of 8309CC alpha chain production can range from none to very nearly normal 8310CC levels. Deletion of both copies of each of the two alpha-globin 8311CC genes causes alpha(0)-thalassemia, also known as homozygous alpha 8312CC thalassemia. Due to the complete absence of alpha chains, the 8313CC predominant fetal hemoglobin is a tetramer of gamma-chains (Bart 8314CC hemoglobin) that has essentially no oxygen carrying capacity. This 8315CC causes oxygen starvation in the fetal tissues leading to prenatal 8316CC lethality or early neonatal death. The loss of three alpha genes 8317CC results in high levels of a tetramer of four beta chains 8318CC (hemoglobin H), causing a severe and life-threatening anemia known 8319CC as hemoglobin H disease. Untreated, most patients die in childhood 8320CC or early adolescence. The loss of two alpha genes results in mild 8321CC alpha-thalassemia, also known as heterozygous alpha-thalassemia. 8322CC Affected individuals have small red cells and a mild anemia 8323CC (microcytosis). If three of the four alpha-globin genes are 8324CC functional, individuals are completely asymptomatic. Some rare 8325CC forms of alpha-thalassemia are due to point mutations (non- 8326CC deletional alpha-thalassemia). The thalassemic phenotype is due to 8327CC unstable globin alpha chains that are rapidly catabolized prior to 8328CC formation of the alpha-beta heterotetramers. 8329CC -!- DISEASE: Note=Alpha(0)-thalassemia is associated with non-immune 8330CC hydrops fetalis, a generalized edema of the fetus with fluid 8331CC accumulation in the body cavities due to non-immune causes. Non- 8332CC immune hydrops fetalis is not a diagnosis in itself but a symptom, 8333CC a feature of many genetic disorders, and the end-stage of a wide 8334CC variety of disorders. 8335CC -!- DISEASE: Defects in HBA1 are the cause of hemoglobin H disease 8336CC (HBH) [MIM:613978]. HBH is a form of alpha-thalassemia due to the 8337CC loss of three alpha genes. This results in high levels of a 8338CC tetramer of four beta chains (hemoglobin H), causing a severe and 8339CC life-threatening anemia. Untreated, most patients die in childhood 8340CC or early adolescence. 8341CC -!- MISCELLANEOUS: Gives blood its red color. 8342CC -!- SIMILARITY: Belongs to the globin family. 8343CC -!- SEQUENCE CAUTION: 8344CC Sequence=BAD97112.1; Type=Erroneous initiation; 8345CC -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and 8346CC thalassemias; 8347CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1"; 8348CC -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and 8349CC thalassemias; 8350CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2"; 8351CC -!- WEB RESOURCE: Name=GeneReviews; 8352CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBA1"; 8353CC -!- WEB RESOURCE: Name=GeneReviews; 8354CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBA2"; 8355CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and 8356CC polymorphism database; 8357CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBA1"; 8358CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry; 8359CC URL="http://en.wikipedia.org/wiki/Hemoglobin"; 8360CC ----------------------------------------------------------------------- 8361CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 8362CC Distributed under the Creative Commons Attribution-NoDerivs License 8363CC ----------------------------------------------------------------------- 8364DR EMBL; J00153; AAB59407.1; -; Genomic_DNA. 8365DR EMBL; J00153; AAB59408.1; -; Genomic_DNA. 8366DR EMBL; V00491; CAA23750.1; -; Genomic_DNA. 8367DR EMBL; V00493; CAA23752.1; -; mRNA. 8368DR EMBL; V00488; CAA23748.1; -; Genomic_DNA. 8369DR EMBL; V00516; CAA23774.1; -; Genomic_DNA. 8370DR EMBL; AF230076; AAF72612.1; -; Genomic_DNA. 8371DR EMBL; AF525460; AAM83102.1; -; Genomic_DNA. 8372DR EMBL; DQ431198; ABD95910.1; -; Genomic_DNA. 8373DR EMBL; DQ431198; ABD95911.1; -; Genomic_DNA. 8374DR EMBL; AF097635; AAC72839.1; -; mRNA. 8375DR EMBL; AF105974; AAC97373.1; -; mRNA. 8376DR EMBL; AF349571; AAK37554.1; -; mRNA. 8377DR EMBL; AF536204; AAN04486.1; -; Genomic_DNA. 8378DR EMBL; DQ499017; ABF56144.1; -; Genomic_DNA. 8379DR EMBL; DQ499018; ABF56145.1; -; Genomic_DNA. 8380DR EMBL; AK223392; BAD97112.1; ALT_INIT; mRNA. 8381DR EMBL; AE006462; AAK61215.1; -; Genomic_DNA. 8382DR EMBL; AE006462; AAK61216.1; -; Genomic_DNA. 8383DR EMBL; Z84721; CAB06554.1; -; Genomic_DNA. 8384DR EMBL; Z84721; CAB06555.1; -; Genomic_DNA. 8385DR EMBL; BC005931; AAH05931.1; -; mRNA. 8386DR EMBL; BC008572; AAH08572.1; -; mRNA. 8387DR EMBL; BC032122; AAH32122.1; -; mRNA. 8388DR EMBL; BC050661; AAH50661.1; -; mRNA. 8389DR EMBL; BC101846; AAI01847.1; -; mRNA. 8390DR EMBL; BC101848; AAI01849.1; -; mRNA. 8391DR IPI; IPI00410714; -. 8392DR PIR; A90807; HAHU. 8393DR PIR; C93303; HACZP. 8394DR PIR; I58217; HACZ. 8395DR RefSeq; NP_000508.1; NM_000517.4. 8396DR RefSeq; NP_000549.1; NM_000558.3. 8397DR UniGene; Hs.449630; -. 8398DR UniGene; Hs.654744; -. 8399DR PDB; 1A00; X-ray; 2.00 A; A/C=2-142. 8400DR PDB; 1A01; X-ray; 1.80 A; A/C=2-142. 8401DR PDB; 1A0U; X-ray; 2.14 A; A/C=2-142. 8402DR PDB; 1A0Z; X-ray; 2.00 A; A/C=2-142. 8403DR PDB; 1A3N; X-ray; 1.80 A; A/C=2-142. 8404DR PDB; 1A3O; X-ray; 1.80 A; A/C=2-142. 8405DR PDB; 1A9W; X-ray; 2.90 A; A/C=2-142. 8406DR PDB; 1ABW; X-ray; 2.00 A; A=2-142. 8407DR PDB; 1ABY; X-ray; 2.60 A; A=2-142. 8408DR PDB; 1AJ9; X-ray; 2.20 A; A=2-142. 8409DR PDB; 1B86; X-ray; 2.50 A; A/C=2-142. 8410DR PDB; 1BAB; X-ray; 1.50 A; A/C=3-142. 8411DR PDB; 1BBB; X-ray; 1.70 A; A/C=2-142. 8412DR PDB; 1BIJ; X-ray; 2.30 A; A/C=2-142. 8413DR PDB; 1BUW; X-ray; 1.90 A; A/C=2-142. 8414DR PDB; 1BZ0; X-ray; 1.50 A; A/C=2-142. 8415DR PDB; 1BZ1; X-ray; 1.59 A; A/C=2-142. 8416DR PDB; 1BZZ; X-ray; 1.59 A; A/C=3-142. 8417DR PDB; 1C7B; X-ray; 1.80 A; A/C=3-142. 8418DR PDB; 1C7C; X-ray; 1.80 A; A=2-142. 8419DR PDB; 1C7D; X-ray; 1.80 A; A=2-142. 8420DR PDB; 1CLS; X-ray; 1.90 A; A/C=2-142. 8421DR PDB; 1CMY; X-ray; 3.00 A; A/C=2-142. 8422DR PDB; 1COH; X-ray; 2.90 A; A/C=2-142. 8423DR PDB; 1DKE; X-ray; 2.10 A; A/C=2-142. 8424DR PDB; 1DXT; X-ray; 1.70 A; A/C=2-142. 8425DR PDB; 1DXU; X-ray; 1.70 A; A/C=2-142. 8426DR PDB; 1DXV; X-ray; 1.70 A; A/C=2-142. 8427DR PDB; 1FDH; X-ray; 2.50 A; A/B=2-142. 8428DR PDB; 1FN3; X-ray; 2.48 A; A/C=2-142. 8429DR PDB; 1G9V; X-ray; 1.85 A; A/C=2-142. 8430DR PDB; 1GBU; X-ray; 1.80 A; A/C=2-142. 8431DR PDB; 1GBV; X-ray; 2.00 A; A/C=2-142. 8432DR PDB; 1GLI; X-ray; 2.50 A; A/C=3-142. 8433DR PDB; 1GZX; X-ray; 2.10 A; A/C=2-142. 8434DR PDB; 1HAB; X-ray; 2.30 A; A/C=2-142. 8435DR PDB; 1HAC; X-ray; 2.60 A; A/C=2-142. 8436DR PDB; 1HBA; X-ray; 2.10 A; A/C=2-142. 8437DR PDB; 1HBB; X-ray; 1.90 A; A/C=2-142. 8438DR PDB; 1HBS; X-ray; 3.00 A; A/C/E/G=2-141. 8439DR PDB; 1HCO; X-ray; 2.70 A; A=2-142. 8440DR PDB; 1HDB; X-ray; 2.20 A; A/C=2-142. 8441DR PDB; 1HGA; X-ray; 2.10 A; A/C=2-142. 8442DR PDB; 1HGB; X-ray; 2.10 A; A/C=2-142. 8443DR PDB; 1HGC; X-ray; 2.10 A; A/C=2-142. 8444DR PDB; 1HHO; X-ray; 2.10 A; A=2-141. 8445DR PDB; 1IRD; X-ray; 1.25 A; A=2-142. 8446DR PDB; 1J3Y; X-ray; 1.55 A; A/C/E/G=2-142. 8447DR PDB; 1J3Z; X-ray; 1.60 A; A/C/E/G=2-142. 8448DR PDB; 1J40; X-ray; 1.45 A; A/C/E/G=2-142. 8449DR PDB; 1J41; X-ray; 1.45 A; A/C/E/G=2-142. 8450DR PDB; 1J7S; X-ray; 2.20 A; A/C=3-142. 8451DR PDB; 1J7W; X-ray; 2.00 A; A/C=3-142. 8452DR PDB; 1J7Y; X-ray; 1.70 A; A/C=3-142. 8453DR PDB; 1JY7; X-ray; 3.20 A; A/C/P/R/U/W=2-142. 8454DR PDB; 1K0Y; X-ray; 1.87 A; A/C=2-142. 8455DR PDB; 1K1K; X-ray; 2.00 A; A=2-142. 8456DR PDB; 1KD2; X-ray; 1.87 A; A/C=2-142. 8457DR PDB; 1LFL; X-ray; 2.70 A; A/C/P/R=2-142. 8458DR PDB; 1LFQ; X-ray; 2.60 A; A=2-142. 8459DR PDB; 1LFT; X-ray; 2.60 A; A=2-142. 8460DR PDB; 1LFV; X-ray; 2.80 A; A=2-142. 8461DR PDB; 1LFY; X-ray; 3.30 A; A=2-142. 8462DR PDB; 1LFZ; X-ray; 3.10 A; A=2-142. 8463DR PDB; 1LJW; X-ray; 2.16 A; A=2-142. 8464DR PDB; 1M9P; X-ray; 2.10 A; A/C=2-142. 8465DR PDB; 1MKO; X-ray; 2.18 A; A/C=2-142. 8466DR PDB; 1NEJ; X-ray; 2.10 A; A/C=2-142. 8467DR PDB; 1NIH; X-ray; 2.60 A; A/C=2-142. 8468DR PDB; 1NQP; X-ray; 1.73 A; A/C=2-142. 8469DR PDB; 1O1I; X-ray; 2.30 A; A=2-142. 8470DR PDB; 1O1J; X-ray; 1.90 A; A=2-142. 8471DR PDB; 1O1K; X-ray; 2.00 A; A/C=3-142. 8472DR PDB; 1O1L; X-ray; 1.80 A; A=2-142. 8473DR PDB; 1O1M; X-ray; 1.85 A; A=2-142. 8474DR PDB; 1O1N; X-ray; 1.80 A; A=2-142. 8475DR PDB; 1O1O; X-ray; 1.80 A; A/C=2-142. 8476DR PDB; 1O1P; X-ray; 1.80 A; A=2-142. 8477DR PDB; 1QI8; X-ray; 1.80 A; A/C=3-142. 8478DR PDB; 1QSH; X-ray; 1.70 A; A/C=2-142. 8479DR PDB; 1QSI; X-ray; 1.70 A; A/C=2-142. 8480DR PDB; 1QXD; X-ray; 2.25 A; A/C=2-142. 8481DR PDB; 1QXE; X-ray; 1.85 A; A/C=2-142. 8482DR PDB; 1R1X; X-ray; 2.15 A; A=2-142. 8483DR PDB; 1R1Y; X-ray; 1.80 A; A/C=2-142. 8484DR PDB; 1RPS; X-ray; 2.11 A; A/C=2-142. 8485DR PDB; 1RQ3; X-ray; 1.91 A; A/C=2-142. 8486DR PDB; 1RQ4; X-ray; 2.11 A; A/C=2-142. 8487DR PDB; 1RQA; X-ray; 2.11 A; A/C=2-141. 8488DR PDB; 1RVW; X-ray; 2.50 A; A=2-142. 8489DR PDB; 1SDK; X-ray; 1.80 A; A/C=2-142. 8490DR PDB; 1SDL; X-ray; 1.80 A; A/C=2-142. 8491DR PDB; 1SHR; X-ray; 1.88 A; A/C=2-142. 8492DR PDB; 1SI4; X-ray; 2.20 A; A/C=2-142. 8493DR PDB; 1THB; X-ray; 1.50 A; A/C=2-142. 8494DR PDB; 1UIW; X-ray; 1.50 A; A/C/E/G=2-142. 8495DR PDB; 1VWT; X-ray; 1.90 A; A/C=2-141. 8496DR PDB; 1XXT; X-ray; 1.91 A; A/C=2-142. 8497DR PDB; 1XY0; X-ray; 1.99 A; A/C=3-142. 8498DR PDB; 1XYE; X-ray; 2.13 A; A/C=3-142. 8499DR PDB; 1XZ2; X-ray; 1.90 A; A/C=1-142. 8500DR PDB; 1XZ4; X-ray; 2.00 A; A/C=3-142. 8501DR PDB; 1XZ5; X-ray; 2.11 A; A/C=3-142. 8502DR PDB; 1XZ7; X-ray; 1.90 A; A/C=3-142. 8503DR PDB; 1XZU; X-ray; 2.16 A; A/C=3-142. 8504DR PDB; 1XZV; X-ray; 2.11 A; A/C=3-142. 8505DR PDB; 1Y01; X-ray; 2.80 A; B=2-141. 8506DR PDB; 1Y09; X-ray; 2.25 A; A/C=3-142. 8507DR PDB; 1Y0A; X-ray; 2.22 A; A/C=3-142. 8508DR PDB; 1Y0C; X-ray; 2.30 A; A/C=3-142. 8509DR PDB; 1Y0D; X-ray; 2.10 A; A/C=2-140. 8510DR PDB; 1Y0T; X-ray; 2.14 A; A/C=1-142. 8511DR PDB; 1Y0W; X-ray; 2.14 A; A/C=1-142. 8512DR PDB; 1Y22; X-ray; 2.16 A; A/C=1-142. 8513DR PDB; 1Y2Z; X-ray; 2.07 A; A/C=1-142. 8514DR PDB; 1Y31; X-ray; 2.13 A; A/C=2-141. 8515DR PDB; 1Y35; X-ray; 2.12 A; A/C=1-142. 8516DR PDB; 1Y45; X-ray; 2.00 A; A/C=1-142. 8517DR PDB; 1Y46; X-ray; 2.22 A; A/C=2-141. 8518DR PDB; 1Y4B; X-ray; 2.10 A; A/C=1-142. 8519DR PDB; 1Y4F; X-ray; 2.00 A; A/C=2-141. 8520DR PDB; 1Y4G; X-ray; 1.91 A; A/C=2-141. 8521DR PDB; 1Y4P; X-ray; 1.98 A; A/C=2-141. 8522DR PDB; 1Y4Q; X-ray; 2.11 A; A/C=1-142. 8523DR PDB; 1Y4R; X-ray; 2.22 A; A/C=1-142. 8524DR PDB; 1Y4V; X-ray; 1.84 A; A/C=1-142. 8525DR PDB; 1Y5F; X-ray; 2.14 A; A/C=1-142. 8526DR PDB; 1Y5J; X-ray; 2.03 A; A/C=1-142. 8527DR PDB; 1Y5K; X-ray; 2.20 A; A/C=1-142. 8528DR PDB; 1Y7C; X-ray; 2.10 A; A/C=1-142. 8529DR PDB; 1Y7D; X-ray; 1.90 A; A/C=1-142. 8530DR PDB; 1Y7G; X-ray; 2.10 A; A/C=1-142. 8531DR PDB; 1Y7Z; X-ray; 1.98 A; A/C=1-142. 8532DR PDB; 1Y83; X-ray; 1.90 A; A/C=1-142. 8533DR PDB; 1Y85; X-ray; 2.13 A; A/C=2-141. 8534DR PDB; 1Y8W; X-ray; 2.90 A; A/C=3-142. 8535DR PDB; 1YDZ; X-ray; 3.30 A; A/C=3-142. 8536DR PDB; 1YE0; X-ray; 2.50 A; A/C=1-142. 8537DR PDB; 1YE1; X-ray; 4.50 A; A/C=1-142. 8538DR PDB; 1YE2; X-ray; 1.80 A; A/C=1-142. 8539DR PDB; 1YEN; X-ray; 2.80 A; A/C=1-142. 8540DR PDB; 1YEO; X-ray; 2.22 A; A/C=1-142. 8541DR PDB; 1YEQ; X-ray; 2.75 A; A/C=1-142. 8542DR PDB; 1YEU; X-ray; 2.12 A; A/C=1-142. 8543DR PDB; 1YEV; X-ray; 2.11 A; A/C=1-142. 8544DR PDB; 1YFF; X-ray; 2.40 A; A/C/E/G=2-142. 8545DR PDB; 1YG5; X-ray; 2.70 A; A/C=1-142. 8546DR PDB; 1YGD; X-ray; 2.73 A; A/C=1-142. 8547DR PDB; 1YGF; X-ray; 2.70 A; A/C=1-142. 8548DR PDB; 1YH9; X-ray; 2.20 A; A/C=1-142. 8549DR PDB; 1YHE; X-ray; 2.10 A; A/C=1-142. 8550DR PDB; 1YHR; X-ray; 2.60 A; A/C=1-142. 8551DR PDB; 1YIE; X-ray; 2.40 A; A/C=1-142. 8552DR PDB; 1YIH; X-ray; 2.00 A; A/C=1-142. 8553DR PDB; 1YVQ; X-ray; 1.80 A; A/C=2-142. 8554DR PDB; 1YVT; X-ray; 1.80 A; A=1-142. 8555DR PDB; 1YZI; X-ray; 2.07 A; A=1-142. 8556DR PDB; 1Z8U; X-ray; 2.40 A; B/D=1-142. 8557DR PDB; 2D5Z; X-ray; 1.45 A; A/C=1-142. 8558DR PDB; 2D60; X-ray; 1.70 A; A/C=1-142. 8559DR PDB; 2DN1; X-ray; 1.25 A; A=2-141. 8560DR PDB; 2DN2; X-ray; 1.25 A; A/C=2-141. 8561DR PDB; 2DN3; X-ray; 1.25 A; A=1-142. 8562DR PDB; 2DXM; Neutron; 2.10 A; A/C=2-142. 8563DR PDB; 2H35; NMR; -; A=1-142, C=2-142. 8564DR PDB; 2HBC; X-ray; 2.10 A; A=1-142. 8565DR PDB; 2HBD; X-ray; 2.20 A; A=2-142. 8566DR PDB; 2HBE; X-ray; 2.00 A; A=1-142. 8567DR PDB; 2HBF; X-ray; 2.20 A; A=1-142. 8568DR PDB; 2HBS; X-ray; 2.05 A; A/C/E/G=1-142. 8569DR PDB; 2HCO; X-ray; 2.70 A; A=2-142. 8570DR PDB; 2HHB; X-ray; 1.74 A; A/C=2-142. 8571DR PDB; 2HHD; X-ray; 2.20 A; A/C=2-142. 8572DR PDB; 2HHE; X-ray; 2.20 A; A/C=1-142. 8573DR PDB; 2W6V; X-ray; 1.80 A; A/C=2-142. 8574DR PDB; 2W72; X-ray; 1.07 A; A=2-142, C=3-142. 8575DR PDB; 2YRS; X-ray; 2.30 A; A/C/I/M=2-142. 8576DR PDB; 3B75; X-ray; 2.30 A; A/C/E/G/S=2-142. 8577DR PDB; 3D17; X-ray; 2.80 A; A/C=2-142. 8578DR PDB; 3D7O; X-ray; 1.80 A; A=2-142. 8579DR PDB; 3DUT; X-ray; 1.55 A; A/C=2-142. 8580DR PDB; 3HHB; X-ray; 1.74 A; A/C=2-142. 8581DR PDB; 3HXN; X-ray; 2.00 A; A/C=2-142. 8582DR PDB; 3IA3; X-ray; 3.20 A; B/D=2-142. 8583DR PDB; 3IC0; X-ray; 1.80 A; A/C=2-141. 8584DR PDB; 3IC2; X-ray; 2.40 A; A/C=2-142. 8585DR PDB; 3KMF; Neutron; 2.00 A; A/E=2-142. 8586DR PDB; 3NL7; X-ray; 1.80 A; A=2-142. 8587DR PDB; 3NMM; X-ray; 1.60 A; A/C=2-142. 8588DR PDB; 3ODQ; X-ray; 3.10 A; A/C=2-142. 8589DR PDB; 3ONZ; X-ray; 2.09 A; A=2-142. 8590DR PDB; 3OO4; X-ray; 1.90 A; A=2-142. 8591DR PDB; 3OO5; X-ray; 2.10 A; A=2-142. 8592DR PDB; 3OVU; X-ray; 2.83 A; C=2-142. 8593DR PDB; 3P5Q; X-ray; 2.00 A; A=2-142. 8594DR PDB; 3QJB; X-ray; 1.80 A; A=2-142. 8595DR PDB; 3QJC; X-ray; 2.00 A; A=2-142. 8596DR PDB; 3QJD; X-ray; 1.56 A; A/C=2-142. 8597DR PDB; 3QJE; X-ray; 1.80 A; A/C=2-142. 8598DR PDB; 3R5I; X-ray; 2.20 A; A/C=2-142. 8599DR PDB; 3S65; X-ray; 1.80 A; A/C=2-142. 8600DR PDB; 3S66; X-ray; 1.40 A; A=2-142. 8601DR PDB; 3SZK; X-ray; 3.01 A; A/D=2-142. 8602DR PDB; 4HHB; X-ray; 1.74 A; A/C=1-142. 8603DR PDB; 6HBW; X-ray; 2.00 A; A/C=1-142. 8604DR PDBsum; 1A00; -. 8605DR PDBsum; 1A01; -. 8606DR PDBsum; 1A0U; -. 8607DR PDBsum; 1A0Z; -. 8608DR PDBsum; 1A3N; -. 8609DR PDBsum; 1A3O; -. 8610DR PDBsum; 1A9W; -. 8611DR PDBsum; 1ABW; -. 8612DR PDBsum; 1ABY; -. 8613DR PDBsum; 1AJ9; -. 8614DR PDBsum; 1B86; -. 8615DR PDBsum; 1BAB; -. 8616DR PDBsum; 1BBB; -. 8617DR PDBsum; 1BIJ; -. 8618DR PDBsum; 1BUW; -. 8619DR PDBsum; 1BZ0; -. 8620DR PDBsum; 1BZ1; -. 8621DR PDBsum; 1BZZ; -. 8622DR PDBsum; 1C7B; -. 8623DR PDBsum; 1C7C; -. 8624DR PDBsum; 1C7D; -. 8625DR PDBsum; 1CLS; -. 8626DR PDBsum; 1CMY; -. 8627DR PDBsum; 1COH; -. 8628DR PDBsum; 1DKE; -. 8629DR PDBsum; 1DXT; -. 8630DR PDBsum; 1DXU; -. 8631DR PDBsum; 1DXV; -. 8632DR PDBsum; 1FDH; -. 8633DR PDBsum; 1FN3; -. 8634DR PDBsum; 1G9V; -. 8635DR PDBsum; 1GBU; -. 8636DR PDBsum; 1GBV; -. 8637DR PDBsum; 1GLI; -. 8638DR PDBsum; 1GZX; -. 8639DR PDBsum; 1HAB; -. 8640DR PDBsum; 1HAC; -. 8641DR PDBsum; 1HBA; -. 8642DR PDBsum; 1HBB; -. 8643DR PDBsum; 1HBS; -. 8644DR PDBsum; 1HCO; -. 8645DR PDBsum; 1HDB; -. 8646DR PDBsum; 1HGA; -. 8647DR PDBsum; 1HGB; -. 8648DR PDBsum; 1HGC; -. 8649DR PDBsum; 1HHO; -. 8650DR PDBsum; 1IRD; -. 8651DR PDBsum; 1J3Y; -. 8652DR PDBsum; 1J3Z; -. 8653DR PDBsum; 1J40; -. 8654DR PDBsum; 1J41; -. 8655DR PDBsum; 1J7S; -. 8656DR PDBsum; 1J7W; -. 8657DR PDBsum; 1J7Y; -. 8658DR PDBsum; 1JY7; -. 8659DR PDBsum; 1K0Y; -. 8660DR PDBsum; 1K1K; -. 8661DR PDBsum; 1KD2; -. 8662DR PDBsum; 1LFL; -. 8663DR PDBsum; 1LFQ; -. 8664DR PDBsum; 1LFT; -. 8665DR PDBsum; 1LFV; -. 8666DR PDBsum; 1LFY; -. 8667DR PDBsum; 1LFZ; -. 8668DR PDBsum; 1LJW; -. 8669DR PDBsum; 1M9P; -. 8670DR PDBsum; 1MKO; -. 8671DR PDBsum; 1NEJ; -. 8672DR PDBsum; 1NIH; -. 8673DR PDBsum; 1NQP; -. 8674DR PDBsum; 1O1I; -. 8675DR PDBsum; 1O1J; -. 8676DR PDBsum; 1O1K; -. 8677DR PDBsum; 1O1L; -. 8678DR PDBsum; 1O1M; -. 8679DR PDBsum; 1O1N; -. 8680DR PDBsum; 1O1O; -. 8681DR PDBsum; 1O1P; -. 8682DR PDBsum; 1QI8; -. 8683DR PDBsum; 1QSH; -. 8684DR PDBsum; 1QSI; -. 8685DR PDBsum; 1QXD; -. 8686DR PDBsum; 1QXE; -. 8687DR PDBsum; 1R1X; -. 8688DR PDBsum; 1R1Y; -. 8689DR PDBsum; 1RPS; -. 8690DR PDBsum; 1RQ3; -. 8691DR PDBsum; 1RQ4; -. 8692DR PDBsum; 1RQA; -. 8693DR PDBsum; 1RVW; -. 8694DR PDBsum; 1SDK; -. 8695DR PDBsum; 1SDL; -. 8696DR PDBsum; 1SHR; -. 8697DR PDBsum; 1SI4; -. 8698DR PDBsum; 1THB; -. 8699DR PDBsum; 1UIW; -. 8700DR PDBsum; 1VWT; -. 8701DR PDBsum; 1XXT; -. 8702DR PDBsum; 1XY0; -. 8703DR PDBsum; 1XYE; -. 8704DR PDBsum; 1XZ2; -. 8705DR PDBsum; 1XZ4; -. 8706DR PDBsum; 1XZ5; -. 8707DR PDBsum; 1XZ7; -. 8708DR PDBsum; 1XZU; -. 8709DR PDBsum; 1XZV; -. 8710DR PDBsum; 1Y01; -. 8711DR PDBsum; 1Y09; -. 8712DR PDBsum; 1Y0A; -. 8713DR PDBsum; 1Y0C; -. 8714DR PDBsum; 1Y0D; -. 8715DR PDBsum; 1Y0T; -. 8716DR PDBsum; 1Y0W; -. 8717DR PDBsum; 1Y22; -. 8718DR PDBsum; 1Y2Z; -. 8719DR PDBsum; 1Y31; -. 8720DR PDBsum; 1Y35; -. 8721DR PDBsum; 1Y45; -. 8722DR PDBsum; 1Y46; -. 8723DR PDBsum; 1Y4B; -. 8724DR PDBsum; 1Y4F; -. 8725DR PDBsum; 1Y4G; -. 8726DR PDBsum; 1Y4P; -. 8727DR PDBsum; 1Y4Q; -. 8728DR PDBsum; 1Y4R; -. 8729DR PDBsum; 1Y4V; -. 8730DR PDBsum; 1Y5F; -. 8731DR PDBsum; 1Y5J; -. 8732DR PDBsum; 1Y5K; -. 8733DR PDBsum; 1Y7C; -. 8734DR PDBsum; 1Y7D; -. 8735DR PDBsum; 1Y7G; -. 8736DR PDBsum; 1Y7Z; -. 8737DR PDBsum; 1Y83; -. 8738DR PDBsum; 1Y85; -. 8739DR PDBsum; 1Y8W; -. 8740DR PDBsum; 1YDZ; -. 8741DR PDBsum; 1YE0; -. 8742DR PDBsum; 1YE1; -. 8743DR PDBsum; 1YE2; -. 8744DR PDBsum; 1YEN; -. 8745DR PDBsum; 1YEO; -. 8746DR PDBsum; 1YEQ; -. 8747DR PDBsum; 1YEU; -. 8748DR PDBsum; 1YEV; -. 8749DR PDBsum; 1YFF; -. 8750DR PDBsum; 1YG5; -. 8751DR PDBsum; 1YGD; -. 8752DR PDBsum; 1YGF; -. 8753DR PDBsum; 1YH9; -. 8754DR PDBsum; 1YHE; -. 8755DR PDBsum; 1YHR; -. 8756DR PDBsum; 1YIE; -. 8757DR PDBsum; 1YIH; -. 8758DR PDBsum; 1YVQ; -. 8759DR PDBsum; 1YVT; -. 8760DR PDBsum; 1YZI; -. 8761DR PDBsum; 1Z8U; -. 8762DR PDBsum; 2D5Z; -. 8763DR PDBsum; 2D60; -. 8764DR PDBsum; 2DN1; -. 8765DR PDBsum; 2DN2; -. 8766DR PDBsum; 2DN3; -. 8767DR PDBsum; 2DXM; -. 8768DR PDBsum; 2H35; -. 8769DR PDBsum; 2HBC; -. 8770DR PDBsum; 2HBD; -. 8771DR PDBsum; 2HBE; -. 8772DR PDBsum; 2HBF; -. 8773DR PDBsum; 2HBS; -. 8774DR PDBsum; 2HCO; -. 8775DR PDBsum; 2HHB; -. 8776DR PDBsum; 2HHD; -. 8777DR PDBsum; 2HHE; -. 8778DR PDBsum; 2W6V; -. 8779DR PDBsum; 2W72; -. 8780DR PDBsum; 2YRS; -. 8781DR PDBsum; 3B75; -. 8782DR PDBsum; 3D17; -. 8783DR PDBsum; 3D7O; -. 8784DR PDBsum; 3DUT; -. 8785DR PDBsum; 3HHB; -. 8786DR PDBsum; 3HXN; -. 8787DR PDBsum; 3IA3; -. 8788DR PDBsum; 3IC0; -. 8789DR PDBsum; 3IC2; -. 8790DR PDBsum; 3KMF; -. 8791DR PDBsum; 3NL7; -. 8792DR PDBsum; 3NMM; -. 8793DR PDBsum; 3ODQ; -. 8794DR PDBsum; 3ONZ; -. 8795DR PDBsum; 3OO4; -. 8796DR PDBsum; 3OO5; -. 8797DR PDBsum; 3OVU; -. 8798DR PDBsum; 3P5Q; -. 8799DR PDBsum; 3QJB; -. 8800DR PDBsum; 3QJC; -. 8801DR PDBsum; 3QJD; -. 8802DR PDBsum; 3QJE; -. 8803DR PDBsum; 3R5I; -. 8804DR PDBsum; 3S65; -. 8805DR PDBsum; 3S66; -. 8806DR PDBsum; 3SZK; -. 8807DR PDBsum; 4HHB; -. 8808DR PDBsum; 6HBW; -. 8809DR ProteinModelPortal; P69905; -. 8810DR SMR; P69905; 2-142. 8811DR IntAct; P69905; 15. 8812DR MINT; MINT-1519936; -. 8813DR STRING; P69905; -. 8814DR PhosphoSite; P69905; -. 8815DR DOSAC-COBS-2DPAGE; P69905; -. 8816DR REPRODUCTION-2DPAGE; IPI00410714; -. 8817DR Siena-2DPAGE; P69905; -. 8818DR SWISS-2DPAGE; P69905; -. 8819DR UCD-2DPAGE; P01922; -. 8820DR UCD-2DPAGE; P69905; -. 8821DR PeptideAtlas; P69905; -. 8822DR PRIDE; P69905; -. 8823DR DNASU; 3039; -. 8824DR Ensembl; ENST00000251595; ENSP00000251595; ENSG00000188536. 8825DR Ensembl; ENST00000320868; ENSP00000322421; ENSG00000206172. 8826DR GeneID; 3039; -. 8827DR GeneID; 3040; -. 8828DR KEGG; hsa:3039; -. 8829DR KEGG; hsa:3040; -. 8830DR UCSC; uc002cfv.4; human. 8831DR CTD; 3039; -. 8832DR CTD; 3040; -. 8833DR GeneCards; GC16P000257; -. 8834DR GeneCards; GC16P000258; -. 8835DR HGNC; HGNC:4823; HBA1. 8836DR HGNC; HGNC:4824; HBA2. 8837DR HPA; CAB032534; -. 8838DR HPA; CAB038417; -. 8839DR HPA; HPA043780; -. 8840DR MIM; 140700; phenotype. 8841DR MIM; 141800; gene+phenotype. 8842DR MIM; 141850; gene. 8843DR MIM; 141860; gene. 8844DR MIM; 604131; phenotype. 8845DR MIM; 613978; phenotype. 8846DR neXtProt; NX_P69905; -. 8847DR Orphanet; 98791; Alpha thalassemia - intellectual deficit syndrome. 8848DR Orphanet; 93616; Hemoglobin H disease. 8849DR Orphanet; 163596; Hydrops fetalis of Bart. 8850DR PharmGKB; PA29199; -. 8851DR eggNOG; NOG283543; -. 8852DR GeneTree; ENSGT00650000093280; -. 8853DR HOVERGEN; HBG009709; -. 8854DR InParanoid; P69905; -. 8855DR KO; K13822; -. 8856DR OMA; TPEVHAS; -. 8857DR OrthoDB; EOG47M209; -. 8858DR DrugBank; DB00613; Amodiaquine. 8859DR DrugBank; DB00608; Chloroquine. 8860DR DrugBank; DB00893; Iron Dextran. 8861DR DrugBank; DB00358; Mefloquine. 8862DR DrugBank; DB01087; Primaquine. 8863DR DrugBank; DB00468; Quinine. 8864DR EvolutionaryTrace; P69905; -. 8865DR NextBio; 12034; -. 8866DR PMAP-CutDB; P69905; -. 8867DR ArrayExpress; P69905; -. 8868DR Bgee; P69905; -. 8869DR CleanEx; HS_HBA1; -. 8870DR CleanEx; HS_HBA2; -. 8871DR Genevestigator; P69905; -. 8872DR GermOnline; ENSG00000188536; Homo sapiens. 8873DR GermOnline; ENSG00000206172; Homo sapiens. 8874DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB. 8875DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL. 8876DR GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB. 8877DR GO; GO:0020037; F:heme binding; IEA:InterPro. 8878DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. 8879DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. 8880DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. 8881DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL. 8882DR GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL. 8883DR GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL. 8884DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 8885DR InterPro; IPR000971; Globin. 8886DR InterPro; IPR009050; Globin-like. 8887DR InterPro; IPR012292; Globin_dom. 8888DR InterPro; IPR002338; Haemoglobin_a. 8889DR InterPro; IPR018331; Haemoglobin_alpha_chain. 8890DR InterPro; IPR002339; Haemoglobin_pi. 8891DR PANTHER; PTHR11442:SF14; Pi_haem; 1. 8892DR Pfam; PF00042; Globin; 1. 8893DR PRINTS; PR00612; ALPHAHAEM. 8894DR PRINTS; PR00815; PIHAEM. 8895DR SUPFAM; SSF46458; Globin_like; 1. 8896DR PROSITE; PS01033; GLOBIN; 1. 8897PE 1: Evidence at protein level; 8898KW 3D-structure; Complete proteome; Direct protein sequencing; 8899KW Disease mutation; Glycation; Glycoprotein; Heme; 8900KW Hereditary hemolytic anemia; Iron; Metal-binding; Oxygen transport; 8901KW Phosphoprotein; Polymorphism; Reference proteome; Transport. 8902FT INIT_MET 1 1 Removed. 8903FT CHAIN 2 142 Hemoglobin subunit alpha. 8904FT /FTId=PRO_0000052653. 8905FT METAL 59 59 Iron (heme distal ligand). 8906FT METAL 88 88 Iron (heme proximal ligand). 8907FT SITE 12 12 Not glycated. 8908FT SITE 57 57 Not glycated. 8909FT SITE 61 61 Not glycated. 8910FT SITE 91 91 Not glycated. 8911FT SITE 100 100 Not glycated. 8912FT MOD_RES 25 25 Phosphotyrosine. 8913FT MOD_RES 43 43 Phosphotyrosine. 8914FT CARBOHYD 8 8 N-linked (Glc) (glycation). 8915FT CARBOHYD 17 17 N-linked (Glc) (glycation). 8916FT CARBOHYD 41 41 N-linked (Glc) (glycation). 8917FT CARBOHYD 62 62 N-linked (Glc) (glycation). 8918FT VARIANT 2 2 V -> E (in Thionville; O(2) affinity 8919FT down). 8920FT /FTId=VAR_002719. 8921FT VARIANT 3 3 L -> R (in ChongQing; O(2) affinity up; 8922FT dbSNP:rs36030576). 8923FT /FTId=VAR_002720. 8924FT VARIANT 6 6 A -> D (in J-Toronto; dbSNP:rs34090856). 8925FT /FTId=VAR_002721. 8926FT VARIANT 6 6 A -> P (in Karachi; dbSNP:rs34751764). 8927FT /FTId=VAR_002722. 8928FT VARIANT 7 7 D -> A (in Sawara; O(2) affinity up; 8929FT dbSNP:rs33986902). 8930FT /FTId=VAR_002723. 8931FT VARIANT 7 7 D -> G (in Swan River). 8932FT /FTId=VAR_002724. 8933FT VARIANT 7 7 D -> N (in Dunn; O(2) affinity up; 8934FT dbSNP:rs33961916). 8935FT /FTId=VAR_002725. 8936FT VARIANT 7 7 D -> V (in Ferndown; O(2) affinity up). 8937FT /FTId=VAR_002726. 8938FT VARIANT 7 7 D -> Y (in Woodville; O(2) affinity up). 8939FT /FTId=VAR_002727. 8940FT VARIANT 8 8 K -> E (in Kurosaki; dbSNP:rs34817956). 8941FT /FTId=VAR_002728. 8942FT VARIANT 10 10 N -> T (in Broomfield). 8943FT /FTId=VAR_038149. 8944FT VARIANT 11 11 V -> F (in dbSNP:rs1799896). 8945FT /FTId=VAR_014605. 8946FT VARIANT 12 12 K -> E (in Anantharaj). 8947FT /FTId=VAR_002729. 8948FT VARIANT 13 13 A -> D (in J-Paris 1/J-Aljezur; 8949FT dbSNP:rs35615982). 8950FT /FTId=VAR_002730. 8951FT VARIANT 14 14 A -> P (in Ravenscourt Park; causes 8952FT alpha-thalassemia; dbSNP:rs35331909). 8953FT /FTId=VAR_038150. 8954FT VARIANT 15 15 W -> R (in Evanston; O(2) affinity up; 8955FT dbSNP:rs33964317). 8956FT /FTId=VAR_002731. 8957FT VARIANT 16 16 G -> R (in Ottawa/Siam; 8958FT dbSNP:rs35816645). 8959FT /FTId=VAR_002732. 8960FT VARIANT 17 17 K -> M (in Harbin; slightly unstable; 8961FT dbSNP:rs35210126). 8962FT /FTId=VAR_002733. 8963FT VARIANT 17 17 K -> N (in Beijing; dbSNP:rs33923844). 8964FT /FTId=VAR_002734. 8965FT VARIANT 19 19 G -> D (in Al-Ain Abu Dhabi; 8966FT dbSNP:rs35993097). 8967FT /FTId=VAR_002735. 8968FT VARIANT 19 19 G -> R (in Handsworth; dbSNP:rs34504387). 8969FT /FTId=VAR_002736. 8970FT VARIANT 20 20 A -> D (in J-Kurosh). 8971FT /FTId=VAR_002737. 8972FT VARIANT 20 20 A -> E (in J-Tashikuergan; 8973FT dbSNP:rs35628685). 8974FT /FTId=VAR_002738. 8975FT VARIANT 21 21 H -> Q (in Le Lamentin; 8976FT dbSNP:rs41525149). 8977FT /FTId=VAR_002739. 8978FT VARIANT 21 21 H -> R (in Hobart; dbSNP:rs33943087). 8979FT /FTId=VAR_002740. 8980FT VARIANT 22 22 A -> D (in J-Nyanza; dbSNP:rs11548605). 8981FT /FTId=VAR_002741. 8982FT VARIANT 22 22 A -> P (in Fontainebleau; 8983FT dbSNP:rs34324664). 8984FT /FTId=VAR_002742. 8985FT VARIANT 23 23 G -> D (in J-Medellin; dbSNP:rs34608326). 8986FT /FTId=VAR_002743. 8987FT VARIANT 24 24 E -> G (in Reims; slightly unstable; 8988FT dbSNP:rs33939421). 8989FT /FTId=VAR_002744. 8990FT VARIANT 24 24 E -> K (in Chad). 8991FT /FTId=VAR_002745. 8992FT VARIANT 25 25 Y -> H (in Luxembourg; unstable). 8993FT /FTId=VAR_002746. 8994FT VARIANT 27 27 A -> E (in Shenyang; unstable). 8995FT /FTId=VAR_002747. 8996FT VARIANT 27 27 A -> V (in Campinas). 8997FT /FTId=VAR_025387. 8998FT VARIANT 28 28 E -> D (in Hekinan). 8999FT /FTId=VAR_002748. 9000FT VARIANT 28 28 E -> G (in Fort Worth). 9001FT /FTId=VAR_002749. 9002FT VARIANT 28 28 E -> V (in Spanish town). 9003FT /FTId=VAR_002750. 9004FT VARIANT 31 31 E -> K (in O-Padova). 9005FT /FTId=VAR_002751. 9006FT VARIANT 32 32 R -> K (causes alpha-thalassemia). 9007FT /FTId=VAR_025002. 9008FT VARIANT 32 32 R -> S (in Prato; unstable). 9009FT /FTId=VAR_002752. 9010FT VARIANT 35 35 L -> R (in Queens/Ogi). 9011FT /FTId=VAR_002753. 9012FT VARIANT 38 38 P -> PE (in Catonsville). 9013FT /FTId=VAR_002755. 9014FT VARIANT 38 38 P -> R (in Bourmedes). 9015FT /FTId=VAR_002754. 9016FT VARIANT 41 41 K -> M (in Kanagawa; O(2) affinity up). 9017FT /FTId=VAR_002756. 9018FT VARIANT 42 42 T -> S (in Miyano; O(2) affinity up). 9019FT /FTId=VAR_002757. 9020FT VARIANT 44 44 F -> L (in Hirosaki; unstable). 9021FT /FTId=VAR_002758. 9022FT VARIANT 45 45 P -> L (in Milledgeville; O(2) affinity 9023FT up; dbSNP:rs41514946). 9024FT /FTId=VAR_002759. 9025FT VARIANT 45 45 P -> R (in Kawachi; O(2) affinity up). 9026FT /FTId=VAR_002760. 9027FT VARIANT 46 46 H -> Q (in Bari). 9028FT /FTId=VAR_002761. 9029FT VARIANT 46 46 H -> R (in Fort de France; O(2) affinity 9030FT up). 9031FT /FTId=VAR_002762. 9032FT VARIANT 48 48 D -> A (in Cordele; unstable). 9033FT /FTId=VAR_002763. 9034FT VARIANT 48 48 D -> G (in Umi/Michigan; unstable). 9035FT /FTId=VAR_002764. 9036FT VARIANT 48 48 D -> H (in Hasharon/Sinai; unstable). 9037FT /FTId=VAR_002765. 9038FT VARIANT 48 48 D -> Y (in Kurdistan). 9039FT /FTId=VAR_002766. 9040FT VARIANT 49 49 L -> R (in Montgomery). 9041FT /FTId=VAR_002767. 9042FT VARIANT 50 50 S -> R (in Savaria). 9043FT /FTId=VAR_002768. 9044FT VARIANT 51 51 H -> R (in Aichi; slightly unstable). 9045FT /FTId=VAR_002769. 9046FT VARIANT 52 52 G -> D (in J-Abidjan). 9047FT /FTId=VAR_002770. 9048FT VARIANT 52 52 G -> R (in Russ). 9049FT /FTId=VAR_002771. 9050FT VARIANT 54 54 A -> D (in J-Rovigo; unstable). 9051FT /FTId=VAR_002772. 9052FT VARIANT 55 55 Q -> R (in Hikoshima/Shimonoseki). 9053FT /FTId=VAR_002773. 9054FT VARIANT 57 57 K -> R (in Port Huron). 9055FT /FTId=VAR_002774. 9056FT VARIANT 57 57 K -> T (in Thailand). 9057FT /FTId=VAR_002775. 9058FT VARIANT 58 58 G -> R (in L-Persian Gulf). 9059FT /FTId=VAR_002776. 9060FT VARIANT 59 59 H -> Q (in Boghe). 9061FT /FTId=VAR_025388. 9062FT VARIANT 59 59 H -> Y (in M-Boston/M-Osaka; O(2) 9063FT affinity down). 9064FT /FTId=VAR_002777. 9065FT VARIANT 60 60 G -> D (in Adana; unstable; causes alpha- 9066FT thalassemia; dbSNP:rs28928878). 9067FT /FTId=VAR_002778. 9068FT VARIANT 60 60 G -> V (in Tottori; unstable). 9069FT /FTId=VAR_002779. 9070FT VARIANT 61 61 K -> N (in Zambia; dbSNP:rs28928887). 9071FT /FTId=VAR_002780. 9072FT VARIANT 61 61 Missing (in Clinic; unstable; causes 9073FT alpha-thalassemia). 9074FT /FTId=VAR_002781. 9075FT VARIANT 62 62 K -> N (in J-Buda). 9076FT /FTId=VAR_002782. 9077FT VARIANT 62 62 K -> T (in J-Anatolia). 9078FT /FTId=VAR_002783. 9079FT VARIANT 63 63 V -> M (in Evans; unstable). 9080FT /FTId=VAR_002784. 9081FT VARIANT 63 63 Missing (in HBH; hemoglobin Aghia 9082FT Sophia). 9083FT /FTId=VAR_066401. 9084FT VARIANT 64 64 A -> D (in Pontoise; unstable). 9085FT /FTId=VAR_002785. 9086FT VARIANT 65 65 D -> Y (in Persepolis). 9087FT /FTId=VAR_002786. 9088FT VARIANT 69 69 N -> K (in G-Philadelphia; 9089FT dbSNP:rs1060339). 9090FT /FTId=VAR_002787. 9091FT VARIANT 72 72 A -> E (in J-Habana). 9092FT /FTId=VAR_002788. 9093FT VARIANT 72 72 A -> V (in Ozieri). 9094FT /FTId=VAR_002789. 9095FT VARIANT 73 73 H -> R (in Daneskgah-Teheran). 9096FT /FTId=VAR_002790. 9097FT VARIANT 75 75 D -> A (in Lille). 9098FT /FTId=VAR_002791. 9099FT VARIANT 75 75 D -> G (in Chapel Hill). 9100FT /FTId=VAR_002792. 9101FT VARIANT 75 75 D -> N (in G-Pest). 9102FT /FTId=VAR_002793. 9103FT VARIANT 76 76 D -> A (in Duan). 9104FT /FTId=VAR_002794. 9105FT VARIANT 76 76 D -> H (in Q-Iran). 9106FT /FTId=VAR_002795. 9107FT VARIANT 77 77 M -> K (in Noko). 9108FT /FTId=VAR_002796. 9109FT VARIANT 77 77 M -> T (in Aztec). 9110FT /FTId=VAR_002797. 9111FT VARIANT 78 78 P -> R (in Guizhou). 9112FT /FTId=VAR_002798. 9113FT VARIANT 79 79 N -> H (in Davenport). 9114FT /FTId=VAR_002799. 9115FT VARIANT 79 79 N -> K (in Stanleyville-2). 9116FT /FTId=VAR_002800. 9117FT VARIANT 80 80 A -> G (in Singapore). 9118FT /FTId=VAR_012662. 9119FT VARIANT 81 81 L -> R (in Ann Arbor; unstable). 9120FT /FTId=VAR_002801. 9121FT VARIANT 82 82 S -> C (in Nigeria). 9122FT /FTId=VAR_002802. 9123FT VARIANT 83 83 A -> D (in Garden State). 9124FT /FTId=VAR_002803. 9125FT VARIANT 85 85 S -> R (in Etobicoke; O(2) affinity up). 9126FT /FTId=VAR_002804. 9127FT VARIANT 86 86 D -> V (in Inkster; O(2) affinity up). 9128FT /FTId=VAR_002805. 9129FT VARIANT 86 86 D -> Y (in Atago; O(2) affinity up). 9130FT /FTId=VAR_002806. 9131FT VARIANT 87 87 L -> R (in Moabit; unstable). 9132FT /FTId=VAR_002807. 9133FT VARIANT 88 88 H -> N (in Auckland; unstable). 9134FT /FTId=VAR_002808. 9135FT VARIANT 88 88 H -> R (in Iwata; unstable). 9136FT /FTId=VAR_002809. 9137FT VARIANT 89 89 A -> S (in Loire; O(2) affinity up). 9138FT /FTId=VAR_002810. 9139FT VARIANT 91 91 K -> M (in Handa; O(2) affinity up). 9140FT /FTId=VAR_002811. 9141FT VARIANT 92 92 L -> F (in dbSNP:rs17407508). 9142FT /FTId=VAR_049272. 9143FT VARIANT 92 92 L -> P (in Port Phillip; unstable; 9144FT dbSNP:rs17407508). 9145FT /FTId=VAR_002812. 9146FT VARIANT 93 93 R -> Q (in J-Cape Town; O(2) affinity 9147FT up). 9148FT /FTId=VAR_002813. 9149FT VARIANT 93 93 R -> W (in Cemenelum; O(2) affinity up). 9150FT /FTId=VAR_020775. 9151FT VARIANT 95 95 D -> A (in Bassett; markedly reduced 9152FT oxygen affinity). 9153FT /FTId=VAR_025389. 9154FT VARIANT 95 95 D -> Y (in Setif; unstable). 9155FT /FTId=VAR_002814. 9156FT VARIANT 96 96 P -> A (in Denmark Hill; O(2) affinity 9157FT up). 9158FT /FTId=VAR_002815. 9159FT VARIANT 96 96 P -> T (in Godavari; O(2) affinity up). 9160FT /FTId=VAR_002816. 9161FT VARIANT 98 98 N -> K (in Dallas; O(2) affinity up). 9162FT /FTId=VAR_002817. 9163FT VARIANT 100 100 K -> E (in Turriff). 9164FT /FTId=VAR_002818. 9165FT VARIANT 103 103 S -> R (in Manitoba; slightly unstable; 9166FT dbSNP:rs41344646). 9167FT /FTId=VAR_002819. 9168FT VARIANT 104 104 H -> R (in Contaldo; unstable). 9169FT /FTId=VAR_002820. 9170FT VARIANT 104 104 H -> Y (in Charolles). 9171FT /FTId=VAR_025390. 9172FT VARIANT 110 110 L -> R (in Suan-Dok; unstable; causes 9173FT alpha-thalassemia). 9174FT /FTId=VAR_002821. 9175FT VARIANT 111 111 A -> D (in Petah Tikva; unstable; causes 9176FT alpha-thalassemia). 9177FT /FTId=VAR_002822. 9178FT VARIANT 113 113 H -> D (in Hopkins-II; unstable). 9179FT /FTId=VAR_002823. 9180FT VARIANT 114 114 L -> H (in Twin Peaks). 9181FT /FTId=VAR_002824. 9182FT VARIANT 115 115 P -> L (in Nouakchott). 9183FT /FTId=VAR_002825. 9184FT VARIANT 115 115 P -> R (in Chiapas). 9185FT /FTId=VAR_002826. 9186FT VARIANT 115 115 P -> S (in Melusine). 9187FT /FTId=VAR_002827. 9188FT VARIANT 116 116 A -> D (in J-Tongariki). 9189FT /FTId=VAR_002828. 9190FT VARIANT 117 117 E -> A (in Ube-4). 9191FT /FTId=VAR_002829. 9192FT VARIANT 117 117 E -> EHLPAE (in Zaire). 9193FT /FTId=VAR_002830. 9194FT VARIANT 118 118 F -> FI (in Phnom Penh). 9195FT /FTId=VAR_002831. 9196FT VARIANT 119 119 T -> TEFT (in Grady). 9197FT /FTId=VAR_002832. 9198FT VARIANT 121 121 A -> E (in J-Meerut/J-Birmingham). 9199FT /FTId=VAR_002833. 9200FT VARIANT 122 122 V -> M (in Owari). 9201FT /FTId=VAR_002834. 9202FT VARIANT 123 123 H -> Q (in Westmead). 9203FT /FTId=VAR_002835. 9204FT VARIANT 126 126 L -> P (in Quong Sze; causes alpha- 9205FT thalassemia). 9206FT /FTId=VAR_002836. 9207FT VARIANT 126 126 L -> R (in Plasencia; family with 9208FT moderate microcytosis and hypochromia). 9209FT /FTId=VAR_025391. 9210FT VARIANT 127 127 D -> G (in West One). 9211FT /FTId=VAR_025392. 9212FT VARIANT 127 127 D -> V (in Fukutomi; O(2) affinity up). 9213FT /FTId=VAR_002837. 9214FT VARIANT 127 127 D -> Y (in Monteriore; O(2) affinity up). 9215FT /FTId=VAR_002838. 9216FT VARIANT 128 128 K -> N (in Jackson). 9217FT /FTId=VAR_002839. 9218FT VARIANT 130 130 L -> P (in Tunis-Bizerte; unstable; 9219FT causes alpha-thalassemia). 9220FT /FTId=VAR_002840. 9221FT VARIANT 131 131 A -> D (in Yuda; O(2) affinity down). 9222FT /FTId=VAR_002842. 9223FT VARIANT 131 131 A -> P (in Sun Prairie; unstable). 9224FT /FTId=VAR_002841. 9225FT VARIANT 132 132 S -> P (in Questembert; highly unstable; 9226FT causes alpha-thalassemia). 9227FT /FTId=VAR_002843. 9228FT VARIANT 134 134 S -> R (in Val de Marne; O(2) affinity 9229FT up). 9230FT /FTId=VAR_002844. 9231FT VARIANT 136 136 V -> E (in Pavie). 9232FT /FTId=VAR_002845. 9233FT VARIANT 137 137 L -> M (in Chicago). 9234FT /FTId=VAR_002846. 9235FT VARIANT 137 137 L -> P (in Bibba; unstable; causes alpha- 9236FT thalassemia). 9237FT /FTId=VAR_002847. 9238FT VARIANT 137 137 L -> R (in Toyama). 9239FT /FTId=VAR_035242. 9240FT VARIANT 139 139 S -> P (in Attleboro; O(2) affinity up). 9241FT /FTId=VAR_002848. 9242FT VARIANT 140 140 K -> E (in Hanamaki; O(2) affinity up). 9243FT /FTId=VAR_002849. 9244FT VARIANT 140 140 K -> T (in Tokoname; O(2) affinity up). 9245FT /FTId=VAR_002850. 9246FT VARIANT 141 141 Y -> H (in Rouen/Ethiopia; O(2) affinity 9247FT up). 9248FT /FTId=VAR_002851. 9249FT VARIANT 142 142 R -> C (in Nunobiki; O(2) affinity up). 9250FT /FTId=VAR_002852. 9251FT VARIANT 142 142 R -> H (in Suresnes; O(2) affinity up). 9252FT /FTId=VAR_002854. 9253FT VARIANT 142 142 R -> L (in Legnano; O(2) affinity up). 9254FT /FTId=VAR_002853. 9255FT VARIANT 142 142 R -> P (in Singapore). 9256FT /FTId=VAR_002855. 9257FT CONFLICT 10 10 N -> H (in Ref. 13; BAD97112). 9258FT HELIX 5 16 9259FT HELIX 17 21 9260FT HELIX 22 36 9261FT HELIX 38 43 9262FT HELIX 54 72 9263FT HELIX 74 76 9264FT HELIX 77 80 9265FT HELIX 82 90 9266FT HELIX 97 113 9267FT TURN 115 117 9268FT HELIX 120 137 9269FT TURN 138 140 9270SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; 9271 MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG 9272 KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP 9273 AVHASLDKFL ASVSTVLTSK YR 9274// 9275ID HBA_PANPA Reviewed; 142 AA. 9276AC P69906; P01922; 9277DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 9278DT 23-JAN-2007, sequence version 2. 9279DT 13-JUN-2012, entry version 47. 9280DE RecName: Full=Hemoglobin subunit alpha; 9281DE AltName: Full=Alpha-globin; 9282DE AltName: Full=Hemoglobin alpha chain; 9283GN Name=HBA1; 9284GN and 9285GN Name=HBA2; 9286OS Pan paniscus (Pygmy chimpanzee) (Bonobo). 9287OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 9288OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 9289OC Catarrhini; Hominidae; Pan. 9290OX NCBI_TaxID=9597; 9291RN [1] 9292RP PROTEIN SEQUENCE OF 2-142. 9293RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; 9294RA Goodman M., Braunitzer G., Stangl A., Schrank B.; 9295RT "Evidence on human origins from haemoglobins of African apes."; 9296RL Nature 303:546-548(1983). 9297CC -!- FUNCTION: Involved in oxygen transport from the lung to the 9298CC various peripheral tissues. 9299CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 9300CC adult hemoglobin A (HbA); two alpha chains and two delta chains in 9301CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon 9302CC chains in early embryonic hemoglobin Gower-2; two alpha chains and 9303CC two gamma chains in fetal hemoglobin F (HbF). 9304CC -!- TISSUE SPECIFICITY: Red blood cells. 9305CC -!- MISCELLANEOUS: Gives blood its red color. 9306CC -!- SIMILARITY: Belongs to the globin family. 9307CC ----------------------------------------------------------------------- 9308CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 9309CC Distributed under the Creative Commons Attribution-NoDerivs License 9310CC ----------------------------------------------------------------------- 9311DR PIR; C93303; HACZP. 9312DR ProteinModelPortal; P69906; -. 9313DR SMR; P69906; 2-142. 9314DR IntAct; P69906; 2. 9315DR PRIDE; P69906; -. 9316DR HOVERGEN; HBG009709; -. 9317DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. 9318DR GO; GO:0020037; F:heme binding; IEA:InterPro. 9319DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. 9320DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. 9321DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 9322DR InterPro; IPR000971; Globin. 9323DR InterPro; IPR009050; Globin-like. 9324DR InterPro; IPR012292; Globin_dom. 9325DR InterPro; IPR002338; Haemoglobin_a. 9326DR InterPro; IPR018331; Haemoglobin_alpha_chain. 9327DR InterPro; IPR002339; Haemoglobin_pi. 9328DR PANTHER; PTHR11442:SF14; Pi_haem; 1. 9329DR Pfam; PF00042; Globin; 1. 9330DR PRINTS; PR00612; ALPHAHAEM. 9331DR PRINTS; PR00815; PIHAEM. 9332DR SUPFAM; SSF46458; Globin_like; 1. 9333DR PROSITE; PS01033; GLOBIN; 1. 9334PE 1: Evidence at protein level; 9335KW Direct protein sequencing; Heme; Iron; Metal-binding; 9336KW Oxygen transport; Transport. 9337FT INIT_MET 1 1 Removed. 9338FT CHAIN 2 142 Hemoglobin subunit alpha. 9339FT /FTId=PRO_0000052717. 9340FT METAL 59 59 Iron (heme distal ligand). 9341FT METAL 88 88 Iron (heme proximal ligand). 9342SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; 9343 MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG 9344 KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP 9345 AVHASLDKFL ASVSTVLTSK YR 9346// 9347ID HBA_PANTR Reviewed; 142 AA. 9348AC P69907; P01922; 9349DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 9350DT 23-JAN-2007, sequence version 2. 9351DT 13-JUN-2012, entry version 57. 9352DE RecName: Full=Hemoglobin subunit alpha; 9353DE AltName: Full=Alpha-globin; 9354DE AltName: Full=Hemoglobin alpha chain; 9355GN Name=HBA1; 9356GN and 9357GN Name=HBA2; 9358OS Pan troglodytes (Chimpanzee). 9359OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 9360OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 9361OC Catarrhini; Hominidae; Pan. 9362OX NCBI_TaxID=9598; 9363RN [1] 9364RP NUCLEOTIDE SEQUENCE [MRNA]. 9365RX MEDLINE=84169526; PubMed=6689503; DOI=10.1093/nar/11.24.8915; 9366RA Liebhaber S.A., Begley K.A.; 9367RT "Structural and evolutionary analysis of the two chimpanzee alpha- 9368RT globin mRNAs."; 9369RL Nucleic Acids Res. 11:8915-8929(1983). 9370RN [2] 9371RP PROTEIN SEQUENCE OF 2-142. 9372RX MEDLINE=66071496; PubMed=5855051; 9373RA Rifkin D.B., Konigsberg W.; 9374RT "The characterization of the tryptic peptides from the hemoglobin of 9375RT the chimpanzee (Pan troglodytes)."; 9376RL Biochim. Biophys. Acta 104:457-461(1965). 9377RN [3] 9378RP PROTEIN SEQUENCE OF 2-142. 9379RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; 9380RA Goodman M., Braunitzer G., Stangl A., Schrank B.; 9381RT "Evidence on human origins from haemoglobins of African apes."; 9382RL Nature 303:546-548(1983). 9383CC -!- FUNCTION: Involved in oxygen transport from the lung to the 9384CC various peripheral tissues. 9385CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 9386CC adult hemoglobin A (HbA); two alpha chains and two delta chains in 9387CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon 9388CC chains in early embryonic hemoglobin Gower-2; two alpha chains and 9389CC two gamma chains in fetal hemoglobin F (HbF). 9390CC -!- TISSUE SPECIFICITY: Red blood cells. 9391CC -!- MISCELLANEOUS: Gives blood its red color. 9392CC -!- SIMILARITY: Belongs to the globin family. 9393CC ----------------------------------------------------------------------- 9394CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 9395CC Distributed under the Creative Commons Attribution-NoDerivs License 9396CC ----------------------------------------------------------------------- 9397DR EMBL; X00226; CAA25044.1; -; mRNA. 9398DR EMBL; X00227; CAA25045.1; -; mRNA. 9399DR PIR; I58217; HACZ. 9400DR RefSeq; NP_001036091.1; NM_001042626.1. 9401DR RefSeq; NP_001036092.1; NM_001042627.1. 9402DR UniGene; Ptr.6291; -. 9403DR UniGene; Ptr.6292; -. 9404DR ProteinModelPortal; P69907; -. 9405DR SMR; P69907; 2-142. 9406DR PRIDE; P69907; -. 9407DR GeneID; 732485; -. 9408DR GeneID; 732486; -. 9409DR KEGG; ptr:732485; -. 9410DR KEGG; ptr:732486; -. 9411DR CTD; 3039; -. 9412DR CTD; 3040; -. 9413DR HOVERGEN; HBG009709; -. 9414DR KO; K13822; -. 9415DR NextBio; 20902653; -. 9416DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. 9417DR GO; GO:0020037; F:heme binding; IEA:InterPro. 9418DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. 9419DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. 9420DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 9421DR InterPro; IPR000971; Globin. 9422DR InterPro; IPR009050; Globin-like. 9423DR InterPro; IPR012292; Globin_dom. 9424DR InterPro; IPR002338; Haemoglobin_a. 9425DR InterPro; IPR018331; Haemoglobin_alpha_chain. 9426DR InterPro; IPR002339; Haemoglobin_pi. 9427DR PANTHER; PTHR11442:SF14; Pi_haem; 1. 9428DR Pfam; PF00042; Globin; 1. 9429DR PRINTS; PR00612; ALPHAHAEM. 9430DR PRINTS; PR00815; PIHAEM. 9431DR SUPFAM; SSF46458; Globin_like; 1. 9432DR PROSITE; PS01033; GLOBIN; 1. 9433PE 1: Evidence at protein level; 9434KW Complete proteome; Direct protein sequencing; Heme; Iron; 9435KW Metal-binding; Oxygen transport; Reference proteome; Transport. 9436FT INIT_MET 1 1 Removed. 9437FT CHAIN 2 142 Hemoglobin subunit alpha. 9438FT /FTId=PRO_0000052720. 9439FT METAL 59 59 Iron (heme distal ligand). 9440FT METAL 88 88 Iron (heme proximal ligand). 9441SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; 9442 MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG 9443 KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP 9444 AVHASLDKFL ASVSTVLTSK YR 9445// 9446ID HBB_HUMAN Reviewed; 147 AA. 9447AC P68871; A4GX73; B2ZUE0; P02023; Q13852; Q14481; Q14510; Q45KT0; 9448AC Q549N7; Q6FI08; Q6R7N2; Q8IZI1; Q9BX96; Q9UCD6; Q9UCP8; Q9UCP9; 9449DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 9450DT 23-JAN-2007, sequence version 2. 9451DT 13-JUN-2012, entry version 108. 9452DE RecName: Full=Hemoglobin subunit beta; 9453DE AltName: Full=Beta-globin; 9454DE AltName: Full=Hemoglobin beta chain; 9455DE Contains: 9456DE RecName: Full=LVV-hemorphin-7; 9457GN Name=HBB; 9458OS Homo sapiens (Human). 9459OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 9460OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 9461OC Catarrhini; Hominidae; Homo. 9462OX NCBI_TaxID=9606; 9463RN [1] 9464RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9465RX MEDLINE=77126403; PubMed=1019344; 9466RA Marotta C., Forget B., Cohen-Solal M., Weissman S.M.; 9467RT "Nucleotide sequence analysis of coding and noncoding regions of human 9468RT beta-globin mRNA."; 9469RL Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976). 9470RN [2] 9471RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9472RX MEDLINE=81064667; PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6; 9473RA Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.; 9474RT "The nucleotide sequence of the human beta-globin gene."; 9475RL Cell 21:647-651(1980). 9476RN [3] 9477RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7. 9478RX PubMed=16175509; DOI=10.1086/491748; 9479RA Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.; 9480RT "The beta-globin recombinational hotspot reduces the effects of strong 9481RT selection around HbC, a recently arisen mutation providing resistance 9482RT to malaria."; 9483RL Am. J. Hum. Genet. 77:637-642(2005). 9484RN [4] 9485RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9486RA Lu L., Hu Z.H., Du C.S., Fu Y.S.; 9487RT "DNA sequence of the human beta-globin gene isolated from a healthy 9488RT Chinese."; 9489RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. 9490RN [5] 9491RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-113. 9492RA Cabeda J.M., Correia C., Estevinho A., Cardoso C., Amorim M.L., 9493RA Cleto E., Vale L., Coimbra E., Pinho L., Justica B.; 9494RT "Unexpected patterns of globin mutations in thalassemia patients from 9495RT north of Portugal."; 9496RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. 9497RN [6] 9498RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LOUISVILLE LEU-43. 9499RC TISSUE=Blood; 9500RA Kutlar F., Harbin J., Brisco J., Kutlar A.; 9501RT "Rapid detection of electrophoretically silent, unstable human 9502RT hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA 9503RT sequencing of mRNA."; 9504RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. 9505RN [7] 9506RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DURHAM-N.C. PRO-115. 9507RC TISSUE=Blood; 9508RA Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.; 9509RT "Electrophoretically silent, very unstable, thalassemic mutation at 9510RT codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA 9511RT sequencing of mRNA, from a Russian women."; 9512RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. 9513RN [8] 9514RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TY GARD GLN-125. 9515RC TISSUE=Blood; 9516RA Kutlar F., Holley L., Leithner C., Kutlar A.; 9517RT "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a 9518RT Caucasian female with erythrocytosis."; 9519RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. 9520RN [9] 9521RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9522RA Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D., 9523RA Kutlar F.; 9524RT "Heterozygote C->A beta-thalassemia mutation at the intron-2/848 9525RT nucleotide of beta globin gene was detected on a Northern European 9526RT (Caucasian) individual."; 9527RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. 9528RN [10] 9529RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-7 AND SER-140. 9530RC TISSUE=Blood; 9531RA Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.; 9532RT "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on 9533RT the same chromosome with hemoglobin S mutation, detected in an 9534RT African-American family."; 9535RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. 9536RN [11] 9537RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT O-ARAB. 9538RC TISSUE=Blood; 9539RA Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.; 9540RT "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta- 9541RT thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish 9542RT patient."; 9543RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. 9544RN [12] 9545RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9546RA Li W.J.; 9547RT "Thalassaemic trait cause by C-T substitution at position -90 in 9548RT proximal CACCC box of beta-globin gene in China family."; 9549RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 9550RN [13] 9551RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-50 AND PRO-76. 9552RC TISSUE=Lymphocyte; 9553RA Fan B., Xie L., Guan X.; 9554RT "The differently expressed genes in the lymphocyte of recovered SARS 9555RT patients."; 9556RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. 9557RN [14] 9558RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 9559RC TISSUE=Blood; 9560RA Mehta S., Li T., Davis D.H., Nechtman J., Kutlar F.; 9561RT "Beta-thalassemia G->C mutation at the nucleotide 5 position of intron 9562RT 1 of beta globin gene was detected in Asian-Indian female with two 9563RT polymorphisms in cis."; 9564RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. 9565RN [15] 9566RP NUCLEOTIDE SEQUENCE [MRNA]. 9567RA Hilliard L.M., Patel N., Li T., Zhang H., Kutlar A., Kutlar F.; 9568RT "Hb Dothan: a novel beta chain variant due to (-GTG) deletion between 9569RT the codons 25/26 of beta globin gene detected in a Caucasian male 9570RT baby."; 9571RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. 9572RN [16] 9573RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 9574RC TISSUE=Spleen; 9575RX PubMed=14702039; DOI=10.1038/ng1285; 9576RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., 9577RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., 9578RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., 9579RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., 9580RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., 9581RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., 9582RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., 9583RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., 9584RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., 9585RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., 9586RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., 9587RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., 9588RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., 9589RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., 9590RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., 9591RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., 9592RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., 9593RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., 9594RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., 9595RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., 9596RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., 9597RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., 9598RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., 9599RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., 9600RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., 9601RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., 9602RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., 9603RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; 9604RT "Complete sequencing and characterization of 21,243 full-length human 9605RT cDNAs."; 9606RL Nat. Genet. 36:40-45(2004). 9607RN [17] 9608RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 9609RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., 9610RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., 9611RA Korn B., Zuo D., Hu Y., LaBaer J.; 9612RT "Cloning of human full open reading frames in Gateway(TM) system entry 9613RT vector (pDONR201)."; 9614RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. 9615RN [18] 9616RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 9617RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 9618RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 9619RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 9620RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 9621RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 9622RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 9623RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 9624RA Venter J.C.; 9625RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 9626RN [19] 9627RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 9628RC TISSUE=Skeletal muscle; 9629RX PubMed=15489334; DOI=10.1101/gr.2596504; 9630RG The MGC Project Team; 9631RT "The status, quality, and expansion of the NIH full-length cDNA 9632RT project: the Mammalian Gene Collection (MGC)."; 9633RL Genome Res. 14:2121-2127(2004). 9634RN [20] 9635RP PROTEIN SEQUENCE OF 2-147. 9636RX PubMed=13872627; 9637RA Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G., 9638RA Rudloff V., Wittmann-Liebold B.; 9639RT "The constitution of normal adult human haemoglobin."; 9640RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961). 9641RN [21] 9642RP PROTEIN SEQUENCE OF 33-42, AND MASS SPECTROMETRY. 9643RX PubMed=1575724; DOI=10.1016/0006-291X(92)90699-L; 9644RA Glaemsta E.-L., Meyerson B., Silberring J., Terenius L., Nyberg F.; 9645RT "Isolation of a hemoglobin-derived opioid peptide from cerebrospinal 9646RT fluid of patients with cerebrovascular bleedings."; 9647RL Biochem. Biophys. Res. Commun. 184:1060-1066(1992). 9648RN [22] 9649RP PROTEIN SEQUENCE OF 33-42. 9650RA Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., 9651RA de Camargo A.C.M., Pimenta D.C.; 9652RL Submitted (JUN-2007) to UniProtKB. 9653RN [23] 9654RP PROTEIN SEQUENCE OF 97-121, NUCLEOTIDE SEQUENCE [MRNA] OF 106-113, AND 9655RP VARIANT BURKE ARG-108. 9656RX MEDLINE=94004581; PubMed=8401300; 9657RA Suzuki H., Wada C., Kamata K., Takahashi E., Sato N., Kunitomo T.; 9658RT "Globin chain synthesis in hemolytic anemia reticulocytes. A case of 9659RT hemoglobin Burke."; 9660RL Biochem. Mol. Biol. Int. 30:425-431(1993). 9661RN [24] 9662RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-147. 9663RX MEDLINE=85205333; PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9; 9664RA Lang K.M., Spritz R.A.; 9665RT "Cloning specific complete polyadenylylated 3'-terminal cDNA 9666RT segments."; 9667RL Gene 33:191-196(1985). 9668RN [25] 9669RP BISPHOSPHOGLYCERATE BINDING. 9670RX PubMed=4555506; DOI=10.1038/237146a0; 9671RA Arnone A.; 9672RT "X-ray diffraction study of binding of 2,3-diphosphoglycerate to human 9673RT deoxyhaemoglobin."; 9674RL Nature 237:146-149(1972). 9675RN [26] 9676RP ACETYLATION AT LYS-145. 9677RX PubMed=4531009; DOI=10.1073/pnas.71.12.4693; 9678RA Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.; 9679RT "Sites of acetylation of sickle cell hemoglobin by aspirin."; 9680RL Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974). 9681RN [27] 9682RP GLYCATION AT VAL-2. 9683RX MEDLINE=78138698; PubMed=635569; DOI=10.1126/science.635569; 9684RA Bunn H.F., Gabbay K.H., Gallop P.M.; 9685RT "The glycosylation of hemoglobin: relevance to diabetes mellitus."; 9686RL Science 200:21-27(1978). 9687RN [28] 9688RP GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, AND LACK OF 9689RP GLYCATION AT LYS-60; LYS-83 AND LYS-96. 9690RX PubMed=7358733; 9691RA Shapiro R., McManus M.J., Zalut C., Bunn H.F.; 9692RT "Sites of nonenzymatic glycosylation of human hemoglobin A."; 9693RL J. Biol. Chem. 255:3120-3127(1980). 9694RN [29] 9695RP INTERACTION WITH HAPTOGLOBIN. 9696RX MEDLINE=86242088; PubMed=3718478; 9697RA Yoshioka N., Atassi M.Z.; 9698RT "Haemoglobin binding with haptoglobin. Localization of the 9699RT haptoglobin-binding sites on the beta-chain of human haemoglobin by 9700RT synthetic overlapping peptides encompassing the entire chain."; 9701RL Biochem. J. 234:453-456(1986). 9702RN [30] 9703RP OXIDATION AT LEU-142. 9704RX PubMed=1520632; DOI=10.1111/j.1365-2141.1992.tb08179.x; 9705RA Brennan S.O., Shaw J., Allen J., George P.M.; 9706RT "Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta- 9707RT Coventry but is replaced by a novel amino acid of mass 129 daltons."; 9708RL Br. J. Haematol. 81:99-103(1992). 9709RN [31] 9710RP S-NITROSYLATION AT CYS-94. 9711RX PubMed=8637569; DOI=10.1038/380221a0; 9712RA Jia L., Bonaventura C., Bonaventura J., Stamler J.S.; 9713RT "S-nitrosohaemoglobin: a dynamic activity of blood involved in 9714RT vascular control."; 9715RL Nature 380:221-226(1996). 9716RN [32] 9717RP S-NITROSYLATION AT CYS-94. 9718RX MEDLINE=99060083; PubMed=9843411; DOI=10.1021/bi9816711; 9719RA Chan N.L., Rogers P.H., Arnone A.; 9720RT "Crystal structure of the S-nitroso form of liganded human 9721RT hemoglobin."; 9722RL Biochemistry 37:16459-16464(1998). 9723RN [33] 9724RP NITRIC OXIDE-BINDING. 9725RX MEDLINE=20056222; PubMed=10588683; DOI=10.1073/pnas.96.25.14206; 9726RA Durner J., Gow A.J., Stamler J.S., Glazebrook J.; 9727RT "Ancient origins of nitric oxide signaling in biological systems."; 9728RL Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999). 9729RN [34] 9730RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND MASS SPECTROMETRY. 9731RC TISSUE=Cervix carcinoma; 9732RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; 9733RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., 9734RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; 9735RT "Substrate and functional diversity of lysine acetylation revealed by 9736RT a proteomics survey."; 9737RL Mol. Cell 23:607-618(2006). 9738RN [35] 9739RP SYNTHESIS OF 33-42, AND FUNCTION. 9740RX PubMed=16904236; DOI=10.1016/j.peptides.2006.06.009; 9741RA Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S., 9742RA de Camargo A.C.M., Pimenta D.C.; 9743RT "Hemorphin and hemorphin-like peptides isolated from dog pancreas and 9744RT sheep brain are able to potentiate bradykinin activity in vivo."; 9745RL Peptides 27:2957-2966(2006). 9746RN [36] 9747RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASS 9748RP SPECTROMETRY. 9749RC TISSUE=Lung carcinoma; 9750RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; 9751RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., 9752RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., 9753RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., 9754RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., 9755RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; 9756RT "Global survey of phosphotyrosine signaling identifies oncogenic 9757RT kinases in lung cancer."; 9758RL Cell 131:1190-1203(2007). 9759RN [37] 9760RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 9761RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; 9762RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., 9763RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; 9764RT "Initial characterization of the human central proteome."; 9765RL BMC Syst. Biol. 5:17-17(2011). 9766RN [38] 9767RP ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS. 9768RX PubMed=4123689; DOI=10.1073/pnas.70.3.718; 9769RA Finch J.T., Perutz M.F., Bertles J.F., Doebler J.; 9770RT "Structure of sickled erythrocytes and of sickle-cell hemoglobin 9771RT fibers."; 9772RL Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973). 9773RN [39] 9774RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7. 9775RX PubMed=1195378; DOI=10.1016/S0022-2836(75)80108-2; 9776RA Wishner B.C., Ward K.B., Lattman E.E., Love W.E.; 9777RT "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution."; 9778RL J. Mol. Biol. 98:179-194(1975). 9779RN [40] 9780RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN. 9781RX MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4; 9782RA Fermi G.; 9783RT "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5- 9784RT A resolution: refinement of the atomic model."; 9785RL J. Mol. Biol. 97:237-256(1975). 9786RN [41] 9787RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN. 9788RX PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3; 9789RA Baldwin J.M.; 9790RT "The structure of human carbonmonoxy haemoglobin at 2.7-A 9791RT resolution."; 9792RL J. Mol. Biol. 136:103-128(1980). 9793RN [42] 9794RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN. 9795RX PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8; 9796RA Fermi G., Perutz M.F., Shaanan B., Fourme R.; 9797RT "The crystal structure of human deoxyhaemoglobin at 1.74 A 9798RT resolution."; 9799RL J. Mol. Biol. 175:159-174(1984). 9800RN [43] 9801RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38. 9802RX MEDLINE=92232710; PubMed=1567857; DOI=10.1021/bi00131a030; 9803RA Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.; 9804RT "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta 9805RT Trp-->Arg: a mutation that creates an intersubunit chloride-binding 9806RT site."; 9807RL Biochemistry 31:4111-4121(1992). 9808RN [44] 9809RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75. 9810RX PubMed=1507231; DOI=10.1016/0022-2836(92)90638-Z; 9811RA Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.; 9812RT "Structure-function relationships in the low-affinity mutant 9813RT haemoglobin Aalborg (Gly74 (E18)beta-->Arg)."; 9814RL J. Mol. Biol. 226:883-888(1992). 9815RN [45] 9816RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND BISPHOSPHOGLYCERATE 9817RP BINDING. 9818RX PubMed=8377203; DOI=10.1006/jmbi.1993.1505; 9819RA Richard V., Dodson G.G., Mauguen Y.; 9820RT "Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt 9821RT structure at 2.5 A resolution."; 9822RL J. Mol. Biol. 233:270-274(1993). 9823RN [46] 9824RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). 9825RX PubMed=8642597; DOI=10.1006/jmbi.1996.0124; 9826RA Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.; 9827RT "Crystal structure of T state haemoglobin with oxygen bound at all 9828RT four haems."; 9829RL J. Mol. Biol. 256:775-792(1996). 9830RN [47] 9831RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; 9832RP GLY-38 AND TYR-38. 9833RX PubMed=9521756; DOI=10.1021/bi9708702; 9834RA Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.; 9835RT "High-resolution crystal structures of human hemoglobin with mutations 9836RT at tryptophan 37beta: structural basis for a high-affinity T-state."; 9837RL Biochemistry 37:4358-4373(1998). 9838RN [48] 9839RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7. 9840RX PubMed=9830011; DOI=10.1074/jbc.273.49.32690; 9841RA Harrington D.J., Adachi K., Royer W.E. Jr.; 9842RT "Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp. 9843RT Implications for the structure and formation of the sickle cell 9844RT fiber."; 9845RL J. Biol. Chem. 273:32690-32696(1998). 9846RN [49] 9847RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7. 9848RX PubMed=12454462; DOI=10.1107/S0907444902016426; 9849RA Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L., 9850RA Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.; 9851RT "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A 9852RT resolution."; 9853RL Acta Crystallogr. D 58:2038-2042(2002). 9854RN [50] 9855RP VARIANT ALABAMA LYS-40. 9856RX MEDLINE=75109326; PubMed=1115799; 9857RA Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., 9858RA Atkins R.; 9859RT "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) 9860RT and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."; 9861RL Biochim. Biophys. Acta 379:28-32(1975). 9862RN [51] 9863RP INVOLVEMENT IN HEIBAN, AND VARIANT ST LOUIS GLN-29. 9864RX PubMed=186485; DOI=10.1172/JCI108561; 9865RA Thillet J., Cohen-Solal M., Seligmann M., Rosa J.; 9866RT "Functional and physicochemical studies of hemoglobin St. Louis beta 9867RT 28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron."; 9868RL J. Clin. Invest. 58:1098-1106(1976). 9869RN [52] 9870RP INVOLVEMENT IN B-THALIB. 9871RX PubMed=1971109; DOI=10.1073/pnas.87.10.3924; 9872RA Thein S.L., Hesketh C., Taylor P., Temperley I.J., Hutchinson R.M., 9873RA Old J.M., Wood W.G., Clegg J.B., Weatherall D.J.; 9874RT "Molecular basis for dominantly inherited inclusion body beta- 9875RT thalassemia."; 9876RL Proc. Natl. Acad. Sci. U.S.A. 87:3924-3928(1990). 9877RN [53] 9878RP VARIANT ALESHA MET-68. 9879RX MEDLINE=93322192; PubMed=8330974; 9880RA Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S., 9881RA Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.; 9882RT "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable 9883RT hemoglobin variant identified through sequencing of amplified DNA."; 9884RL Hemoglobin 17:217-225(1993). 9885RN [54] 9886RP VARIANT J-ALTGELDS GARDENS ASP-93. 9887RX MEDLINE=79067354; PubMed=721609; 9888RA Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.; 9889RT "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a 9890RT substitution of the proximal histidine of the beta-chain."; 9891RL Hemoglobin 2:403-415(1978). 9892RN [55] 9893RP VARIANT ANKARA ASP-11. 9894RX MEDLINE=74297498; PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0; 9895RA Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.; 9896RT "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp)."; 9897RL FEBS Lett. 42:121-123(1974). 9898RN [56] 9899RP VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128. 9900RX MEDLINE=86216227; PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0; 9901RA Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S., 9902RA Webber B.B., Altay C., Martinez A.V.; 9903RT "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family 9904RT and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish 9905RT family; correction of a previously published identification."; 9906RL Biochim. Biophys. Acta 871:229-231(1986). 9907RN [57] 9908RP VARIANT J-AUCKLAND ASP-26. 9909RX MEDLINE=88006903; PubMed=3654265; 9910RA Williamson D., Wells R.M.G., Anderson R., Matthews J.; 9911RT "A new unstable and low oxygen affinity hemoglobin variant: Hb J- 9912RT Auckland [beta 25(B7)Gly-->Asp]."; 9913RL Hemoglobin 11:221-230(1987). 9914RN [58] 9915RP VARIANT AURORA TYR-140. 9916RX MEDLINE=96352910; PubMed=8718692; 9917RA Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.; 9918RT "Identification of a new high oxygen affinity hemoglobin variant: Hb 9919RT Aurora [beta 139(H17) Asn-->Tyr]."; 9920RL Hemoglobin 19:335-341(1995). 9921RN [59] 9922RP VARIANT BREST LYS-128. 9923RX MEDLINE=88256755; PubMed=3384710; 9924RA Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., 9925RA Briere J., Galacteros F.; 9926RT "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human 9927RT hemoglobin variant located at the alpha 1 beta 1 interface with 9928RT specific electrophoretic behavior."; 9929RL Hemoglobin 12:179-188(1988). 9930RN [60] 9931RP VARIANT BRISBANE HIS-69. 9932RX MEDLINE=81239159; PubMed=6166590; 9933RA Brennan S.O., Wells R.M., Smith H., Carrell R.W.; 9934RT "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen 9935RT affinity variant."; 9936RL Hemoglobin 5:325-335(1981). 9937RN [61] 9938RP VARIANT BUNBURY ASN-95. 9939RX MEDLINE=84031649; PubMed=6629823; 9940RA Como P.F., Kennett D., Wilkinson T., Kronenberg H.; 9941RT "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury: 9942RT alpha 2 beta 2 [94 (FG1) Asp replaced by Asn]."; 9943RL Hemoglobin 7:413-421(1983). 9944RN [62] 9945RP VARIANT J-CAIRO GLN-66. 9946RX MEDLINE=76114933; PubMed=1247583; 9947RA Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.; 9948RT "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin 9949RT variant discovered in an Egyptian family."; 9950RL Biochim. Biophys. Acta 420:97-104(1976). 9951RN [63] 9952RP VARIANT CAMPERDOWN SER-105. 9953RX MEDLINE=75184109; PubMed=1138922; 9954RA Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M., 9955RA Kronenberg H.; 9956RT "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) 9957RT arginine->serine)."; 9958RL Biochim. Biophys. Acta 393:195-200(1975). 9959RN [64] 9960RP VARIANT CARIBBEAN ARG-92. 9961RX MEDLINE=77048866; PubMed=992050; DOI=10.1016/0014-5793(76)80662-X; 9962RA Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E., 9963RA Seakins M., Lang A., Middleton A., Lehmann H.; 9964RT "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly 9965RT haemoglobin with a low oxygen affinity."; 9966RL FEBS Lett. 69:99-102(1976). 9967RN [65] 9968RP VARIANT CITY OF HOPE SER-70. 9969RX MEDLINE=85006311; PubMed=6434492; 9970RA Rahbar S., Asmerom Y., Blume K.G.; 9971RT "A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope 9972RT beta 69 (E13) Gly-->Ser."; 9973RL Hemoglobin 8:333-342(1984). 9974RN [66] 9975RP VARIANT COIMBRA GLU-100. 9976RX MEDLINE=92267852; PubMed=1814856; 9977RA Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M., 9978RA Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.; 9979RT "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered 9980RT high oxygen affinity variant."; 9981RL Hemoglobin 15:487-496(1991). 9982RN [67] 9983RP VARIANT COSTA RICA ARG-78. 9984RX MEDLINE=96235282; PubMed=8641705; DOI=10.1007/s004390050145; 9985RA Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H., 9986RA Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.; 9987RT "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example 9988RT of a somatic cell mutation in a globin gene."; 9989RL Hum. Genet. 97:829-833(1996). 9990RN [68] 9991RP VARIANT DEBROUSSE PRO-97. 9992RX MEDLINE=96180033; PubMed=8602627; 9993RX DOI=10.1002/(SICI)1096-8652(199604)51:4<276::AID-AJH5>3.0.CO;2-T; 9994RA Lacan P., Kister J., Francina A., Souillet G., Galacteros F., 9995RA Delaunay J., Wajcman H.; 9996RT "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable 9997RT hemoglobin with twofold increased oxygen affinity."; 9998RL Am. J. Hematol. 51:276-281(1996). 9999RN [69] 10000RP VARIANT DHONBURI GLY-127. 10001RX MEDLINE=90379198; PubMed=2399911; DOI=10.1002/ajh.2830350206; 10002RA Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., 10003RA Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P., 10004RA Galacteros F.; 10005RT "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable 10006RT beta variant producing a beta-thalassemia intermedia phenotype in 10007RT association with beta zero-thalassemia."; 10008RL Am. J. Hematol. 35:96-99(1990). 10009RN [70] 10010RP VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, AND DESCRIPTION OF 10011RP VARIANT DUINO. 10012RX MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961; 10013RA Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., 10014RA Melevendi C., Rasore A., Galacteros F.; 10015RT "Two new human hemoglobin variants caused by unusual mutational 10016RT events: Hb Zaire contains a five residue repetition within the alpha- 10017RT chain and Hb Duino has two residues substituted in the beta-chain."; 10018RL Hum. Genet. 89:676-680(1992). 10019RN [71] 10020RP VARIANT DURHAM-N.C. PRO-115. 10021RX MEDLINE=93244842; PubMed=1301199; DOI=10.1002/humu.1380010207; 10022RA Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M., 10023RA Melevendi C., Pirastu M., Cao A.; 10024RT "A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), 10025RT causing a severe beta-thalassemia intermedia phenotype."; 10026RL Hum. Mutat. 1:124-128(1992). 10027RN [72] 10028RP VARIANT DURHAM-N.C. PRO-115. 10029RX MEDLINE=94154273; PubMed=8111050; 10030RA de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.; 10031RT "A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], 10032RT produces a dominant thalassemia-like phenotype."; 10033RL Blood 83:1109-1116(1994). 10034RN [73] 10035RP VARIANT J-EUROPA ASP-63. 10036RX MEDLINE=96407264; PubMed=8811317; 10037RA Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F., 10038RA Wajcman H.; 10039RT "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties 10040RT in a new variant involving a residue located distal to the heme."; 10041RL Hemoglobin 20:135-140(1996). 10042RN [74] 10043RP VARIANT GEELONG ASP-140. 10044RX MEDLINE=92010939; PubMed=1917539; 10045RA Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B., 10046RA Tibben E.A., Wilkinson T., Kronenberg H.; 10047RT "Hb Geelong [beta 139(H17)Asn-->Asp]."; 10048RL Hemoglobin 15:85-95(1991). 10049RN [75] 10050RP VARIANT GRANGE-BLANCHE VAL-28. 10051RX MEDLINE=88030044; PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4; 10052RA Baklouti F., Giraud Y., Francina A., Richard G., Perier C., 10053RA Geyssant A., Jaubert J., Brizard C., Delaunay J.; 10054RT "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with 10055RT normal expression and increased affinity for oxygen."; 10056RL FEBS Lett. 223:59-62(1987). 10057RN [76] 10058RP VARIANT GRAZ LEU-3. 10059RX MEDLINE=93138927; PubMed=1487420; 10060RA Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P., 10061RA Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.; 10062RT "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant 10063RT observed in four families from southern Austria."; 10064RL Hemoglobin 16:493-501(1992). 10065RN [77] 10066RP VARIANT HELSINKI MET-83. 10067RX MEDLINE=77062201; PubMed=826083; 10068RA Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F., 10069RA Nagai K., Lang A., Lehmann H.; 10070RT "Hb Helsinki: a variant with a high oxygen affinity and a substitution 10071RT at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met)."; 10072RL Acta Haematol. 56:257-275(1976). 10073RN [78] 10074RP VARIANT HIMEJI ASP-141. 10075RX MEDLINE=86167527; PubMed=3754244; 10076RA Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., 10077RA Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.; 10078RT "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin 10079RT with increased beta N-terminal glycation."; 10080RL Hemoglobin 10:109-126(1986). 10081RN [79] 10082RP VARIANT HINSDALE LYS-140. 10083RX MEDLINE=90093866; PubMed=2513289; 10084RA Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.; 10085RT "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central 10086RT cavity showing reduced affinity for oxygen and 2,3- 10087RT diphosphoglycerate."; 10088RL Hemoglobin 13:455-464(1989). 10089RN [80] 10090RP VARIANT HINWIL ASN-39. 10091RX MEDLINE=96351651; PubMed=8745430; 10092RA Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C., 10093RA Cao A., Breitenstein U., Fehr J., Tuchschmid P.; 10094RT "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected 10095RT in a Swiss family."; 10096RL Hemoglobin 20:31-40(1996). 10097RN [81] 10098RP VARIANT HOWICK GLY-38. 10099RX MEDLINE=94193408; PubMed=8144352; 10100RA Owen M.C., Ockelford P.A., Wells R.M.G.; 10101RT "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant 10102RT of the alpha 1 beta 2 contact."; 10103RL Hemoglobin 17:513-521(1993). 10104RN [82] 10105RP VARIANT INDIANAPOLIS ARG-113. 10106RX MEDLINE=79151109; PubMed=429365; 10107RA Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G., 10108RA Tsistrakis G.A.; 10109RT "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An 10110RT unstable variant detectable only by isotopic labeling."; 10111RL J. Biol. Chem. 254:3479-3482(1979). 10112RN [83] 10113RP VARIANT ISEHARA ASN-93. 10114RX MEDLINE=92155974; PubMed=1787097; 10115RA Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.; 10116RT "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable 10117RT variant with a proximal histidine substitution at the heme contact."; 10118RL Hemoglobin 15:279-290(1991). 10119RN [84] 10120RP VARIANT ISTAMBUL GLN-93. 10121RX MEDLINE=73054825; PubMed=4639022; DOI=10.1172/JCI107050; 10122RA Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J., 10123RA Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.; 10124RT "Hemoglobin Istanbul: substitution of glutamine for histidine in a 10125RT proximal histidine (F8(92))."; 10126RL J. Clin. Invest. 51:2380-2387(1972). 10127RN [85] 10128RP VARIANT JACKSONVILLE ASP-55. 10129RX MEDLINE=91331861; PubMed=2101840; 10130RA Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H., 10131RA Moo-Penn W.F.; 10132RT "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable 10133RT variant found in a patient with hemolytic anemia."; 10134RL Hemoglobin 14:653-659(1990). 10135RN [86] 10136RP VARIANT JIANGHUA ILE-121. 10137RX MEDLINE=84007581; PubMed=6618888; 10138RA Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H., 10139RA Huang P.Y., Chen S.S., Jai P.C., Yang K.G.; 10140RT "Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast- 10141RT moving variant found in China."; 10142RL Hemoglobin 7:321-326(1983). 10143RN [87] 10144RP VARIANT KARLSKOGA HIS-22. 10145RX MEDLINE=93322190; PubMed=8330972; 10146RA Landin B.; 10147RT "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving 10148RT variant found in Sweden."; 10149RL Hemoglobin 17:201-208(1993). 10150RN [88] 10151RP VARIANT KNOSSOS SER-28. 10152RX MEDLINE=83079719; PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1; 10153RA Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y., 10154RA Komis G., Sellaye M., Boussiou M., Rosa J.; 10155RT "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to 10156RT Ser. A new abnormal hemoglobin present as a silent beta-thalassemia."; 10157RL FEBS Lett. 147:247-250(1982). 10158RN [89] 10159RP VARIANT KODAIRA GLN-147. 10160RX MEDLINE=92340295; PubMed=1634367; 10161RA Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., 10162RA Matsunaga T.; 10163RT "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an 10164RT amino acid substitution at the C-terminus."; 10165RL Hemoglobin 16:85-91(1992). 10166RN [90] 10167RP VARIANT KOFU ILE-85. 10168RX MEDLINE=86303641; PubMed=3744871; 10169RA Harano T., Harano K., Ueda S., Imai N., Kitazumi T.; 10170RT "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu 10171RT or alpha 2 beta 2 84 (EF8) Thr-->Ile."; 10172RL Hemoglobin 10:417-420(1986). 10173RN [91] 10174RP VARIANT HRADEC KRALOVE ASP-116. 10175RX MEDLINE=94042221; PubMed=7693620; 10176RA Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P., 10177RA Huisman T.H.J.; 10178RT "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a 10179RT severely unstable hemoglobin variant resulting in a dominant beta- 10180RT thalassemia trait in a Czech family."; 10181RL Hemoglobin 17:319-328(1993). 10182RN [92] 10183RP VARIANT LA DESIRADE VAL-130. 10184RX MEDLINE=87165149; PubMed=3557994; 10185RA Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., 10186RA Galacteros F., Feingold J., Rosa J.; 10187RT "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new 10188RT unstable hemoglobin."; 10189RL Hemoglobin 10:593-605(1986). 10190RN [93] 10191RP VARIANT LA ROCHE-SUR-YON HIS-82. 10192RX MEDLINE=92172947; PubMed=1540659; DOI=10.1016/0925-4439(92)90052-O; 10193RA Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C., 10194RA Cottenceau D., Galacteros F.; 10195RT "Structure of the EF corner favors deamidation of asparaginyl residues 10196RT in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) 10197RT Leu-->His]."; 10198RL Biochim. Biophys. Acta 1138:127-132(1992). 10199RN [94] 10200RP VARIANT LAS PALMAS PHE-50. 10201RX MEDLINE=88256753; PubMed=3384708; 10202RA Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H., 10203RA Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.; 10204RT "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable 10205RT hemoglobin variant."; 10206RL Hemoglobin 12:163-170(1988). 10207RN [95] 10208RP VARIANT LINKOPING THR-37. 10209RX MEDLINE=88083482; PubMed=3691763; 10210RA Berlin G., Wranne B., Jeppsson J.-O.; 10211RT "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity 10212RT hemoglobin variant found in two families of Finnish origin."; 10213RL Eur. J. Haematol. 39:452-456(1987). 10214RN [96] 10215RP VARIANT MAPUTO TYR-48. 10216RX MEDLINE=84031650; PubMed=6629824; 10217RA Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L., 10218RA Labie D.; 10219RT "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) 10220RT Asp replaced by Tyr) in combination with hemoglobin S, identified by 10221RT high performance liquid chromatography (HPLC)."; 10222RL Hemoglobin 7:423-433(1983). 10223RN [97] 10224RP VARIANT MATERA LYS-56. 10225RX MEDLINE=90346586; PubMed=2384314; 10226RA Sciarratta G.V., Ivaldi G.; 10227RT "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant 10228RT in an Italian family."; 10229RL Hemoglobin 14:79-85(1990). 10230RN [98] 10231RP VARIANT MIYASHIRO GLY-24. 10232RX MEDLINE=82166873; PubMed=7338468; 10233RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., 10234RA Shinohara T., Hori T., Takayama J.; 10235RT "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an 10236RT electrophoretically silent variant discovered by the isopropanol 10237RT test."; 10238RL Hemoglobin 5:653-666(1981). 10239RN [99] 10240RP VARIANT MIZUHO PRO-69. 10241RX MEDLINE=77248961; PubMed=893142; 10242RA Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.; 10243RT "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new 10244RT unstable variant associated with severe hemolytic anemia."; 10245RL Hemoglobin 1:467-477(1977). 10246RN [100] 10247RP VARIANT MUSCAT VAL-33. 10248RX MEDLINE=92387956; PubMed=1517102; 10249RA Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D., 10250RA Liu J.C., McKie K.M., Huisman T.H.J.; 10251RT "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed 10252RT in association with HB S in an Arabian family."; 10253RL Hemoglobin 16:259-266(1992). 10254RN [101] 10255RP VARIANT N-TIMONE GLU-9. 10256RX MEDLINE=90236754; PubMed=2634671; 10257RA Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C., 10258RA Blouquit Y., Craescu C.T., Galacteros F.; 10259RT "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving 10260RT variant with normal stability and oxygen affinity."; 10261RL Hemoglobin 13:743-747(1989). 10262RN [102] 10263RP VARIANT NAGOYA PRO-98. 10264RX MEDLINE=85206960; PubMed=3838976; 10265RA Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., 10266RA Shibata K., Shimokata H., Kuzuya F., Miwa S.; 10267RT "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 10268RT (FG4) His-->Pro."; 10269RL Hemoglobin 9:11-24(1985). 10270RN [103] 10271RP VARIANT D-NEATH ALA-122. 10272RX MEDLINE=93322197; PubMed=8330979; 10273RA Welch S.G., Bateman C.; 10274RT "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D 10275RT family."; 10276RL Hemoglobin 17:255-259(1993). 10277RN [104] 10278RP VARIANT NORTH CHICAGO SER-37. 10279RX MEDLINE=86139289; PubMed=3937824; 10280RA Rahbar S., Louis J., Lee T., Asmerom Y.; 10281RT "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high 10282RT affinity hemoglobin."; 10283RL Hemoglobin 9:559-576(1985). 10284RN [105] 10285RP VARIANT NORTH SHORE-CARACAS GLU-135. 10286RX MEDLINE=77246803; PubMed=891976; DOI=10.1016/0014-5793(77)80453-5; 10287RA Arends T., Lehmann H., Plowman D., Stathopoulou R.; 10288RT "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by 10289RT glutamic acid."; 10290RL FEBS Lett. 80:261-265(1977). 10291RN [106] 10292RP VARIANT OLOMOUC ASP-87. 10293RX MEDLINE=87307470; PubMed=3623975; 10294RA Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B., 10295RA Kutlar A., Huisman T.H.J.; 10296RT "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen 10297RT affinity variant."; 10298RL Hemoglobin 11:151-155(1987). 10299RN [107] 10300RP VARIANT PALMERSTON NORTH PHE-24. 10301RX MEDLINE=83135041; PubMed=7161106; 10302RA Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.; 10303RT "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new 10304RT variant identified in a patient with polycythemia."; 10305RL Hemoglobin 6:569-575(1982). 10306RN [108] 10307RP VARIANT PIERRE-BENITE ASP-91. 10308RX MEDLINE=88256754; PubMed=3384709; 10309RA Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J., 10310RA Delaunay J.; 10311RT "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity 10312RT variant found in a French family."; 10313RL Hemoglobin 12:171-177(1988). 10314RN [109] 10315RP VARIANT PRESBYTERIAN LYS-109. 10316RX MEDLINE=78215075; PubMed=668922; DOI=10.1016/0014-5793(78)80720-0; 10317RA Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.; 10318RT "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A 10319RT hemoglobin variant with low oxygen affinity."; 10320RL FEBS Lett. 92:53-56(1978). 10321RN [110] 10322RP VARIANT PUTTELANGE VAL-141. 10323RX MEDLINE=96101899; PubMed=8522332; DOI=10.1007/BF00210304; 10324RA Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I., 10325RA Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J., 10326RA Goossens M., Galacteros F.; 10327RT "Germline mosaicism for an alanine to valine substitution at residue 10328RT beta 140 in hemoglobin Puttelange, a new variant with high oxygen 10329RT affinity."; 10330RL Hum. Genet. 96:711-716(1995). 10331RN [111] 10332RP VARIANT QUIN-HAI ARG-79. 10333RX MEDLINE=84031648; PubMed=6629822; 10334RA Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y., 10335RA Chang F.Q., Chow Y.C., Chiu Y.; 10336RT "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new 10337RT abnormal hemoglobin found in Guangdong, China."; 10338RL Hemoglobin 7:407-412(1983). 10339RN [112] 10340RP VARIANT RAMBAM ASP-70. 10341RX MEDLINE=98432396; PubMed=9761252; 10342RA Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W., 10343RA van Dorsselaer A., Wieland H.; 10344RT "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment 10345RT of diabetic control: characterization by electrospray mass 10346RT spectrometry and HPLC."; 10347RL Clin. Chem. 44:2172-2177(1998). 10348RN [113] 10349RP VARIANT RANDWICK GLY-16. 10350RX MEDLINE=88256752; PubMed=3384707; 10351RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F., 10352RA Kwan Y.L., Holland R.A.B.; 10353RT "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta- 10354RT chain hemoglobin variant."; 10355RL Hemoglobin 12:149-161(1988). 10356RN [114] 10357RP VARIANT RIO GRANDE THR-9. 10358RX MEDLINE=83185445; PubMed=6857757; 10359RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L., 10360RA Therrell B.L. Jr.; 10361RT "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant 10362RT found in a Mexican-American family."; 10363RL Hemoglobin 7:91-95(1983). 10364RN [115] 10365RP VARIANT RUSH GLN-102. 10366RX MEDLINE=74080282; PubMed=4129558; 10367RA Adams J.G. III, Winter W.P., Tausk K., Heller P.; 10368RT "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin 10369RT causing mild hemolytic anemia."; 10370RL Blood 43:261-269(1974). 10371RN [116] 10372RP VARIANT SAITAMA PRO-118. 10373RX MEDLINE=83185440; PubMed=6687721; 10374RA Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., 10375RA Miyaji T.; 10376RT "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant 10377RT causing hemolytic disease."; 10378RL Hemoglobin 7:47-56(1983). 10379RN [117] 10380RP VARIANT M-SASKATOON TYR-64. 10381RX PubMed=13897827; DOI=10.1073/pnas.47.11.1758; 10382RA Gerald P.S., Efron M.L.; 10383RT "Chemical studies of several varieties of Hb M."; 10384RL Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961). 10385RN [118] 10386RP VARIANT SHELBY/LESLIE/DEACONESS LYS-132. 10387RX MEDLINE=85130256; PubMed=6526653; 10388RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.; 10389RT "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the 10390RT structure of hemoglobin Deaconess and hemoglobin Leslie."; 10391RL Hemoglobin 8:583-593(1984). 10392RN [119] 10393RP VARIANT J-SICILIA ASN-66. 10394RX MEDLINE=74302182; PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5; 10395RA Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.; 10396RT "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia."; 10397RL FEBS Lett. 39:200-204(1974). 10398RN [120] 10399RP VARIANT STANMORE ALA-112. 10400RX MEDLINE=92010936; PubMed=1917537; 10401RA Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T., 10402RA Kronenberg H., Holland R.A.B., Tibben E.A.; 10403RT "A new unstable and low oxygen affinity hemoglobin variant: Hb 10404RT Stanmore [beta 111(G13)Val-->Ala]."; 10405RL Hemoglobin 15:53-65(1991). 10406RN [121] 10407RP VARIANT ST MANDE TYR-103. 10408RX MEDLINE=81212764; PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0; 10409RA Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., 10410RA Chevrier M., Bordahandy C., Rosa J.; 10411RT "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low 10412RT oxygen affinity variant."; 10413RL FEBS Lett. 126:114-116(1981). 10414RN [122] 10415RP VARIANT WINDSOR ASP-12. 10416RX MEDLINE=90093865; PubMed=2599880; 10417RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B., 10418RA Tibben E.A.; 10419RT "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta- 10420RT chain hemoglobin variant producing a hemolytic anemia."; 10421RL Hemoglobin 13:437-453(1989). 10422RN [123] 10423RP VARIANT YAHATA TYR-113. 10424RX MEDLINE=92010926; PubMed=1917530; 10425RA Harano T., Harano K., Kushida Y., Ueda S.; 10426RT "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in 10427RT a Japanese: structural confirmation by DNA sequencing of the beta- 10428RT globin gene."; 10429RL Hemoglobin 15:109-113(1991). 10430RN [124] 10431RP VARIANT YOKOHAMA PRO-32. 10432RX MEDLINE=82166874; PubMed=7338469; 10433RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., 10434RA Matsumoto N.; 10435RT "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting 10436RT for Pro, causing hemolytic anemia."; 10437RL Hemoglobin 5:667-678(1981). 10438RN [125] 10439RP INVOLVEMENT IN HEIBAN, AND VARIANT HAMMERSMITH SER-43. 10440RX PubMed=6259091; 10441RA Rahbar S., Feagler R.J., Beutler E.; 10442RT "Hemoglobin Hammersmith (beta 42 (CD1) Phe replaced by Ser) associated 10443RT with severe hemolytic anemia."; 10444RL Hemoglobin 5:97-105(1981). 10445RN [126] 10446RP INVOLVEMENT IN HEIBAN, AND VARIANTS BRUXELLES PHE-42 DEL AND PHE-43 10447RP DEL. 10448RX PubMed=2599881; 10449RA Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H., 10450RA Orsini A., Rosa J., Galacteros F.; 10451RT "Hb Bruxelles: alpha 2A beta (2)41 or 42(C7 or CD1)Phe deleted."; 10452RL Hemoglobin 13:465-474(1989). 10453RN [127] 10454RP VARIANT ZENGCHENG MET-115. 10455RX MEDLINE=91177717; PubMed=2079435; 10456RA Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J., 10457RA Zeng Y.T., Shen M.; 10458RT "Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met."; 10459RL Hemoglobin 14:555-557(1990). 10460RN [128] 10461RP VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68. 10462RX PubMed=8280608; DOI=10.1111/j.1365-2141.1993.tb03178.x; 10463RA Fay K.C., Brennan S.O., Costello J.M., Potter H.C., Williamson D.A., 10464RA Trent R.J., Ockelford P.A., Boswell D.R.; 10465RT "Haemoglobin Manukau beta 67[E11] Val-->Gly: transfusion-dependent 10466RT haemolytic anaemia ameliorated by coexisting alpha thalassaemia."; 10467RL Br. J. Haematol. 85:352-355(1993). 10468RN [129] 10469RP INVOLVEMENT IN HEIBAN, AND VARIANT BRISTOL ASP-68. 10470RX PubMed=8704193; 10471RA Rees D.C., Rochette J., Schofield C., Green B., Morris M., 10472RA Parker N.E., Sasaki H., Tanaka A., Ohba Y., Clegg J.B.; 10473RT "A novel silent posttranslational mechanism converts methionine to 10474RT aspartate in hemoglobin Bristol (beta 67[E11] Val-Met->Asp)."; 10475RL Blood 88:341-348(1996). 10476RN [130] 10477RP VARIANT IRAQ-HALABJA VAL-11. 10478RX PubMed=10398311; 10479RX DOI=10.1002/(SICI)1096-8652(199907)61:3<187::AID-AJH5>3.0.CO;2-7; 10480RA Deutsch S., Darbellay R., Offord R.E., Frutiger A., Kister J., 10481RA Wajcman H., Beris P.; 10482RT "Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain 10483RT silent variant in a family with multiple Hb disorders."; 10484RL Am. J. Hematol. 61:187-193(1999). 10485RN [131] 10486RP VARIANT VILLEJUIF ILE-124. 10487RX PubMed=11300351; DOI=10.1081/HEM-100103071; 10488RA Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C., 10489RA Pucci P.; 10490RT "Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern 10491RT Italy."; 10492RL Hemoglobin 25:67-78(2001). 10493RN [132] 10494RP VARIANT TSUKUMI TYR-118. 10495RX PubMed=11300344; DOI=10.1081/HEM-100103076; 10496RA North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J., 10497RA Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.; 10498RT "Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman."; 10499RL Hemoglobin 25:107-110(2001). 10500RN [133] 10501RP VARIANT CANTERBURY PHE-113. 10502RX PubMed=11939514; DOI=10.1081/HEM-120002942; 10503RA Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A., 10504RA Ferguson M.M.; 10505RT "Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable 10506RT variant."; 10507RL Hemoglobin 26:67-69(2002). 10508RN [134] 10509RP VARIANT PYRGOS ASP-84, AND VARIANT E LYS-27. 10510RX PubMed=12144064; DOI=10.1081/HEM-120005459; 10511RA Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P., 10512RA Srisomsap C., Svasti J., Fucharoen S.; 10513RT "Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E 10514RT [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia."; 10515RL Hemoglobin 26:191-196(2002). 10516RN [135] 10517RP VARIANT SANTANDER ASP-35. 10518RX PubMed=12603091; DOI=10.1081/HEM-120016378; 10519RA Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E., 10520RA Rodrigo E., Arias M.; 10521RT "Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable 10522RT variant found as a de novo mutation in a Spanish patient."; 10523RL Hemoglobin 27:31-35(2003). 10524RN [136] 10525RP VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117. 10526RX PubMed=12908805; DOI=10.1081/HEM-120023384; 10527RA Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J., 10528RA Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L., 10529RA Galacteros F.; 10530RT "Two new hemoglobin variants with increased oxygen affinity: Hb Nantes 10531RT [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu]."; 10532RL Hemoglobin 27:191-199(2003). 10533RN [137] 10534RP VARIANT LYS-27. 10535RX PubMed=15481886; DOI=10.1081/HEM-120040334; 10536RA Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.; 10537RT "The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta- 10538RT globin anomalies in the Lao Theung population of southern Laos."; 10539RL Hemoglobin 28:197-204(2004). 10540CC -!- FUNCTION: Involved in oxygen transport from the lung to the 10541CC various peripheral tissues. 10542CC -!- FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin, 10543CC causing a decrease in blood pressure. 10544CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 10545CC adult hemoglobin A (HbA). 10546CC -!- INTERACTION: 10547CC P69905:HBA2; NbExp=19; IntAct=EBI-715554, EBI-714680; 10548CC -!- TISSUE SPECIFICITY: Red blood cells. 10549CC -!- PTM: Glucose reacts non-enzymatically with the N-terminus of the 10550CC beta chain to form a stable ketoamine linkage. This takes place 10551CC slowly and continuously throughout the 120-day life span of the 10552CC red blood cell. The rate of glycation is increased in patients 10553CC with diabetes mellitus. 10554CC -!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+) 10555CC and then transferred to Cys-94 to allow capture of O(2). 10556CC -!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin 10557CC exposure. PubMed:16916647 reports the identification of HBB 10558CC acetylated on Lys-145 in the cytosolic fraction of HeLa cells. 10559CC This may have resulted from contamination of the sample. 10560CC -!- MASS SPECTROMETRY: Mass=1310; Method=FAB; Range=33-42; 10561CC Source=PubMed:1575724; 10562CC -!- DISEASE: Defects in HBB may be a cause of Heinz body anemias 10563CC (HEIBAN) [MIM:140700]. This is a form of non-spherocytic hemolytic 10564CC anemia of Dacie type 1. After splenectomy, which has little 10565CC benefit, basophilic inclusions called Heinz bodies are 10566CC demonstrable in the erythrocytes. Before splenectomy, diffuse or 10567CC punctate basophilia may be evident. Most of these cases are 10568CC probably instances of hemoglobinopathy. The hemoglobin 10569CC demonstrates heat lability. Heinz bodies are observed also with 10570CC the Ivemark syndrome (asplenia with cardiovascular anomalies) and 10571CC with glutathione peroxidase deficiency. 10572CC -!- DISEASE: Defects in HBB are the cause of beta-thalassemia (B-THAL) 10573CC [MIM:613985]. A form of thalassemia. Thalassemias are common 10574CC monogenic diseases occurring mostly in Mediterranean and Southeast 10575CC Asian populations. The hallmark of beta-thalassemia is an 10576CC imbalance in globin-chain production in the adult HbA molecule. 10577CC Absence of beta chain causes beta(0)-thalassemia, while reduced 10578CC amounts of detectable beta globin causes beta(+)-thalassemia. In 10579CC the severe forms of beta-thalassemia, the excess alpha globin 10580CC chains accumulate in the developing erythroid precursors in the 10581CC marrow. Their deposition leads to a vast increase in erythroid 10582CC apoptosis that in turn causes ineffective erythropoiesis and 10583CC severe microcytic hypochromic anemia. Clinically, beta-thalassemia 10584CC is divided into thalassemia major which is transfusion dependent, 10585CC thalassemia intermedia (of intermediate severity), and thalassemia 10586CC minor that is asymptomatic. 10587CC -!- DISEASE: Defects in HBB are the cause of sickle cell anemia (SKCA) 10588CC [MIM:603903]; also known as sickle cell disease. Sickle cell 10589CC anemia is characterized by abnormally shaped red cells resulting 10590CC in chronic anemia and periodic episodes of pain, serious 10591CC infections and damage to vital organs. Normal red blood cells are 10592CC round and flexible and flow easily through blood vessels, but in 10593CC sickle cell anemia, the abnormal hemoglobin (called Hb S) causes 10594CC red blood cells to become stiff. They are C-shaped and resembles a 10595CC sickle. These stiffer red blood cells can led to microvascular 10596CC occlusion thus cutting off the blood supply to nearby tissues. 10597CC -!- DISEASE: Defects in HBB are the cause of beta-thalassemia dominant 10598CC inclusion body type (B-THALIB) [MIM:603902]. An autosomal dominant 10599CC form of beta thalassemia characterized by moderate anemia, 10600CC lifelong jaundice, cholelithiasis and splenomegaly, marked 10601CC morphologic changes in the red cells, erythroid hyperplasia of the 10602CC bone marrow with increased numbers of multinucleate red cell 10603CC precursors, and the presence of large inclusion bodies in the 10604CC normoblasts, both in the marrow and in the peripheral blood after 10605CC splenectomy. 10606CC -!- MISCELLANEOUS: One molecule of 2,3-bisphosphoglycerate can bind to 10607CC two beta chains per hemoglobin tetramer. 10608CC -!- SIMILARITY: Belongs to the globin family. 10609CC -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and 10610CC thalassemias; 10611CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB"; 10612CC -!- WEB RESOURCE: Name=GeneReviews; 10613CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBB"; 10614CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and 10615CC polymorphism database; 10616CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB"; 10617CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry; 10618CC URL="http://en.wikipedia.org/wiki/Hemoglobin"; 10619CC ----------------------------------------------------------------------- 10620CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 10621CC Distributed under the Creative Commons Attribution-NoDerivs License 10622CC ----------------------------------------------------------------------- 10623DR EMBL; M25079; AAA35597.1; -; mRNA. 10624DR EMBL; V00499; CAA23758.1; -; Genomic_DNA. 10625DR EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA. 10626DR EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA. 10627DR EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA. 10628DR EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA. 10629DR EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA. 10630DR EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA. 10631DR EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA. 10632DR EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA. 10633DR EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA. 10634DR EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA. 10635DR EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA. 10636DR EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA. 10637DR EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA. 10638DR EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA. 10639DR EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA. 10640DR EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA. 10641DR EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA. 10642DR EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA. 10643DR EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA. 10644DR EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA. 10645DR EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA. 10646DR EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA. 10647DR EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA. 10648DR EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA. 10649DR EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA. 10650DR EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA. 10651DR EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA. 10652DR EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA. 10653DR EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA. 10654DR EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA. 10655DR EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA. 10656DR EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA. 10657DR EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA. 10658DR EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA. 10659DR EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA. 10660DR EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA. 10661DR EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA. 10662DR EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA. 10663DR EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA. 10664DR EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA. 10665DR EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA. 10666DR EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA. 10667DR EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA. 10668DR EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA. 10669DR EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA. 10670DR EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA. 10671DR EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA. 10672DR EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA. 10673DR EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA. 10674DR EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA. 10675DR EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA. 10676DR EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA. 10677DR EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA. 10678DR EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA. 10679DR EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA. 10680DR EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA. 10681DR EMBL; AF007546; AAB62944.1; -; Genomic_DNA. 10682DR EMBL; AF083883; AAL68978.1; -; Genomic_DNA. 10683DR EMBL; AF117710; AAD19696.1; -; mRNA. 10684DR EMBL; AF181989; AAF00489.1; -; mRNA. 10685DR EMBL; AF349114; AAK29639.1; -; mRNA. 10686DR EMBL; AF527577; AAM92001.1; -; Genomic_DNA. 10687DR EMBL; AY136510; AAN11320.1; -; mRNA. 10688DR EMBL; AY163866; AAN84548.1; -; Genomic_DNA. 10689DR EMBL; AY260740; AAP21062.1; -; Genomic_DNA. 10690DR EMBL; AY509193; AAR96398.1; -; mRNA. 10691DR EMBL; EF450778; ABO36678.1; -; Genomic_DNA. 10692DR EMBL; EU694432; ACD39349.1; -; mRNA. 10693DR EMBL; AK311825; BAG34767.1; -; mRNA. 10694DR EMBL; CR536530; CAG38767.1; -; mRNA. 10695DR EMBL; CR541913; CAG46711.1; -; mRNA. 10696DR EMBL; CH471064; EAW68806.1; -; Genomic_DNA. 10697DR EMBL; BC007075; AAH07075.1; -; mRNA. 10698DR EMBL; U01317; AAA16334.1; -; Genomic_DNA. 10699DR EMBL; V00497; CAA23756.1; -; mRNA. 10700DR EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA. 10701DR EMBL; L26462; AAA21100.1; -; Genomic_DNA. 10702DR EMBL; L26463; AAA21101.1; -; Genomic_DNA. 10703DR EMBL; L26464; AAA21102.1; -; Genomic_DNA. 10704DR EMBL; L26465; AAA21103.1; -; Genomic_DNA. 10705DR EMBL; L26466; AAA21104.1; -; Genomic_DNA. 10706DR EMBL; L26467; AAA21105.1; -; Genomic_DNA. 10707DR EMBL; L26468; AAA21106.1; -; Genomic_DNA. 10708DR EMBL; L26469; AAA21107.1; -; Genomic_DNA. 10709DR EMBL; L26470; AAA21108.1; -; Genomic_DNA. 10710DR EMBL; L26471; AAA21109.1; -; Genomic_DNA. 10711DR EMBL; L26472; AAA21110.1; -; Genomic_DNA. 10712DR EMBL; L26473; AAA21111.1; -; Genomic_DNA. 10713DR EMBL; L26474; AAA21112.1; -; Genomic_DNA. 10714DR EMBL; L26475; AAA21113.1; -; Genomic_DNA. 10715DR EMBL; L26476; AAA21114.1; -; Genomic_DNA. 10716DR EMBL; L26477; AAA21115.1; -; Genomic_DNA. 10717DR EMBL; L26478; AAA21116.1; -; Genomic_DNA. 10718DR EMBL; L48213; AAA88063.1; -; Genomic_DNA. 10719DR EMBL; L48214; AAA88061.1; -; Genomic_DNA. 10720DR EMBL; L48215; AAA88059.1; -; Genomic_DNA. 10721DR EMBL; L48216; AAA88065.1; -; Genomic_DNA. 10722DR EMBL; L48217; AAA88067.1; -; Genomic_DNA. 10723DR EMBL; M36640; AAA52634.1; -; Genomic_DNA. 10724DR EMBL; M11428; AAA52633.1; -; mRNA. 10725DR EMBL; M25113; AAA35966.1; -; mRNA. 10726DR EMBL; L48932; AAA88054.1; -; Genomic_DNA. 10727DR IPI; IPI00654755; -. 10728DR PIR; A53136; HBHU. 10729DR RefSeq; NP_000509.1; NM_000518.4. 10730DR UniGene; Hs.523443; -. 10731DR PDB; 1A00; X-ray; 2.00 A; B/D=3-147. 10732DR PDB; 1A01; X-ray; 1.80 A; B/D=3-147. 10733DR PDB; 1A0U; X-ray; 2.14 A; B/D=3-147. 10734DR PDB; 1A0Z; X-ray; 2.00 A; B/D=3-147. 10735DR PDB; 1A3N; X-ray; 1.80 A; B/D=2-147. 10736DR PDB; 1A3O; X-ray; 1.80 A; B/D=2-147. 10737DR PDB; 1ABW; X-ray; 2.00 A; B/D=3-147. 10738DR PDB; 1ABY; X-ray; 2.60 A; B/D=3-147. 10739DR PDB; 1AJ9; X-ray; 2.20 A; B=2-147. 10740DR PDB; 1B86; X-ray; 2.50 A; B/D=2-147. 10741DR PDB; 1BAB; X-ray; 1.50 A; B/D=2-147. 10742DR PDB; 1BBB; X-ray; 1.70 A; B/D=2-147. 10743DR PDB; 1BIJ; X-ray; 2.30 A; B/D=2-147. 10744DR PDB; 1BUW; X-ray; 1.90 A; B/D=2-147. 10745DR PDB; 1BZ0; X-ray; 1.50 A; B/D=2-147. 10746DR PDB; 1BZ1; X-ray; 1.59 A; B/D=2-147. 10747DR PDB; 1BZZ; X-ray; 1.59 A; B/D=2-147. 10748DR PDB; 1C7B; X-ray; 1.80 A; B/D=3-147. 10749DR PDB; 1C7C; X-ray; 1.80 A; B/D=3-147. 10750DR PDB; 1C7D; X-ray; 1.80 A; B/D=3-147. 10751DR PDB; 1CBL; X-ray; 1.80 A; A/B/C/D=2-147. 10752DR PDB; 1CBM; X-ray; 1.74 A; A/B/C/D=1-147. 10753DR PDB; 1CH4; X-ray; 2.50 A; A/B/C/D=2-107. 10754DR PDB; 1CLS; X-ray; 1.90 A; B/D=1-147. 10755DR PDB; 1CMY; X-ray; 3.00 A; B/D=1-147. 10756DR PDB; 1COH; X-ray; 2.90 A; B/D=1-147. 10757DR PDB; 1DKE; X-ray; 2.10 A; B/D=1-147. 10758DR PDB; 1DXT; X-ray; 1.70 A; B/D=1-147. 10759DR PDB; 1DXU; X-ray; 1.70 A; B/D=3-147. 10760DR PDB; 1DXV; X-ray; 1.70 A; B/D=3-147. 10761DR PDB; 1FN3; X-ray; 2.48 A; B/D=2-147. 10762DR PDB; 1G9V; X-ray; 1.85 A; B/D=2-147. 10763DR PDB; 1GBU; X-ray; 1.80 A; B/D=2-147. 10764DR PDB; 1GBV; X-ray; 2.00 A; B/D=2-147. 10765DR PDB; 1GLI; X-ray; 2.50 A; B/D=3-147. 10766DR PDB; 1GZX; X-ray; 2.10 A; B/D=2-147. 10767DR PDB; 1HAB; X-ray; 2.30 A; B/D=2-146. 10768DR PDB; 1HAC; X-ray; 2.60 A; B/D=2-146. 10769DR PDB; 1HBA; X-ray; 2.10 A; B/D=2-147. 10770DR PDB; 1HBB; X-ray; 1.90 A; B/D=2-147. 10771DR PDB; 1HBS; X-ray; 3.00 A; B/D/F/H=1-147. 10772DR PDB; 1HCO; X-ray; 2.70 A; B=2-147. 10773DR PDB; 1HDB; X-ray; 2.20 A; B/D=1-147. 10774DR PDB; 1HGA; X-ray; 2.10 A; B/D=1-147. 10775DR PDB; 1HGB; X-ray; 2.10 A; B/D=1-147. 10776DR PDB; 1HGC; X-ray; 2.10 A; B/D=1-147. 10777DR PDB; 1HHO; X-ray; 2.10 A; B=1-147. 10778DR PDB; 1IRD; X-ray; 1.25 A; B=1-147. 10779DR PDB; 1J3Y; X-ray; 1.55 A; B/D/F/H=1-147. 10780DR PDB; 1J3Z; X-ray; 1.60 A; B/D/F/H=1-147. 10781DR PDB; 1J40; X-ray; 1.45 A; B/D/F/H=1-147. 10782DR PDB; 1J41; X-ray; 1.45 A; B/D/F/H=1-147. 10783DR PDB; 1J7S; X-ray; 2.20 A; B/D=3-147. 10784DR PDB; 1J7W; X-ray; 2.00 A; B/D=3-147. 10785DR PDB; 1J7Y; X-ray; 1.70 A; B/D=3-147. 10786DR PDB; 1JY7; X-ray; 3.20 A; B/D/Q/S/V/X=1-147. 10787DR PDB; 1K0Y; X-ray; 1.87 A; B/D=1-147. 10788DR PDB; 1K1K; X-ray; 2.00 A; B=1-147. 10789DR PDB; 1KD2; X-ray; 1.87 A; B/D=1-147. 10790DR PDB; 1LFL; X-ray; 2.70 A; B/D/Q/S=1-147. 10791DR PDB; 1LFQ; X-ray; 2.60 A; B=1-147. 10792DR PDB; 1LFT; X-ray; 2.60 A; B=1-147. 10793DR PDB; 1LFV; X-ray; 2.80 A; B=1-147. 10794DR PDB; 1LFY; X-ray; 3.30 A; B=1-147. 10795DR PDB; 1LFZ; X-ray; 3.10 A; B=1-147. 10796DR PDB; 1LJW; X-ray; 2.16 A; B=1-147. 10797DR PDB; 1M9P; X-ray; 2.10 A; B/D=1-147. 10798DR PDB; 1MKO; X-ray; 2.18 A; B/D=1-147. 10799DR PDB; 1NEJ; X-ray; 2.10 A; B/D=1-147. 10800DR PDB; 1NIH; X-ray; 2.60 A; B/D=1-147. 10801DR PDB; 1NQP; X-ray; 1.73 A; B/D=1-147. 10802DR PDB; 1O1I; X-ray; 2.30 A; B=1-147. 10803DR PDB; 1O1J; X-ray; 1.90 A; B/D=1-147. 10804DR PDB; 1O1K; X-ray; 2.00 A; B/D=1-147. 10805DR PDB; 1O1L; X-ray; 1.80 A; B/D=1-147. 10806DR PDB; 1O1M; X-ray; 1.85 A; B/D=1-147. 10807DR PDB; 1O1N; X-ray; 1.80 A; B/D=1-147. 10808DR PDB; 1O1O; X-ray; 1.80 A; B/D=1-147. 10809DR PDB; 1O1P; X-ray; 1.80 A; B/D=1-147. 10810DR PDB; 1QI8; X-ray; 1.80 A; B/D=3-147. 10811DR PDB; 1QSH; X-ray; 1.70 A; B/D=1-147. 10812DR PDB; 1QSI; X-ray; 1.70 A; B/D=1-147. 10813DR PDB; 1QXD; X-ray; 2.25 A; B/D=1-147. 10814DR PDB; 1QXE; X-ray; 1.85 A; B/D=1-147. 10815DR PDB; 1R1X; X-ray; 2.15 A; B=1-147. 10816DR PDB; 1R1Y; X-ray; 1.80 A; B/D=1-147. 10817DR PDB; 1RPS; X-ray; 2.11 A; B/D=1-147. 10818DR PDB; 1RQ3; X-ray; 1.91 A; B/D=1-147. 10819DR PDB; 1RQ4; X-ray; 2.11 A; B/D=1-147. 10820DR PDB; 1RQA; X-ray; 2.11 A; B/D=3-147. 10821DR PDB; 1RVW; X-ray; 2.50 A; B=1-147. 10822DR PDB; 1SDK; X-ray; 1.80 A; B/D=1-147. 10823DR PDB; 1SDL; X-ray; 1.80 A; B/D=1-147. 10824DR PDB; 1THB; X-ray; 1.50 A; B/D=1-147. 10825DR PDB; 1UIW; X-ray; 1.50 A; B/D/F/H=1-147. 10826DR PDB; 1VWT; X-ray; 1.90 A; B/D=1-147. 10827DR PDB; 1XXT; X-ray; 1.91 A; B/D=1-147. 10828DR PDB; 1XY0; X-ray; 1.99 A; B/D=1-147. 10829DR PDB; 1XYE; X-ray; 2.13 A; B/D=1-147. 10830DR PDB; 1XZ2; X-ray; 1.90 A; B/D=1-147. 10831DR PDB; 1XZ4; X-ray; 2.00 A; B/D=1-147. 10832DR PDB; 1XZ5; X-ray; 2.11 A; B/D=1-147. 10833DR PDB; 1XZ7; X-ray; 1.90 A; B/D=1-147. 10834DR PDB; 1XZU; X-ray; 2.16 A; B/D=1-147. 10835DR PDB; 1XZV; X-ray; 2.11 A; B/D=1-147. 10836DR PDB; 1Y09; X-ray; 2.25 A; B/D=1-147. 10837DR PDB; 1Y0A; X-ray; 2.22 A; B/D=1-147. 10838DR PDB; 1Y0C; X-ray; 2.30 A; B/D=1-147. 10839DR PDB; 1Y0D; X-ray; 2.10 A; B/D=1-147. 10840DR PDB; 1Y0T; X-ray; 2.14 A; B/D=3-147. 10841DR PDB; 1Y0W; X-ray; 2.14 A; B/D=3-147. 10842DR PDB; 1Y22; X-ray; 2.16 A; B/D=3-147. 10843DR PDB; 1Y2Z; X-ray; 2.07 A; B/D=3-147. 10844DR PDB; 1Y31; X-ray; 2.13 A; B/D=3-147. 10845DR PDB; 1Y35; X-ray; 2.12 A; B/D=3-147. 10846DR PDB; 1Y45; X-ray; 2.00 A; B/D=3-147. 10847DR PDB; 1Y46; X-ray; 2.22 A; B/D=3-147. 10848DR PDB; 1Y4B; X-ray; 2.10 A; B/D=3-147. 10849DR PDB; 1Y4F; X-ray; 2.00 A; B/D=3-147. 10850DR PDB; 1Y4G; X-ray; 1.91 A; B/D=3-147. 10851DR PDB; 1Y4P; X-ray; 1.98 A; B/D=3-147. 10852DR PDB; 1Y4Q; X-ray; 2.11 A; B/D=3-147. 10853DR PDB; 1Y4R; X-ray; 2.22 A; B/D=3-147. 10854DR PDB; 1Y4V; X-ray; 1.84 A; B/D=3-147. 10855DR PDB; 1Y5F; X-ray; 2.14 A; B/D=3-147. 10856DR PDB; 1Y5J; X-ray; 2.03 A; B/D=3-147. 10857DR PDB; 1Y5K; X-ray; 2.20 A; B/D=3-147. 10858DR PDB; 1Y7C; X-ray; 2.10 A; B/D=3-147. 10859DR PDB; 1Y7D; X-ray; 1.90 A; B/D=3-147. 10860DR PDB; 1Y7G; X-ray; 2.10 A; B/D=3-147. 10861DR PDB; 1Y7Z; X-ray; 1.98 A; B/D=3-147. 10862DR PDB; 1Y83; X-ray; 1.90 A; B/D=3-147. 10863DR PDB; 1Y85; X-ray; 2.13 A; B/D=1-146. 10864DR PDB; 1Y8W; X-ray; 2.90 A; B/D=1-147. 10865DR PDB; 1YDZ; X-ray; 3.30 A; B/D=1-147. 10866DR PDB; 1YE0; X-ray; 2.50 A; B/D=3-147. 10867DR PDB; 1YE1; X-ray; 4.50 A; B/D=3-147. 10868DR PDB; 1YE2; X-ray; 1.80 A; B/D=3-147. 10869DR PDB; 1YEN; X-ray; 2.80 A; B/D=3-147. 10870DR PDB; 1YEO; X-ray; 2.22 A; B/D=3-147. 10871DR PDB; 1YEQ; X-ray; 2.75 A; B/D=3-147. 10872DR PDB; 1YEU; X-ray; 2.12 A; B/D=3-147. 10873DR PDB; 1YEV; X-ray; 2.11 A; B/D=3-147. 10874DR PDB; 1YFF; X-ray; 2.40 A; B/D/F/H=1-147. 10875DR PDB; 1YG5; X-ray; 2.70 A; B/D=3-147. 10876DR PDB; 1YGD; X-ray; 2.73 A; B/D=3-147. 10877DR PDB; 1YGF; X-ray; 2.70 A; B/D=3-147. 10878DR PDB; 1YH9; X-ray; 2.20 A; B/D=1-147. 10879DR PDB; 1YHE; X-ray; 2.10 A; B/D=1-147. 10880DR PDB; 1YHR; X-ray; 2.60 A; B/D=1-147. 10881DR PDB; 1YIE; X-ray; 2.40 A; B/D=3-147. 10882DR PDB; 1YIH; X-ray; 2.00 A; B/D=3-147. 10883DR PDB; 1YVQ; X-ray; 1.80 A; B/D=1-147. 10884DR PDB; 1YVT; X-ray; 1.80 A; B=1-147. 10885DR PDB; 1YZI; X-ray; 2.07 A; B=1-147. 10886DR PDB; 2D5Z; X-ray; 1.45 A; B/D=1-147. 10887DR PDB; 2D60; X-ray; 1.70 A; B/D=1-147. 10888DR PDB; 2DN1; X-ray; 1.25 A; B=1-147. 10889DR PDB; 2DN2; X-ray; 1.25 A; B/D=1-147. 10890DR PDB; 2DN3; X-ray; 1.25 A; B=2-147. 10891DR PDB; 2DXM; Neutron; 2.10 A; B/D=2-147. 10892DR PDB; 2H35; NMR; -; B/D=2-147. 10893DR PDB; 2HBC; X-ray; 2.10 A; B=1-147. 10894DR PDB; 2HBD; X-ray; 2.20 A; B=1-147. 10895DR PDB; 2HBE; X-ray; 2.00 A; B=1-147. 10896DR PDB; 2HBF; X-ray; 2.20 A; B=1-147. 10897DR PDB; 2HBS; X-ray; 2.05 A; B/D/F/H=1-147. 10898DR PDB; 2HCO; X-ray; 2.70 A; B=2-147. 10899DR PDB; 2HHB; X-ray; 1.74 A; B/D=2-147. 10900DR PDB; 2HHD; X-ray; 2.20 A; B/D=1-147. 10901DR PDB; 2HHE; X-ray; 2.20 A; B/D=4-147. 10902DR PDB; 2W6V; X-ray; 1.80 A; B/D=2-147. 10903DR PDB; 2W72; X-ray; 1.07 A; B/D=3-147. 10904DR PDB; 2YRS; X-ray; 2.30 A; B/D/K/O=2-147. 10905DR PDB; 3B75; X-ray; 2.30 A; B/D/F/H/T=2-147. 10906DR PDB; 3D17; X-ray; 2.80 A; B/D=2-147. 10907DR PDB; 3D7O; X-ray; 1.80 A; B=2-147. 10908DR PDB; 3DUT; X-ray; 1.55 A; B/D=2-147. 10909DR PDB; 3HHB; X-ray; 1.74 A; B/D=2-147. 10910DR PDB; 3HXN; X-ray; 2.00 A; B/D=2-147. 10911DR PDB; 3IC0; X-ray; 1.80 A; B/D=2-146. 10912DR PDB; 3IC2; X-ray; 2.40 A; B/D=2-147. 10913DR PDB; 3KMF; Neutron; 2.00 A; C/G=2-147. 10914DR PDB; 3NL7; X-ray; 1.80 A; B=2-147. 10915DR PDB; 3NMM; X-ray; 1.60 A; B/D=2-147. 10916DR PDB; 3ODQ; X-ray; 3.10 A; B/D=2-147. 10917DR PDB; 3ONZ; X-ray; 2.09 A; B=2-147. 10918DR PDB; 3OO4; X-ray; 1.90 A; B=2-147. 10919DR PDB; 3OO5; X-ray; 2.10 A; B=2-147. 10920DR PDB; 3P5Q; X-ray; 2.00 A; B=2-147. 10921DR PDB; 3QJB; X-ray; 1.80 A; B=2-147. 10922DR PDB; 3QJC; X-ray; 2.00 A; B=2-147. 10923DR PDB; 3QJD; X-ray; 1.56 A; B/D=2-147. 10924DR PDB; 3QJE; X-ray; 1.80 A; B/D=2-147. 10925DR PDB; 3R5I; X-ray; 2.20 A; B/D=2-147. 10926DR PDB; 3S65; X-ray; 1.80 A; B/D=2-147. 10927DR PDB; 3S66; X-ray; 1.40 A; B=2-147. 10928DR PDB; 3SZK; X-ray; 3.01 A; B/E=2-147. 10929DR PDB; 4HHB; X-ray; 1.74 A; B/D=2-147. 10930DR PDB; 6HBW; X-ray; 2.00 A; B/D=2-147. 10931DR PDBsum; 1A00; -. 10932DR PDBsum; 1A01; -. 10933DR PDBsum; 1A0U; -. 10934DR PDBsum; 1A0Z; -. 10935DR PDBsum; 1A3N; -. 10936DR PDBsum; 1A3O; -. 10937DR PDBsum; 1ABW; -. 10938DR PDBsum; 1ABY; -. 10939DR PDBsum; 1AJ9; -. 10940DR PDBsum; 1B86; -. 10941DR PDBsum; 1BAB; -. 10942DR PDBsum; 1BBB; -. 10943DR PDBsum; 1BIJ; -. 10944DR PDBsum; 1BUW; -. 10945DR PDBsum; 1BZ0; -. 10946DR PDBsum; 1BZ1; -. 10947DR PDBsum; 1BZZ; -. 10948DR PDBsum; 1C7B; -. 10949DR PDBsum; 1C7C; -. 10950DR PDBsum; 1C7D; -. 10951DR PDBsum; 1CBL; -. 10952DR PDBsum; 1CBM; -. 10953DR PDBsum; 1CH4; -. 10954DR PDBsum; 1CLS; -. 10955DR PDBsum; 1CMY; -. 10956DR PDBsum; 1COH; -. 10957DR PDBsum; 1DKE; -. 10958DR PDBsum; 1DXT; -. 10959DR PDBsum; 1DXU; -. 10960DR PDBsum; 1DXV; -. 10961DR PDBsum; 1FN3; -. 10962DR PDBsum; 1G9V; -. 10963DR PDBsum; 1GBU; -. 10964DR PDBsum; 1GBV; -. 10965DR PDBsum; 1GLI; -. 10966DR PDBsum; 1GZX; -. 10967DR PDBsum; 1HAB; -. 10968DR PDBsum; 1HAC; -. 10969DR PDBsum; 1HBA; -. 10970DR PDBsum; 1HBB; -. 10971DR PDBsum; 1HBS; -. 10972DR PDBsum; 1HCO; -. 10973DR PDBsum; 1HDB; -. 10974DR PDBsum; 1HGA; -. 10975DR PDBsum; 1HGB; -. 10976DR PDBsum; 1HGC; -. 10977DR PDBsum; 1HHO; -. 10978DR PDBsum; 1IRD; -. 10979DR PDBsum; 1J3Y; -. 10980DR PDBsum; 1J3Z; -. 10981DR PDBsum; 1J40; -. 10982DR PDBsum; 1J41; -. 10983DR PDBsum; 1J7S; -. 10984DR PDBsum; 1J7W; -. 10985DR PDBsum; 1J7Y; -. 10986DR PDBsum; 1JY7; -. 10987DR PDBsum; 1K0Y; -. 10988DR PDBsum; 1K1K; -. 10989DR PDBsum; 1KD2; -. 10990DR PDBsum; 1LFL; -. 10991DR PDBsum; 1LFQ; -. 10992DR PDBsum; 1LFT; -. 10993DR PDBsum; 1LFV; -. 10994DR PDBsum; 1LFY; -. 10995DR PDBsum; 1LFZ; -. 10996DR PDBsum; 1LJW; -. 10997DR PDBsum; 1M9P; -. 10998DR PDBsum; 1MKO; -. 10999DR PDBsum; 1NEJ; -. 11000DR PDBsum; 1NIH; -. 11001DR PDBsum; 1NQP; -. 11002DR PDBsum; 1O1I; -. 11003DR PDBsum; 1O1J; -. 11004DR PDBsum; 1O1K; -. 11005DR PDBsum; 1O1L; -. 11006DR PDBsum; 1O1M; -. 11007DR PDBsum; 1O1N; -. 11008DR PDBsum; 1O1O; -. 11009DR PDBsum; 1O1P; -. 11010DR PDBsum; 1QI8; -. 11011DR PDBsum; 1QSH; -. 11012DR PDBsum; 1QSI; -. 11013DR PDBsum; 1QXD; -. 11014DR PDBsum; 1QXE; -. 11015DR PDBsum; 1R1X; -. 11016DR PDBsum; 1R1Y; -. 11017DR PDBsum; 1RPS; -. 11018DR PDBsum; 1RQ3; -. 11019DR PDBsum; 1RQ4; -. 11020DR PDBsum; 1RQA; -. 11021DR PDBsum; 1RVW; -. 11022DR PDBsum; 1SDK; -. 11023DR PDBsum; 1SDL; -. 11024DR PDBsum; 1THB; -. 11025DR PDBsum; 1UIW; -. 11026DR PDBsum; 1VWT; -. 11027DR PDBsum; 1XXT; -. 11028DR PDBsum; 1XY0; -. 11029DR PDBsum; 1XYE; -. 11030DR PDBsum; 1XZ2; -. 11031DR PDBsum; 1XZ4; -. 11032DR PDBsum; 1XZ5; -. 11033DR PDBsum; 1XZ7; -. 11034DR PDBsum; 1XZU; -. 11035DR PDBsum; 1XZV; -. 11036DR PDBsum; 1Y09; -. 11037DR PDBsum; 1Y0A; -. 11038DR PDBsum; 1Y0C; -. 11039DR PDBsum; 1Y0D; -. 11040DR PDBsum; 1Y0T; -. 11041DR PDBsum; 1Y0W; -. 11042DR PDBsum; 1Y22; -. 11043DR PDBsum; 1Y2Z; -. 11044DR PDBsum; 1Y31; -. 11045DR PDBsum; 1Y35; -. 11046DR PDBsum; 1Y45; -. 11047DR PDBsum; 1Y46; -. 11048DR PDBsum; 1Y4B; -. 11049DR PDBsum; 1Y4F; -. 11050DR PDBsum; 1Y4G; -. 11051DR PDBsum; 1Y4P; -. 11052DR PDBsum; 1Y4Q; -. 11053DR PDBsum; 1Y4R; -. 11054DR PDBsum; 1Y4V; -. 11055DR PDBsum; 1Y5F; -. 11056DR PDBsum; 1Y5J; -. 11057DR PDBsum; 1Y5K; -. 11058DR PDBsum; 1Y7C; -. 11059DR PDBsum; 1Y7D; -. 11060DR PDBsum; 1Y7G; -. 11061DR PDBsum; 1Y7Z; -. 11062DR PDBsum; 1Y83; -. 11063DR PDBsum; 1Y85; -. 11064DR PDBsum; 1Y8W; -. 11065DR PDBsum; 1YDZ; -. 11066DR PDBsum; 1YE0; -. 11067DR PDBsum; 1YE1; -. 11068DR PDBsum; 1YE2; -. 11069DR PDBsum; 1YEN; -. 11070DR PDBsum; 1YEO; -. 11071DR PDBsum; 1YEQ; -. 11072DR PDBsum; 1YEU; -. 11073DR PDBsum; 1YEV; -. 11074DR PDBsum; 1YFF; -. 11075DR PDBsum; 1YG5; -. 11076DR PDBsum; 1YGD; -. 11077DR PDBsum; 1YGF; -. 11078DR PDBsum; 1YH9; -. 11079DR PDBsum; 1YHE; -. 11080DR PDBsum; 1YHR; -. 11081DR PDBsum; 1YIE; -. 11082DR PDBsum; 1YIH; -. 11083DR PDBsum; 1YVQ; -. 11084DR PDBsum; 1YVT; -. 11085DR PDBsum; 1YZI; -. 11086DR PDBsum; 2D5Z; -. 11087DR PDBsum; 2D60; -. 11088DR PDBsum; 2DN1; -. 11089DR PDBsum; 2DN2; -. 11090DR PDBsum; 2DN3; -. 11091DR PDBsum; 2DXM; -. 11092DR PDBsum; 2H35; -. 11093DR PDBsum; 2HBC; -. 11094DR PDBsum; 2HBD; -. 11095DR PDBsum; 2HBE; -. 11096DR PDBsum; 2HBF; -. 11097DR PDBsum; 2HBS; -. 11098DR PDBsum; 2HCO; -. 11099DR PDBsum; 2HHB; -. 11100DR PDBsum; 2HHD; -. 11101DR PDBsum; 2HHE; -. 11102DR PDBsum; 2W6V; -. 11103DR PDBsum; 2W72; -. 11104DR PDBsum; 2YRS; -. 11105DR PDBsum; 3B75; -. 11106DR PDBsum; 3D17; -. 11107DR PDBsum; 3D7O; -. 11108DR PDBsum; 3DUT; -. 11109DR PDBsum; 3HHB; -. 11110DR PDBsum; 3HXN; -. 11111DR PDBsum; 3IC0; -. 11112DR PDBsum; 3IC2; -. 11113DR PDBsum; 3KMF; -. 11114DR PDBsum; 3NL7; -. 11115DR PDBsum; 3NMM; -. 11116DR PDBsum; 3ODQ; -. 11117DR PDBsum; 3ONZ; -. 11118DR PDBsum; 3OO4; -. 11119DR PDBsum; 3OO5; -. 11120DR PDBsum; 3P5Q; -. 11121DR PDBsum; 3QJB; -. 11122DR PDBsum; 3QJC; -. 11123DR PDBsum; 3QJD; -. 11124DR PDBsum; 3QJE; -. 11125DR PDBsum; 3R5I; -. 11126DR PDBsum; 3S65; -. 11127DR PDBsum; 3S66; -. 11128DR PDBsum; 3SZK; -. 11129DR PDBsum; 4HHB; -. 11130DR PDBsum; 6HBW; -. 11131DR ProteinModelPortal; P68871; -. 11132DR SMR; P68871; 2-147. 11133DR IntAct; P68871; 6. 11134DR MINT; MINT-5000306; -. 11135DR STRING; P68871; -. 11136DR PhosphoSite; P68871; -. 11137DR DMDM; 56749856; -. 11138DR PMMA-2DPAGE; P68871; -. 11139DR REPRODUCTION-2DPAGE; IPI00654755; -. 11140DR REPRODUCTION-2DPAGE; P68871; -. 11141DR Siena-2DPAGE; P68871; -. 11142DR SWISS-2DPAGE; P68871; -. 11143DR UCD-2DPAGE; P02023; -. 11144DR UCD-2DPAGE; P68871; -. 11145DR PeptideAtlas; P68871; -. 11146DR PRIDE; P68871; -. 11147DR DNASU; 3043; -. 11148DR Ensembl; ENST00000335295; ENSP00000333994; ENSG00000244734. 11149DR GeneID; 3043; -. 11150DR KEGG; hsa:3043; -. 11151DR UCSC; uc001mae.1; human. 11152DR CTD; 3043; -. 11153DR GeneCards; GC11M005250; -. 11154DR HGNC; HGNC:4827; HBB. 11155DR HPA; CAB009526; -. 11156DR MIM; 140700; phenotype. 11157DR MIM; 141900; gene+phenotype. 11158DR MIM; 603902; phenotype. 11159DR MIM; 603903; phenotype. 11160DR MIM; 613985; phenotype. 11161DR neXtProt; NX_P68871; -. 11162DR Orphanet; 231214; Beta-thalassemia major. 11163DR Orphanet; 178330; Heinz body anemia. 11164DR Orphanet; 231242; Hemoglobin C - beta-thalassemia. 11165DR Orphanet; 2132; Hemoglobin C disease. 11166DR Orphanet; 46532; Hereditary persistence of fetal hemoglobin - beta-thalassemia. 11167DR Orphanet; 251359; Sickle cell - beta-thalassemia disease. 11168DR Orphanet; 232; Sickle cell anemia. 11169DR PharmGKB; PA29202; -. 11170DR eggNOG; NOG269316; -. 11171DR GeneTree; ENSGT00650000093060; -. 11172DR HOVERGEN; HBG009709; -. 11173DR InParanoid; P68871; -. 11174DR KO; K13823; -. 11175DR OMA; DAVMNNP; -. 11176DR OrthoDB; EOG4THVVF; -. 11177DR Reactome; REACT_604; Hemostasis. 11178DR DrugBank; DB00893; Iron Dextran. 11179DR EvolutionaryTrace; P68871; -. 11180DR NextBio; 12048; -. 11181DR PMAP-CutDB; P68871; -. 11182DR ArrayExpress; P68871; -. 11183DR Bgee; P68871; -. 11184DR Genevestigator; P68871; -. 11185DR GermOnline; ENSG00000188170; Homo sapiens. 11186DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL. 11187DR GO; GO:0005833; C:hemoglobin complex; NAS:UniProtKB. 11188DR GO; GO:0020037; F:heme binding; IEA:InterPro. 11189DR GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB. 11190DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB. 11191DR GO; GO:0005344; F:oxygen transporter activity; NAS:UniProtKB. 11192DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. 11193DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL. 11194DR GO; GO:0030185; P:nitric oxide transport; NAS:UniProtKB. 11195DR GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL. 11196DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:UniProtKB. 11197DR GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL. 11198DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW. 11199DR GO; GO:0050880; P:regulation of blood vessel size; IEA:UniProtKB-KW. 11200DR GO; GO:0070293; P:renal absorption; IMP:UniProtKB. 11201DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 11202DR InterPro; IPR000971; Globin. 11203DR InterPro; IPR009050; Globin-like. 11204DR InterPro; IPR012292; Globin_dom. 11205DR InterPro; IPR002337; Haemoglobin_b. 11206DR Pfam; PF00042; Globin; 1. 11207DR PRINTS; PR00814; BETAHAEM. 11208DR SUPFAM; SSF46458; Globin_like; 1. 11209DR PROSITE; PS01033; GLOBIN; 1. 11210PE 1: Evidence at protein level; 11211KW 3D-structure; Acetylation; Complete proteome; 11212KW Congenital dyserythropoietic anemia; Direct protein sequencing; 11213KW Disease mutation; Glycation; Glycoprotein; Heme; 11214KW Hereditary hemolytic anemia; Hypotensive agent; Iron; Metal-binding; 11215KW Oxygen transport; Phosphoprotein; Polymorphism; Pyruvate; 11216KW Reference proteome; S-nitrosylation; Transport; Vasoactive. 11217FT INIT_MET 1 1 Removed. 11218FT CHAIN 2 147 Hemoglobin subunit beta. 11219FT /FTId=PRO_0000052976. 11220FT PEPTIDE 33 42 LVV-hemorphin-7. 11221FT /FTId=PRO_0000296641. 11222FT METAL 64 64 Iron (heme distal ligand). 11223FT METAL 93 93 Iron (heme proximal ligand). 11224FT BINDING 2 2 2,3-bisphosphoglycerate; via amino 11225FT nitrogen. 11226FT BINDING 3 3 2,3-bisphosphoglycerate. 11227FT BINDING 83 83 2,3-bisphosphoglycerate. 11228FT BINDING 144 144 2,3-bisphosphoglycerate. 11229FT SITE 60 60 Not glycated. 11230FT SITE 83 83 Not glycated. 11231FT SITE 96 96 Not glycated. 11232FT SITE 142 142 Susceptible to oxidation; associated with 11233FT variant Atlanta, variant non-spherocytic 11234FT haemolytic anemia and variant 11235FT Christchurch. 11236FT SITE 145 145 Aspirin-acetylated lysine. 11237FT MOD_RES 2 2 N-acetylalanine; in variant Raleigh. 11238FT MOD_RES 2 2 N-pyruvate 2-iminyl-valine; in Hb A1b. 11239FT MOD_RES 94 94 S-nitrosocysteine. 11240FT MOD_RES 131 131 Phosphotyrosine. 11241FT CARBOHYD 2 2 N-linked (Glc) (glycation); in Hb A1c. 11242FT CARBOHYD 9 9 N-linked (Glc) (glycation). 11243FT CARBOHYD 18 18 N-linked (Glc) (glycation). 11244FT CARBOHYD 67 67 N-linked (Glc) (glycation). 11245FT CARBOHYD 121 121 N-linked (Glc) (glycation). 11246FT CARBOHYD 145 145 N-linked (Glc) (glycation). 11247FT VARIANT 2 2 V -> A (in Raleigh; O(2) affinity down; 11248FT dbSNP:rs33949930). 11249FT /FTId=VAR_002856. 11250FT VARIANT 3 3 H -> L (in Graz; dbSNP:rs35906307). 11251FT /FTId=VAR_002857. 11252FT VARIANT 3 3 H -> Q (in Okayama; O(2) affinity up; 11253FT dbSNP:rs713040). 11254FT /FTId=VAR_002858. 11255FT VARIANT 3 3 H -> R (in Deer Lodge; O(2) affinity up; 11256FT dbSNP:rs33983205). 11257FT /FTId=VAR_002859. 11258FT VARIANT 3 3 H -> Y (in Fukuoka; dbSNP:rs35906307). 11259FT /FTId=VAR_002860. 11260FT VARIANT 6 6 P -> R (in Warwickshire; 11261FT dbSNP:rs34769005). 11262FT /FTId=VAR_002861. 11263FT VARIANT 7 7 E -> A (in G-Makassar). 11264FT /FTId=VAR_002862. 11265FT VARIANT 7 7 E -> K (in C). 11266FT /FTId=VAR_002864. 11267FT VARIANT 7 7 E -> Q (in Machida; dbSNP:rs33930165). 11268FT /FTId=VAR_002865. 11269FT VARIANT 7 7 E -> V (in S; sickle cell anemia; 11270FT dbSNP:rs334). 11271FT /FTId=VAR_002863. 11272FT VARIANT 8 8 E -> G (in G-San Jose; mildly unstable; 11273FT dbSNP:rs34948328). 11274FT /FTId=VAR_002866. 11275FT VARIANT 8 8 E -> K (in G-Siriraj; dbSNP:rs34948328). 11276FT /FTId=VAR_002867. 11277FT VARIANT 9 9 K -> E (in N-Timone; dbSNP:rs33932981). 11278FT /FTId=VAR_002868. 11279FT VARIANT 9 9 K -> Q (in J-Luhe; dbSNP:rs33926764). 11280FT /FTId=VAR_002869. 11281FT VARIANT 9 9 K -> T (in Rio Grande). 11282FT /FTId=VAR_002870. 11283FT VARIANT 10 10 S -> C (in Porto Alegre; O(2) affinity 11284FT up; dbSNP:rs33918131). 11285FT /FTId=VAR_002871. 11286FT VARIANT 11 11 A -> D (in Ankara; dbSNP:rs33947457). 11287FT /FTId=VAR_002872. 11288FT VARIANT 11 11 A -> V (in Iraq-Halabja). 11289FT /FTId=VAR_025393. 11290FT VARIANT 12 12 V -> D (in Windsor; O(2) affinity up; 11291FT unstable; dbSNP:rs33974228). 11292FT /FTId=VAR_002873. 11293FT VARIANT 12 12 V -> I (in Hamilton). 11294FT /FTId=VAR_002874. 11295FT VARIANT 14 14 A -> D (in J-Lens; dbSNP:rs35203747). 11296FT /FTId=VAR_002875. 11297FT VARIANT 15 15 L -> P (in Saki; unstable). 11298FT /FTId=VAR_002876. 11299FT VARIANT 15 15 L -> R (in Soegn; unstable; 11300FT dbSNP:rs33935445). 11301FT /FTId=VAR_002877. 11302FT VARIANT 16 16 W -> G (in Randwick; unstable; 11303FT dbSNP:rs33946157). 11304FT /FTId=VAR_002878. 11305FT VARIANT 16 16 W -> R (in Belfast; O(2) affinity up; 11306FT unstable; dbSNP:rs33946157). 11307FT /FTId=VAR_002879. 11308FT VARIANT 17 17 G -> D (in J-Baltimore/J-Trinidad/J- 11309FT Ireland/J-Georgia/N-New Haven). 11310FT /FTId=VAR_002880. 11311FT VARIANT 17 17 G -> R (in D-Bushman). 11312FT /FTId=VAR_002881. 11313FT VARIANT 18 18 K -> E (in Nagasaki; dbSNP:rs33986703). 11314FT /FTId=VAR_002882. 11315FT VARIANT 18 18 K -> N (in J-Amiens; dbSNP:rs36006214). 11316FT /FTId=VAR_002883. 11317FT VARIANT 18 18 K -> Q (in Nikosia; dbSNP:rs33986703). 11318FT /FTId=VAR_002884. 11319FT VARIANT 19 19 V -> M (in Baden; slightly unstable; 11320FT dbSNP:rs35802118). 11321FT /FTId=VAR_002885. 11322FT VARIANT 20 20 N -> D (in Alamo; dbSNP:rs34866629). 11323FT /FTId=VAR_002886. 11324FT VARIANT 20 20 N -> K (in D-Ouleh RABAH). 11325FT /FTId=VAR_002887. 11326FT VARIANT 20 20 N -> S (in Malay; dbSNP:rs33972047). 11327FT /FTId=VAR_002888. 11328FT VARIANT 21 21 V -> M (in Olympia; O(2) affinity up; 11329FT dbSNP:rs35890959). 11330FT /FTId=VAR_002889. 11331FT VARIANT 22 22 D -> G (in Connecticut; O(2) affinity 11332FT down; dbSNP:rs33977536). 11333FT /FTId=VAR_002890. 11334FT VARIANT 22 22 D -> H (in Karlskoga; dbSNP:rs33950093). 11335FT /FTId=VAR_002892. 11336FT VARIANT 22 22 D -> N (in Cocody). 11337FT /FTId=VAR_002891. 11338FT VARIANT 22 22 D -> Y (in Yusa). 11339FT /FTId=VAR_002893. 11340FT VARIANT 23 23 E -> A (in G-Coushatta/G-Saskatoon/G- 11341FT Taegu/Hsin Chu; dbSNP:rs33936254). 11342FT /FTId=VAR_002894. 11343FT VARIANT 23 23 E -> G (in G-Taipei). 11344FT /FTId=VAR_002895. 11345FT VARIANT 23 23 E -> K (in E-Saskatoon; unstable). 11346FT /FTId=VAR_002896. 11347FT VARIANT 23 23 E -> Q (in D-Iran). 11348FT /FTId=VAR_002897. 11349FT VARIANT 23 23 E -> V (in D-Granada). 11350FT /FTId=VAR_002898. 11351FT VARIANT 24 24 V -> D (in Strasbourg; O(2) affinity up). 11352FT /FTId=VAR_002899. 11353FT VARIANT 24 24 V -> F (in Palmerston North; O(2) 11354FT affinity up; unstable). 11355FT /FTId=VAR_002900. 11356FT VARIANT 24 24 V -> G (in Miyashiro; O(2) affinity up; 11357FT unstable). 11358FT /FTId=VAR_002901. 11359FT VARIANT 25 25 G -> D (in Moscva; O(2) affinity down; 11360FT unstable). 11361FT /FTId=VAR_002902. 11362FT VARIANT 25 25 G -> R (in Riverdale-Bronx; O(2) affinity 11363FT up; unstable). 11364FT /FTId=VAR_002903. 11365FT VARIANT 25 25 G -> V (in Savannah; unstable). 11366FT /FTId=VAR_002904. 11367FT VARIANT 26 26 G -> D (in J-Auckland; unstable; O(2) 11368FT affinity down). 11369FT /FTId=VAR_002905. 11370FT VARIANT 26 26 G -> R (in G-Taiwan Ami). 11371FT /FTId=VAR_002906. 11372FT VARIANT 27 27 E -> K (in E). 11373FT /FTId=VAR_002907. 11374FT VARIANT 27 27 E -> V (in Henri Mondor; slightly 11375FT unstable). 11376FT /FTId=VAR_002908. 11377FT VARIANT 28 28 A -> D (in Volga/Drenthe; unstable). 11378FT /FTId=VAR_002909. 11379FT VARIANT 28 28 A -> S (in Knossos). 11380FT /FTId=VAR_002910. 11381FT VARIANT 28 28 A -> V (in Grange-blanche; O(2) affinity 11382FT up). 11383FT /FTId=VAR_002911. 11384FT VARIANT 29 29 L -> P (in Genova/Hyogo; unstable). 11385FT /FTId=VAR_002912. 11386FT VARIANT 29 29 L -> Q (in St Louis). 11387FT /FTId=VAR_035236. 11388FT VARIANT 30 30 G -> D (in Lufkin; unstable). 11389FT /FTId=VAR_002913. 11390FT VARIANT 31 31 R -> S (in Tacoma; unstable). 11391FT /FTId=VAR_002914. 11392FT VARIANT 32 32 L -> P (in Yokohama; unstable). 11393FT /FTId=VAR_002915. 11394FT VARIANT 33 33 L -> R (in Castilla; unstable). 11395FT /FTId=VAR_002916. 11396FT VARIANT 33 33 L -> V (in Muscat; slightly unstable). 11397FT /FTId=VAR_002917. 11398FT VARIANT 35 35 V -> D (in Santander; unstable). 11399FT /FTId=VAR_025394. 11400FT VARIANT 35 35 V -> F (in Pitie-Salpetriere; O(2) 11401FT affinity up). 11402FT /FTId=VAR_002918. 11403FT VARIANT 35 35 V -> L (in Nantes; increased oxygen 11404FT affinity). 11405FT /FTId=VAR_025395. 11406FT VARIANT 36 36 Y -> F (in Philly; O(2) affinity up; 11407FT unstable). 11408FT /FTId=VAR_002919. 11409FT VARIANT 37 37 P -> R (in Sunnybrook). 11410FT /FTId=VAR_002920. 11411FT VARIANT 37 37 P -> S (in North Chicago; O(2) affinity 11412FT up). 11413FT /FTId=VAR_002921. 11414FT VARIANT 37 37 P -> T (in Linkoping/Finlandia; O(2) 11415FT affinity up). 11416FT /FTId=VAR_002922. 11417FT VARIANT 38 38 W -> G (in Howick). 11418FT /FTId=VAR_002923. 11419FT VARIANT 38 38 W -> R (in Rothschild; O(2) affinity 11420FT down). 11421FT /FTId=VAR_002925. 11422FT VARIANT 38 38 W -> S (in Hirose; O(2) affinity up). 11423FT /FTId=VAR_002924. 11424FT VARIANT 39 39 T -> N (in Hinwil; O(2) affinity up). 11425FT /FTId=VAR_002926. 11426FT VARIANT 40 40 Q -> E (in Vaasa; unstable). 11427FT /FTId=VAR_002927. 11428FT VARIANT 40 40 Q -> K (in Alabama). 11429FT /FTId=VAR_002928. 11430FT VARIANT 40 40 Q -> R (in Tianshui). 11431FT /FTId=VAR_002929. 11432FT VARIANT 42 42 F -> Y (in Mequon). 11433FT /FTId=VAR_002930. 11434FT VARIANT 42 42 Missing (in Bruxelles). 11435FT /FTId=VAR_035237. 11436FT VARIANT 43 43 F -> L (in Louisville; unstable). 11437FT /FTId=VAR_002931. 11438FT VARIANT 43 43 F -> S (in Hammersmith). 11439FT /FTId=VAR_035239. 11440FT VARIANT 43 43 Missing (in Bruxelles). 11441FT /FTId=VAR_035238. 11442FT VARIANT 44 44 E -> Q (in Hoshida/Chaya). 11443FT /FTId=VAR_002932. 11444FT VARIANT 45 45 S -> C (in Mississippi). 11445FT /FTId=VAR_002933. 11446FT VARIANT 46 46 F -> S (in Cheverly; unstable). 11447FT /FTId=VAR_002934. 11448FT VARIANT 47 47 G -> E (in K-Ibadan). 11449FT /FTId=VAR_002935. 11450FT VARIANT 48 48 D -> A (in Avicenna). 11451FT /FTId=VAR_002936. 11452FT VARIANT 48 48 D -> G (in Gavello). 11453FT /FTId=VAR_002937. 11454FT VARIANT 48 48 D -> Y (in Maputo). 11455FT /FTId=VAR_002938. 11456FT VARIANT 49 49 L -> P (in Bab-Saadoum; slightly 11457FT unstable). 11458FT /FTId=VAR_002939. 11459FT VARIANT 50 50 S -> F (in Las Palmas; slightly 11460FT unstable). 11461FT /FTId=VAR_002940. 11462FT VARIANT 51 51 T -> K (in Edmonton). 11463FT /FTId=VAR_002941. 11464FT VARIANT 52 52 P -> R (in Willamette; O(2) affinity up; 11465FT unstable). 11466FT /FTId=VAR_002942. 11467FT VARIANT 53 53 D -> A (in Ocho Rios). 11468FT /FTId=VAR_002943. 11469FT VARIANT 53 53 D -> H (in Summer Hill). 11470FT /FTId=VAR_002944. 11471FT VARIANT 55 55 V -> D (in Jacksonville; O(2) affinity 11472FT up; unstable). 11473FT /FTId=VAR_002945. 11474FT VARIANT 56 56 M -> K (in Matera; unstable). 11475FT /FTId=VAR_002946. 11476FT VARIANT 57 57 G -> R (in Hamadan). 11477FT /FTId=VAR_002947. 11478FT VARIANT 58 58 N -> K (in G-ferrara; unstable). 11479FT /FTId=VAR_002948. 11480FT VARIANT 59 59 P -> R (in Dhofar/Yukuhashi). 11481FT /FTId=VAR_002949. 11482FT VARIANT 60 60 K -> E (in I-High Wycombe). 11483FT /FTId=VAR_002950. 11484FT VARIANT 61 61 V -> A (in Collingwood; unstable). 11485FT /FTId=VAR_002951. 11486FT VARIANT 62 62 K -> E (in N-Seatlle). 11487FT /FTId=VAR_002952. 11488FT VARIANT 62 62 K -> M (in Bologna; O(2) affinity down). 11489FT /FTId=VAR_002953. 11490FT VARIANT 62 62 K -> N (in Hikari). 11491FT /FTId=VAR_002954. 11492FT VARIANT 63 63 A -> D (in J-Europa). 11493FT /FTId=VAR_002955. 11494FT VARIANT 63 63 A -> P (in Duarte; unstable). 11495FT /FTId=VAR_002956. 11496FT VARIANT 64 64 H -> Y (in M-Saskatoon; O(2) affinity 11497FT up). 11498FT /FTId=VAR_002957. 11499FT VARIANT 66 66 K -> M (in J-Antakya). 11500FT /FTId=VAR_002958. 11501FT VARIANT 66 66 K -> N (in J-Sicilia). 11502FT /FTId=VAR_002959. 11503FT VARIANT 66 66 K -> Q (in J-Cairo). 11504FT /FTId=VAR_002960. 11505FT VARIANT 67 67 K -> T (in Chico; O(2) affinity down). 11506FT /FTId=VAR_002961. 11507FT VARIANT 68 68 V -> A (in Sydney; unstable). 11508FT /FTId=VAR_002962. 11509FT VARIANT 68 68 V -> D (in Bristol). 11510FT /FTId=VAR_035240. 11511FT VARIANT 68 68 V -> G (in non-spherocytic haemolytic 11512FT anemia; Manukau; dbSNP:rs33918343). 11513FT /FTId=VAR_040060. 11514FT VARIANT 68 68 V -> M (in Alesha; unstable). 11515FT /FTId=VAR_002963. 11516FT VARIANT 69 69 L -> H (in Brisbane; O(2) affinity up). 11517FT /FTId=VAR_002964. 11518FT VARIANT 69 69 L -> P (in Mizuho; unstable). 11519FT /FTId=VAR_002965. 11520FT VARIANT 70 70 G -> D (in Rambam). 11521FT /FTId=VAR_002966. 11522FT VARIANT 70 70 G -> R (in Kenitra). 11523FT /FTId=VAR_002967. 11524FT VARIANT 70 70 G -> S (in City of Hope). 11525FT /FTId=VAR_002968. 11526FT VARIANT 71 71 A -> D (in Seattle; O(2) affinity down; 11527FT unstable). 11528FT /FTId=VAR_002969. 11529FT VARIANT 72 72 F -> S (in Christchurch; unstable). 11530FT /FTId=VAR_002970. 11531FT VARIANT 74 74 D -> G (in Tilburg; O(2) affinity down). 11532FT /FTId=VAR_002971. 11533FT VARIANT 74 74 D -> V (in Mobile; O(2) affinity down). 11534FT /FTId=VAR_002972. 11535FT VARIANT 74 74 D -> Y (in Vancouver; O(2) affinity 11536FT down). 11537FT /FTId=VAR_002973. 11538FT VARIANT 75 75 G -> R (in Aalborg; unstable). 11539FT /FTId=VAR_002974. 11540FT VARIANT 75 75 G -> V (in Bushwick; unstable). 11541FT /FTId=VAR_002975. 11542FT VARIANT 76 76 L -> P (in Atlanta; unstable). 11543FT /FTId=VAR_002976. 11544FT VARIANT 76 76 L -> R (in Pasadena; O(2) affinity up; 11545FT unstable). 11546FT /FTId=VAR_002977. 11547FT VARIANT 77 77 A -> D (in J-Chicago). 11548FT /FTId=VAR_002978. 11549FT VARIANT 78 78 H -> D (in J-Iran). 11550FT /FTId=VAR_002979. 11551FT VARIANT 78 78 H -> R (in Costa Rica). 11552FT /FTId=VAR_002980. 11553FT VARIANT 78 78 H -> Y (in Fukuyama). 11554FT /FTId=VAR_002981. 11555FT VARIANT 79 79 L -> R (in Quin-hai). 11556FT /FTId=VAR_002982. 11557FT VARIANT 80 80 D -> Y (in Tampa). 11558FT /FTId=VAR_002983. 11559FT VARIANT 81 81 N -> K (in G-Szuhu/Gifu). 11560FT /FTId=VAR_002984. 11561FT VARIANT 82 82 L -> H (in La Roche-sur-Yon; unstable and 11562FT O(2) affinity up). 11563FT /FTId=VAR_012663. 11564FT VARIANT 82 82 L -> R (in Baylor; unstable). 11565FT /FTId=VAR_002985. 11566FT VARIANT 82 82 L -> V (in dbSNP:rs11549406). 11567FT /FTId=VAR_049273. 11568FT VARIANT 83 83 K -> M (in Helsinki; O(2) affinity up). 11569FT /FTId=VAR_002986. 11570FT VARIANT 83 83 K -> N (in Providence). 11571FT /FTId=VAR_012664. 11572FT VARIANT 84 84 G -> D (in Pyrgos). 11573FT /FTId=VAR_025396. 11574FT VARIANT 84 84 G -> R (in Muskegon). 11575FT /FTId=VAR_002987. 11576FT VARIANT 85 85 T -> I (in Kofu). 11577FT /FTId=VAR_002988. 11578FT VARIANT 87 87 A -> D (in Olomouc; O(2) affinity up). 11579FT /FTId=VAR_002989. 11580FT VARIANT 88 88 T -> I (in Quebec-Chori). 11581FT /FTId=VAR_002990. 11582FT VARIANT 88 88 T -> K (in D-Ibadan). 11583FT /FTId=VAR_002991. 11584FT VARIANT 88 88 T -> P (in Valletta). 11585FT /FTId=VAR_002992. 11586FT VARIANT 89 89 L -> P (in Santa Ana; unstable). 11587FT /FTId=VAR_002993. 11588FT VARIANT 89 89 L -> R (in Boras; unstable). 11589FT /FTId=VAR_002994. 11590FT VARIANT 90 90 S -> N (in Creteil; O(2) affinity up). 11591FT /FTId=VAR_002995. 11592FT VARIANT 90 90 S -> R (in Vanderbilt; O(2) affinity up). 11593FT /FTId=VAR_002996. 11594FT VARIANT 91 91 E -> D (in Pierre-Benite; O(2) affinity 11595FT up). 11596FT /FTId=VAR_002997. 11597FT VARIANT 91 91 E -> K (in Agenogi; O(2) affinity down). 11598FT /FTId=VAR_002998. 11599FT VARIANT 92 92 L -> P (in Sabine; unstable). 11600FT /FTId=VAR_002999. 11601FT VARIANT 92 92 L -> R (in Caribbean; O(2) affinity down; 11602FT unstable). 11603FT /FTId=VAR_003000. 11604FT VARIANT 93 93 H -> D (in J-Altgelds Gardens; unstable). 11605FT /FTId=VAR_003001. 11606FT VARIANT 93 93 H -> N (in Isehara; unstable). 11607FT /FTId=VAR_003002. 11608FT VARIANT 93 93 H -> P (in Newcastle and Duino; 11609FT associated with S-104 in Duino; 11610FT unstable). 11611FT /FTId=VAR_003003. 11612FT VARIANT 93 93 H -> Q (in Istambul; O(2) affinity up; 11613FT unstable). 11614FT /FTId=VAR_003004. 11615FT VARIANT 94 94 C -> R (in Okazaki; O(2) affinity up; 11616FT unstable). 11617FT /FTId=VAR_003005. 11618FT VARIANT 95 95 D -> G (in Chandigarh). 11619FT /FTId=VAR_003006. 11620FT VARIANT 95 95 D -> H (in Barcelona; O(2) affinity up). 11621FT /FTId=VAR_003007. 11622FT VARIANT 95 95 D -> N (in Bunbury; O(2) affinity up). 11623FT /FTId=VAR_003008. 11624FT VARIANT 96 96 K -> M (in J-Cordoba). 11625FT /FTId=VAR_003009. 11626FT VARIANT 96 96 K -> N (in Detroit). 11627FT /FTId=VAR_003010. 11628FT VARIANT 97 97 L -> P (in Debrousse; unstable; O(2) 11629FT affinity up). 11630FT /FTId=VAR_003011. 11631FT VARIANT 97 97 L -> V (in Regina; O(2) affinity up). 11632FT /FTId=VAR_003012. 11633FT VARIANT 98 98 H -> L (in Wood; O(2) affinity up). 11634FT /FTId=VAR_003013. 11635FT VARIANT 98 98 H -> P (in Nagoya; O(2) affinity up; 11636FT unstable). 11637FT /FTId=VAR_003014. 11638FT VARIANT 98 98 H -> Q (in Malmoe; O(2) affinity up). 11639FT /FTId=VAR_003015. 11640FT VARIANT 98 98 H -> Y (in Moriguchi). 11641FT /FTId=VAR_003016. 11642FT VARIANT 99 99 V -> G (in Nottingham; unstable). 11643FT /FTId=VAR_003017. 11644FT VARIANT 100 100 D -> E (in Coimbra; O(2) affinity up). 11645FT /FTId=VAR_003018. 11646FT VARIANT 101 101 P -> L (in Brigham; O(2) affinity up). 11647FT /FTId=VAR_003019. 11648FT VARIANT 101 101 P -> R (in New Mexico). 11649FT /FTId=VAR_003020. 11650FT VARIANT 102 102 E -> D (in Potomac; O(2) affinity up). 11651FT /FTId=VAR_003021. 11652FT VARIANT 102 102 E -> G (in Alberta; O(2) affinity up). 11653FT /FTId=VAR_003022. 11654FT VARIANT 102 102 E -> K (in British Columbia; O(2) 11655FT affinity up). 11656FT /FTId=VAR_003023. 11657FT VARIANT 102 102 E -> Q (in Rush; unstable). 11658FT /FTId=VAR_003024. 11659FT VARIANT 103 103 N -> S (in Beth Israel; O(2) affinity 11660FT down; unstable). 11661FT /FTId=VAR_003025. 11662FT VARIANT 103 103 N -> Y (in St Mande; O(2) affinity down). 11663FT /FTId=VAR_003026. 11664FT VARIANT 104 104 F -> L (in Heathrow; O(2) affinity up). 11665FT /FTId=VAR_003027. 11666FT VARIANT 105 105 R -> S (in Camperdown and Duino; 11667FT associated with P-92 in Duino; unstable). 11668FT /FTId=VAR_003028. 11669FT VARIANT 105 105 R -> T (in Sherwood Forest). 11670FT /FTId=VAR_003029. 11671FT VARIANT 108 108 G -> R (in Burke; O(2) affinity down; 11672FT unstable). 11673FT /FTId=VAR_003030. 11674FT VARIANT 109 109 N -> K (in Presbyterian; O(2) affinity 11675FT down; unstable). 11676FT /FTId=VAR_003031. 11677FT VARIANT 110 110 V -> M (in San Diego; O(2) affinity up). 11678FT /FTId=VAR_003032. 11679FT VARIANT 111 111 L -> P (in Showa-Yakushiji). 11680FT /FTId=VAR_003033. 11681FT VARIANT 112 112 V -> A (in Stanmore; O(2) affinity down; 11682FT unstable). 11683FT /FTId=VAR_003034. 11684FT VARIANT 113 113 C -> F (in Canterbury). 11685FT /FTId=VAR_025397. 11686FT VARIANT 113 113 C -> R (in Indianapolis). 11687FT /FTId=VAR_003035. 11688FT VARIANT 113 113 C -> Y (in Yahata). 11689FT /FTId=VAR_003036. 11690FT VARIANT 115 115 L -> M (in Zengcheng). 11691FT /FTId=VAR_010144. 11692FT VARIANT 115 115 L -> P (in Durham-N.C./Brescia; causes 11693FT beta-thalassemia). 11694FT /FTId=VAR_010145. 11695FT VARIANT 116 116 A -> D (in Hradec Kralove; unstable; 11696FT causes severe beta-thalassemia). 11697FT /FTId=VAR_003037. 11698FT VARIANT 116 116 A -> P (in Madrid; unstable). 11699FT /FTId=VAR_003038. 11700FT VARIANT 117 117 H -> L (in Vexin; increased oxygen 11701FT affinity). 11702FT /FTId=VAR_025398. 11703FT VARIANT 117 117 H -> Q (in Hafnia). 11704FT /FTId=VAR_003039. 11705FT VARIANT 118 118 H -> P (in Saitama; unstable). 11706FT /FTId=VAR_003040. 11707FT VARIANT 118 118 H -> R (in P-Galveston). 11708FT /FTId=VAR_003041. 11709FT VARIANT 118 118 H -> Y (in Tsukumi). 11710FT /FTId=VAR_025399. 11711FT VARIANT 120 120 G -> A (in Iowa). 11712FT /FTId=VAR_003042. 11713FT VARIANT 121 121 K -> E (in Hijiyama). 11714FT /FTId=VAR_003043. 11715FT VARIANT 121 121 K -> I (in Jianghua). 11716FT /FTId=VAR_003044. 11717FT VARIANT 121 121 K -> Q (in Takamatsu). 11718FT /FTId=VAR_003045. 11719FT VARIANT 122 122 E -> A (in D-Neath). 11720FT /FTId=VAR_003046. 11721FT VARIANT 122 122 E -> G (in St Francis). 11722FT /FTId=VAR_003047. 11723FT VARIANT 122 122 E -> K (in O-Arab). 11724FT /FTId=VAR_003049. 11725FT VARIANT 122 122 E -> Q (in D-Los Angeles/D-Punjab/D- 11726FT Portugal/D-Chicago/D-Oak Ridge). 11727FT /FTId=VAR_003048. 11728FT VARIANT 122 122 E -> V (in D-Camperdown/Beograd). 11729FT /FTId=VAR_003050. 11730FT VARIANT 124 124 T -> I (in Villejuif; asymptomatic 11731FT variant). 11732FT /FTId=VAR_003051. 11733FT VARIANT 125 125 P -> Q (in Ty Gard; O(2) affinity up). 11734FT /FTId=VAR_003053. 11735FT VARIANT 125 125 P -> R (in Khartoum; unstable). 11736FT /FTId=VAR_003052. 11737FT VARIANT 125 125 P -> S (in Tunis). 11738FT /FTId=VAR_003054. 11739FT VARIANT 127 127 V -> A (in Beirut). 11740FT /FTId=VAR_003055. 11741FT VARIANT 127 127 V -> E (in Hofu; unstable). 11742FT /FTId=VAR_003057. 11743FT VARIANT 127 127 V -> G (in Dhonburi/Neapolis; unstable; 11744FT beta-thalassemia). 11745FT /FTId=VAR_003056. 11746FT VARIANT 128 128 Q -> E (in Complutense). 11747FT /FTId=VAR_003058. 11748FT VARIANT 128 128 Q -> K (in Brest; unstable). 11749FT /FTId=VAR_003059. 11750FT VARIANT 129 129 A -> D (in J-Guantanamo; unstable). 11751FT /FTId=VAR_003060. 11752FT VARIANT 130 130 A -> P (in Crete; O(2) affinity up; 11753FT unstable). 11754FT /FTId=VAR_003061. 11755FT VARIANT 130 130 A -> V (in La Desirade; O(2) affinity 11756FT down; unstable). 11757FT /FTId=VAR_003062. 11758FT VARIANT 131 131 Y -> D (in Wien; unstable). 11759FT /FTId=VAR_003063. 11760FT VARIANT 131 131 Y -> S (in Nevers). 11761FT /FTId=VAR_003064. 11762FT VARIANT 132 132 Q -> E (in Camden/Tokuchi/Motown). 11763FT /FTId=VAR_003065. 11764FT VARIANT 132 132 Q -> K (in Shelby/Leslie/Deaconess; 11765FT unstable). 11766FT /FTId=VAR_003066. 11767FT VARIANT 132 132 Q -> P (in Shangai; unstable). 11768FT /FTId=VAR_003067. 11769FT VARIANT 132 132 Q -> R (in Sarrebourg; unstable). 11770FT /FTId=VAR_003068. 11771FT VARIANT 133 133 K -> N (in Yamagata; O(2) affinity down). 11772FT /FTId=VAR_003069. 11773FT VARIANT 133 133 K -> Q (in K-Woolwich). 11774FT /FTId=VAR_003070. 11775FT VARIANT 134 134 V -> L (in Extredemura). 11776FT /FTId=VAR_003071. 11777FT VARIANT 135 135 V -> E (in North Shore-Caracas; 11778FT unstable). 11779FT /FTId=VAR_003072. 11780FT VARIANT 136 136 A -> E (in Beckman; O(2) affinity down; 11781FT unstable). 11782FT /FTId=VAR_003073. 11783FT VARIANT 136 136 A -> P (in Altdorf; O(2) affinity up; 11784FT unstable). 11785FT /FTId=VAR_003074. 11786FT VARIANT 137 137 G -> D (in Hope; O(2) affinity down; 11787FT unstable). 11788FT /FTId=VAR_003075. 11789FT VARIANT 139 139 A -> P (in Brockton; unstable). 11790FT /FTId=VAR_003076. 11791FT VARIANT 140 140 N -> D (in Geelong; unstable). 11792FT /FTId=VAR_003077. 11793FT VARIANT 140 140 N -> K (in Hinsdale; O(2) affinity down). 11794FT /FTId=VAR_003078. 11795FT VARIANT 140 140 N -> S (in S-Wake; associated with V-6). 11796FT /FTId=VAR_025335. 11797FT VARIANT 140 140 N -> Y (in Aurora; O(2) affinity up). 11798FT /FTId=VAR_003079. 11799FT VARIANT 141 141 A -> D (in Himeji; unstable; O(2) 11800FT affinity down). 11801FT /FTId=VAR_003080. 11802FT VARIANT 141 141 A -> T (in St Jacques: O(2) affinity up). 11803FT /FTId=VAR_003081. 11804FT VARIANT 141 141 A -> V (in Puttelange; polycythemia; O(2) 11805FT affinity up). 11806FT /FTId=VAR_003082. 11807FT VARIANT 142 142 L -> R (in Olmsted; unstable). 11808FT /FTId=VAR_003083. 11809FT VARIANT 143 143 A -> D (in Ohio; O(2) affinity up). 11810FT /FTId=VAR_003084. 11811FT VARIANT 144 144 H -> D (in Rancho Mirage). 11812FT /FTId=VAR_003085. 11813FT VARIANT 144 144 H -> P (in Syracuse; O(2) affinity up). 11814FT /FTId=VAR_003087. 11815FT VARIANT 144 144 H -> Q (in Little Rock; O(2) affinity 11816FT up). 11817FT /FTId=VAR_003086. 11818FT VARIANT 144 144 H -> R (in Abruzzo; O(2) affinity up). 11819FT /FTId=VAR_003088. 11820FT VARIANT 145 145 K -> E (in Mito; O(2) affinity up). 11821FT /FTId=VAR_003089. 11822FT VARIANT 146 146 Y -> C (in Rainier; O(2) affinity up). 11823FT /FTId=VAR_003090. 11824FT VARIANT 146 146 Y -> H (in Bethesda; O(2) affinity up). 11825FT /FTId=VAR_003091. 11826FT VARIANT 147 147 H -> D (in Hiroshima; O(2) affinity up). 11827FT /FTId=VAR_003092. 11828FT VARIANT 147 147 H -> L (in Cowtown; O(2) affinity up). 11829FT /FTId=VAR_003093. 11830FT VARIANT 147 147 H -> P (in York; O(2) affinity up). 11831FT /FTId=VAR_003094. 11832FT VARIANT 147 147 H -> Q (in Kodaira; O(2) affinity up). 11833FT /FTId=VAR_003095. 11834FT CONFLICT 26 26 Missing (in Ref. 15; ACD39349). 11835FT CONFLICT 42 42 F -> L (in Ref. 13; AAR96398). 11836FT HELIX 6 16 11837FT TURN 21 23 11838FT HELIX 24 35 11839FT HELIX 37 42 11840FT HELIX 44 46 11841FT HELIX 52 57 11842FT HELIX 59 77 11843FT TURN 78 80 11844FT HELIX 82 94 11845FT TURN 95 97 11846FT HELIX 102 119 11847FT HELIX 120 122 11848FT HELIX 125 142 11849FT HELIX 144 146 11850SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; 11851 MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK 11852 VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG 11853 KEFTPPVQAA YQKVVAGVAN ALAHKYH 11854// 11855ID HBB_PANPA Reviewed; 147 AA. 11856AC P68872; P02023; Q13852; Q14481; Q14510; Q9BX96; Q9UCP8; Q9UCP9; 11857DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 11858DT 23-JAN-2007, sequence version 2. 11859DT 13-JUN-2012, entry version 44. 11860DE RecName: Full=Hemoglobin subunit beta; 11861DE AltName: Full=Beta-globin; 11862DE AltName: Full=Hemoglobin beta chain; 11863GN Name=HBB; 11864OS Pan paniscus (Pygmy chimpanzee) (Bonobo). 11865OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 11866OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 11867OC Catarrhini; Hominidae; Pan. 11868OX NCBI_TaxID=9597; 11869RN [1] 11870RP PROTEIN SEQUENCE OF 2-147. 11871RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; 11872RA Goodman M., Braunitzer G., Stangl A., Schrank B.; 11873RT "Evidence on human origins from haemoglobins of African apes."; 11874RL Nature 303:546-548(1983). 11875CC -!- FUNCTION: Involved in oxygen transport from the lung to the 11876CC various peripheral tissues. 11877CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 11878CC adult hemoglobin A (HbA). 11879CC -!- TISSUE SPECIFICITY: Red blood cells. 11880CC -!- SIMILARITY: Belongs to the globin family. 11881CC ----------------------------------------------------------------------- 11882CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 11883CC Distributed under the Creative Commons Attribution-NoDerivs License 11884CC ----------------------------------------------------------------------- 11885DR PIR; D93303; HBCZP. 11886DR ProteinModelPortal; P68872; -. 11887DR SMR; P68872; 2-147. 11888DR PRIDE; P68872; -. 11889DR HOVERGEN; HBG009709; -. 11890DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. 11891DR GO; GO:0020037; F:heme binding; IEA:InterPro. 11892DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. 11893DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. 11894DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 11895DR InterPro; IPR000971; Globin. 11896DR InterPro; IPR009050; Globin-like. 11897DR InterPro; IPR012292; Globin_dom. 11898DR InterPro; IPR002337; Haemoglobin_b. 11899DR Pfam; PF00042; Globin; 1. 11900DR PRINTS; PR00814; BETAHAEM. 11901DR SUPFAM; SSF46458; Globin_like; 1. 11902DR PROSITE; PS01033; GLOBIN; 1. 11903PE 1: Evidence at protein level; 11904KW Direct protein sequencing; Heme; Iron; Metal-binding; 11905KW Oxygen transport; Transport. 11906FT INIT_MET 1 1 Removed. 11907FT CHAIN 2 147 Hemoglobin subunit beta. 11908FT /FTId=PRO_0000053056. 11909FT METAL 64 64 Iron (heme distal ligand). 11910FT METAL 93 93 Iron (heme proximal ligand). 11911SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; 11912 MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK 11913 VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG 11914 KEFTPPVQAA YQKVVAGVAN ALAHKYH 11915// 11916ID HBB_PANTR Reviewed; 147 AA. 11917AC P68873; P02023; Q13852; Q14481; Q14510; Q28799; Q9BX96; Q9UCP8; 11918AC Q9UCP9; 11919DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 11920DT 23-JAN-2007, sequence version 2. 11921DT 13-JUN-2012, entry version 67. 11922DE RecName: Full=Hemoglobin subunit beta; 11923DE AltName: Full=Beta-globin; 11924DE AltName: Full=Hemoglobin beta chain; 11925GN Name=HBB; 11926OS Pan troglodytes (Chimpanzee). 11927OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 11928OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 11929OC Catarrhini; Hominidae; Pan. 11930OX NCBI_TaxID=9598; 11931RN [1] 11932RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121. 11933RX MEDLINE=85210896; PubMed=3999143; DOI=10.1016/0022-2836(85)90024-5; 11934RA Savatier P., Trabuchet G., Faure C., Chebloune Y., Gouy M., 11935RA Verdier G., Nigon V.M.; 11936RT "Evolution of the primate beta-globin gene region. High rate of 11937RT variation in CpG dinucleotides and in short repeated sequences between 11938RT man and chimpanzee."; 11939RL J. Mol. Biol. 182:21-29(1985). 11940RN [2] 11941RP PROTEIN SEQUENCE OF 2-147. 11942RX MEDLINE=66071496; PubMed=5855051; 11943RA Rifkin D.B., Konigsberg W.; 11944RT "The characterization of the tryptic peptides from the hemoglobin of 11945RT the chimpanzee (Pan troglodytes)."; 11946RL Biochim. Biophys. Acta 104:457-461(1965). 11947CC -!- FUNCTION: Involved in oxygen transport from the lung to the 11948CC various peripheral tissues. 11949CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in 11950CC adult hemoglobin A (HbA). 11951CC -!- TISSUE SPECIFICITY: Red blood cells. 11952CC -!- SIMILARITY: Belongs to the globin family. 11953CC -!- SEQUENCE CAUTION: 11954CC Sequence=CAA26204.1; Type=Erroneous gene model prediction; 11955CC ----------------------------------------------------------------------- 11956CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 11957CC Distributed under the Creative Commons Attribution-NoDerivs License 11958CC ----------------------------------------------------------------------- 11959DR EMBL; X02345; CAA26204.1; ALT_SEQ; Genomic_DNA. 11960DR PIR; B93303; HBCZ. 11961DR RefSeq; XP_003312929.1; XM_003312881.1. 11962DR RefSeq; XP_508242.1; XM_508242.3. 11963DR ProteinModelPortal; P68873; -. 11964DR SMR; P68873; 2-147. 11965DR STRING; P68873; -. 11966DR PRIDE; P68873; -. 11967DR Ensembl; ENSPTRT00000006177; ENSPTRP00000005700; ENSPTRG00000040047. 11968DR GeneID; 450978; -. 11969DR KEGG; ptr:450978; -. 11970DR CTD; 3043; -. 11971DR eggNOG; NOG269316; -. 11972DR GeneTree; ENSGT00650000093060; -. 11973DR HOVERGEN; HBG009709; -. 11974DR KO; K13823; -. 11975DR OMA; DAVMNNP; -. 11976DR NextBio; 20833659; -. 11977DR GO; GO:0020037; F:heme binding; IEA:InterPro. 11978DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW. 11979DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. 11980DR InterPro; IPR000971; Globin. 11981DR InterPro; IPR009050; Globin-like. 11982DR InterPro; IPR012292; Globin_dom. 11983DR InterPro; IPR002337; Haemoglobin_b. 11984DR Pfam; PF00042; Globin; 1. 11985DR PRINTS; PR00814; BETAHAEM. 11986DR SUPFAM; SSF46458; Globin_like; 1. 11987DR PROSITE; PS01033; GLOBIN; 1. 11988PE 1: Evidence at protein level; 11989KW Complete proteome; Direct protein sequencing; Heme; Iron; 11990KW Metal-binding; Oxygen transport; Reference proteome; Transport. 11991FT INIT_MET 1 1 Removed. 11992FT CHAIN 2 147 Hemoglobin subunit beta. 11993FT /FTId=PRO_0000053060. 11994FT METAL 64 64 Iron (heme distal ligand). 11995FT METAL 93 93 Iron (heme proximal ligand). 11996SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; 11997 MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK 11998 VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG 11999 KEFTPPVQAA YQKVVAGVAN ALAHKYH 12000// 12001ID HD_TAKRU Reviewed; 3148 AA. 12002AC P51112; 12003DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 12004DT 01-OCT-1996, sequence version 1. 12005DT 16-MAY-2012, entry version 64. 12006DE RecName: Full=Huntingtin; 12007DE AltName: Full=Huntington disease protein homolog; 12008DE Short=HD protein homolog; 12009GN Name=htt; Synonyms=hd; 12010OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 12011OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 12012OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 12013OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 12014OC Tetradontoidea; Tetraodontidae; Takifugu. 12015OX NCBI_TaxID=31033; 12016RN [1] 12017RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12018RX MEDLINE=95375788; PubMed=7647794; DOI=10.1038/ng0595-67; 12019RA Baxendale S., Abdulla S., Elgar G., Buck D., Berks M., Micklem G., 12020RA Durbin R., Bates G., Brenner S., Beck S., Lehrach H.; 12021RT "Comparative sequence analysis of the human and pufferfish 12022RT Huntington's disease genes."; 12023RL Nat. Genet. 10:67-76(1995). 12024CC -!- FUNCTION: May play a role in microtubule-mediated transport or 12025CC vesicle function. 12026CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By 12027CC similarity). 12028CC -!- POLYMORPHISM: The poly-Gln region (four residues) does not appear 12029CC to be polymorphic, explaining the absence of a HD-like disorder. 12030CC -!- SIMILARITY: Belongs to the huntingtin family. 12031CC -!- SIMILARITY: Contains 10 HEAT repeats. 12032CC ----------------------------------------------------------------------- 12033CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 12034CC Distributed under the Creative Commons Attribution-NoDerivs License 12035CC ----------------------------------------------------------------------- 12036DR EMBL; X82939; CAA58112.1; -; Genomic_DNA. 12037DR ProteinModelPortal; P51112; -. 12038DR STRING; P51112; -. 12039DR PRIDE; P51112; -. 12040DR eggNOG; NOG82191; -. 12041DR GO; GO:0005737; C:cytoplasm; ISS:RefGenome. 12042DR GO; GO:0005634; C:nucleus; ISS:RefGenome. 12043DR GO; GO:0008134; F:transcription factor binding; ISS:RefGenome. 12044DR GO; GO:0048513; P:organ development; ISS:RefGenome. 12045DR Gene3D; G3DSA:1.25.10.10; ARM-like; 4. 12046DR InterPro; IPR011989; ARM-like. 12047DR InterPro; IPR016024; ARM-type_fold. 12048DR InterPro; IPR021133; HEAT_type_2. 12049DR InterPro; IPR000091; Huntingtin. 12050DR InterPro; IPR024613; Huntingtin_middle-repeat. 12051DR PANTHER; PTHR10170; Huntingtin; 1. 12052DR Pfam; PF12372; DUF3652; 1. 12053DR PRINTS; PR00375; HUNTINGTIN. 12054DR SUPFAM; SSF48371; ARM-type_fold; 1. 12055DR PROSITE; PS50077; HEAT_REPEAT; 1. 12056PE 3: Inferred from homology; 12057KW Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat. 12058FT CHAIN 1 3148 Huntingtin. 12059FT /FTId=PRO_0000083941. 12060FT REPEAT 149 186 HEAT 1. 12061FT REPEAT 191 228 HEAT 2. 12062FT REPEAT 760 797 HEAT 3. 12063FT REPEAT 861 898 HEAT 4. 12064FT REPEAT 1419 1456 HEAT 5. 12065FT MOTIF 2398 2407 Nuclear export signal (By similarity). 12066FT COMPBIAS 18 21 Poly-Gln. 12067FT COMPBIAS 679 682 Poly-Ala. 12068FT COMPBIAS 1104 1108 Poly-Ser. 12069SQ SEQUENCE 3148 AA; 348937 MW; D9358676B0345243 CRC64; 12070 MATMEKLMKA FESLKSFQQQ QGPPTAEEIV QRQKKEQATT KKDRVSHCLT ICENIVAQSL 12071 RTSPEFQKLL GIAMEMFLLC SDDSESDVRM VADECLNRII KALMDSNLPR LQLELYKEIK 12072 KNGASRSLRA ALWRFAELAH LIRPQKCRPY LVNLLPCLTR ITKRQEETIQ ETLAAAMPKI 12073 MAALGHFAND GEIKMLLKSF VANLKSSSPT IRRTAASSAV SVCQHSRRTS YFYTWLLNVL 12074 LGLLVPVDEE HHSHLILGVL LTLRYLMPLL QQQVNTISLK GSFGVMQKEA DVQPAPEQLL 12075 QVYELTLHYT QHWDHNVVTA ALELLQQTLR TPPPELLHVL ITAGSIQHAS VFRQDIESRA 12076 RSGSILELIA GGGSTCSPLL HRKHRGKMLS GEEDALEDDP EKTDVTTGYF TAVGADNSSA 12077 AQVDIITQQP RSSQHTIQPG DSVDLSASSE QGGRGGGASA SDTPESPNDE EDMLSRSSSC 12078 GANITPETVE DATPENPAQE GRPVGGSGAY DHSLPPSDSS QTTTEGPDSA VTPSDVAELV 12079 LDGSESQYSG MQIGTLQDEE DEGTATSSQE DPPDPFLRSA LALSKPHLFE SRGHNRQGSD 12080 SSVDRFIPKD EPPEPEPDNK MSRIKGAIGH YTDRGAEPVV HCVRLLSASF LLTGQKNGLT 12081 PDRDVRVSVK ALAVSCVGAA AALHPEAFFN SLYLEPLDGL RAEEQQYISD VLGFIDHGDP 12082 QIRGATAILC AAIIQAALSK MRYNIHSWLA SVQSKTGNPL SLVDLVPLLQ KALKDESSVT 12083 CKMACSAVRH CIMSLCGSTL SELGLRLVVD LFALKDSSYW LVRTELLETL AEMDFRLVNF 12084 LERKSEALHK GEHHYTGRLR LQERVLNDVV IQLLGDDDPR VRHVAASAVS RLVSRLFFDC 12085 DQGQADPVVA IARDQSSVYL QLLMHETQPP SQLTVSTITR TYRGFNLSNN VADVTVENNL 12086 SRVVTAVSHA FTSSTSRALT FGCCEALCLL AVHFPICTWT TGWHCGHISS QSSFSSRVGR 12087 SRGRTLSVSQ SGSTPASSTT SSAVDPERRT LTVGTANMVL SLLSSAWFPL DLSAHQDALL 12088 LCGNLLAAVA PKCLRNPWAG EDDSSSSSTN TSGGTHKMEE PWAALSDRAF VAMVEQLFSH 12089 LLKVLNICAH VLDDTPPGPP VKATLPSLTN TPSLSPIRRK GKDKDAVDSS SAPLSPKKGN 12090 EANTGRPTES TGSTAVHKST TLGSFYHLPP YLKLYDVLKA THANFKVMLD LHSNQEKFGS 12091 FLRAALDVLS QLLELATLND INKCVEEILG YLKSCFSREP TMATVCVQQL LKTLFGTNLA 12092 SQYEGFLSGP SRSQGKALRL GSSSLRPGLY HYCFMAPYTH FTQALADASL RNMVQAEHEQ 12093 DTSGWFDVMQ KTSNQLRSNI ANAARHRGDK NAIHNHIRLF EPLVIKALKQ YTTSTSVALQ 12094 RQVLDLLAQL VQLRVNYCLL DSDQVFIGFV LKQFEYIEVG QFRDSEAIIP NIFFFLVLLS 12095 YERYHSKQII SIPKIIQLCD GIMASGRKAV THAIPALQPI VHDLFVLRGS NKADAGKELE 12096 TQKEVVVSML LRLVQYHQVL EMFILVLQQC HKENEDKWKR LSRQIADVIL PMIAKQQMHL 12097 DSPEALGVLN TLFETVAPSS LRPVDMLLKS MFTTPVTMAS VATVQLWVSG ILAVLRVLVS 12098 QSTEDIVLSR IHELSLSPHL LSCHTIKRLQ QPNLSPSDQP AGDGQQNQEP NGEAQKSLPE 12099 ETFARFLIQL VGVLLDDISS RHVKVDITEQ QHTFYCQQLG TLLMCLIHVF KSGMFRRITV 12100 AASRLLKGES GSGHSGIEFY PLEGLNSMVH CLITTHPSLV LLWCQVLLII DYTNYSWWTE 12101 VHQTPKGHSL SCTKLLSPHS SGEGEEKPET RLAMINREIV RRGALILFCD YVCQNLHDSE 12102 HLTWLIVNHV RDLIDLSHEP PVQDFISAVH RNSAASGLFI QAIQSRCDNL NSPTMLKKTL 12103 QCLEGIHLSQ SGSLLMLYVD KLLSTPFRVL ARMVDTLACR RVEMLLAETL QNSVAQLPLE 12104 ELHRIQEYLQ TSGLAQRHQR FYSLLDRFRA TVSDTSSPST PVTSHPLDGD PPPAPELVIA 12105 DKEWYVALVK SQCCLHGDVS LLETTELLTK LPPADLLSVM SCKEFNLSLL CPCLSLGVQR 12106 LLRGQGSLLL ETALQVTLEQ LAGATGLLPV PHHSFIPTSH PQSHWKQLAE VYGDPGFYSR 12107 VLSLCRALSQ YLLTVKQLPS SLRIPSDKEH LITTFTCAAT EVVVWHLLQD QLPLSVDLQW 12108 ALSCLCLALQ QPCVWNKLST PEYNTHTCSL IYCLHHIILA VAVSPGDQLL HPERKKTKAL 12109 RHSDDEDQVD SVHDNHTLEW QACEIMAELV EGLQSVLSLG HHRNTAFPAF LTPTLRNIII 12110 SLSRLPLVNS HTRVPPLVWK LGWSPQPGGE FGTTLPEIPV DFLQEKDVFR EFLYRINTLG 12111 WSNRTQFEET WATLLGVLVT QPITMDQEEE TQQEEDLERT QLNVLAVQAI TSLVLSAMTL 12112 PTAGNPAVSC LEQQPRNKSL KALETRFGRK LAVIRGEVER EIQALVSKRD NVHTYHPYHA 12113 WDPVPSLSAA SPGTLISHEK LLLQINTERE LGNMDYKLGQ VSIHSVWLGN NITPLREEEW 12114 GEDEDDEADP PAPTSPPLSP INSRKHRAGV DIHSCSQFLL ELYSQWVIPG SPSNRKTPTI 12115 LISEVVRSLL AVSDLFTERN QFDMMFSTLM ELQKLHPPED EILNQYLVPA ICKAAAVLGM 12116 DKAIAEPVCR LLETTLRSTH LPSRMGALHG VLYVLECDLL DDTAKQLIPT VSEYLLSNLR 12117 AIAHCVNLHN QQHVLVMCAV AFYMMENYPL DVGTEFMAGI IQLCGVMVSA SEDSTPSIIY 12118 HCVLRGLERL LLSEQLSRVD GEALVKLSVD RVNMPSPHRA MAALGLMLTC MYTGKEKASP 12119 AARSAHSDPQ VPDSESIIVA MERVSVLFDR IRKGLPSEAR VVARILPQFL DDFFPPQDIM 12120 NKVIGEFLSN QQPYPQFMAT VVYKVFQTLH ATGQSSMVRD WVLLSLSNFT QRTPVAMAMW 12121 SLSCFFVSAS TSQWISALLP HVISRMGSSD VVDVNLFCLV AMDFYRHQID EELDRRAFQS 12122 VFETVASPGS PYFQLLACLQ SIHQDKSL 12123// 12124ID HIRA_TAKRU Reviewed; 1025 AA. 12125AC O42611; 12126DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. 12127DT 01-JAN-1998, sequence version 1. 12128DT 16-MAY-2012, entry version 79. 12129DE RecName: Full=Protein HIRA; 12130DE AltName: Full=TUP1-like enhancer of split protein 1; 12131GN Name=hira; Synonyms=tuple1; 12132OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 12133OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 12134OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 12135OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 12136OC Tetradontoidea; Tetraodontidae; Takifugu. 12137OX NCBI_TaxID=31033; 12138RN [1] 12139RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 12140RX MEDLINE=98201624; PubMed=9524281; DOI=10.1016/S0378-1119(98)00010-9; 12141RA Llevadot R., Estivill X., Scambler P., Pritchard M.; 12142RT "Isolation and genomic characterization of the TUPLE1/HIRA gene of the 12143RT pufferfish Fugu rubripes."; 12144RL Gene 208:279-283(1998). 12145CC -!- FUNCTION: Required for replication-independent chromatin assembly 12146CC and for the periodic repression of histone gene transcription 12147CC during the cell cycle (By similarity). 12148CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). 12149CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. 12150CC -!- SIMILARITY: Contains 9 WD repeats. 12151CC ----------------------------------------------------------------------- 12152CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 12153CC Distributed under the Creative Commons Attribution-NoDerivs License 12154CC ----------------------------------------------------------------------- 12155DR EMBL; U94325; AAC60370.1; -; Genomic_DNA. 12156DR EMBL; U94324; AAC60369.1; -; mRNA. 12157DR RefSeq; NP_001027852.1; NM_001032680.1. 12158DR UniGene; Tru.1844; -. 12159DR ProteinModelPortal; O42611; -. 12160DR STRING; O42611; -. 12161DR GeneID; 446054; -. 12162DR CTD; 7290; -. 12163DR eggNOG; COG2319; -. 12164DR InParanoid; O42611; -. 12165DR OrthoDB; EOG42NHZN; -. 12166DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 12167DR GO; GO:0003682; F:chromatin binding; IEA:InterPro. 12168DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. 12169DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. 12170DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 12171DR Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1. 12172DR InterPro; IPR011494; Hira. 12173DR InterPro; IPR019015; HIRA_B_motif. 12174DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. 12175DR InterPro; IPR001680; WD40_repeat. 12176DR InterPro; IPR019775; WD40_repeat_CS. 12177DR InterPro; IPR017986; WD40_repeat_dom. 12178DR Pfam; PF07569; Hira; 1. 12179DR Pfam; PF09453; HIRA_B; 1. 12180DR Pfam; PF00400; WD40; 5. 12181DR SMART; SM00320; WD40; 8. 12182DR SUPFAM; SSF50978; WD40_like; 1. 12183DR PROSITE; PS00678; WD_REPEATS_1; 1. 12184DR PROSITE; PS50082; WD_REPEATS_2; 3. 12185DR PROSITE; PS50294; WD_REPEATS_REGION; 1. 12186PE 2: Evidence at transcript level; 12187KW Chromatin regulator; Complete proteome; Nucleus; Reference proteome; 12188KW Repeat; Repressor; Transcription; Transcription regulation; WD repeat. 12189FT CHAIN 1 1025 Protein HIRA. 12190FT /FTId=PRO_0000051021. 12191FT REPEAT 11 53 WD 1. 12192FT REPEAT 68 107 WD 2. 12193FT REPEAT 129 168 WD 3. 12194FT REPEAT 172 211 WD 4. 12195FT REPEAT 220 263 WD 5. 12196FT REPEAT 266 322 WD 6. 12197FT REPEAT 326 367 WD 7. 12198FT REPEAT 737 778 WD 8. 12199FT REPEAT 779 817 WD 9. 12200SQ SEQUENCE 1025 AA; 111857 MW; A4212152D75B6A37 CRC64; 12201 MKLLKPSWVS HNGKPIFSVD IHPDGTKFAT GGQGEDSGKV MIWNMAPVLK EEDEKNENVP 12202 KMLCQMDNHL ACVNCVRWSN NGLYLASGGD DKLVMVWKRA ALIGPSTVFG SSNKLANVEQ 12203 WRCVTILRNH TGDVMDVSWS PHDVWLASCS VDNTIVIWNA RKFPEMVTCL RGHTGLVKGL 12204 TWDPVGKYIA SQADDHSLRV WRTVDWQMEA NITKPFSECG GTTHVLRLSW SPDGQYLVSA 12205 HAMNNSGPTA QIVERDGWRT NMDFVGHRKA VTVVKFNPKI FKKKQKNGGS PKPSCPYCCC 12206 AVGSKDRSLS VWLTSLKRPL VVIHDLFDKS IMDISWTLTG LGMLVCSMDG TVAYLDFSLD 12207 ELGDPLSEEE KNSIHQNIYG KSLAITNTEP QLSTTIIENP EMLKYQQERR NSTQANSGPG 12208 ATGSESATPK LNSVMNGESL EDIRKNLLKK QVETRTPDGR RRITPLCIAQ LDTGDFSPAL 12209 FNSAPILPSG SSMSNQLTSQ LSSDSSPGQA PPLGLRPSQD PMLISPPPSS AAKVLEDNKD 12210 GVKSCLLLTS ASKIEPMKAL DSRFTERSKA TPGATAAIAS STGLTPSERP KESTPMQKDV 12211 KSKEDTSSDS EDKMATINKN LAFNKRKPEL LMDGAEVVEK RKKGRPRKDK MAASIAQPLT 12212 QTTSPAEREP SRAAAAGAGA AAPTAAAALK LPTPSIKKAF TLQVSMDPSV VLEVENEVSV 12213 VAGSRLSQLR CSRDGRDWNT LLPSSVLTAA GSSDVVAVAS QDRMLSVFSS CGRRLLPAIQ 12214 LATPASALHC SAHFVMVLTS GATLSVWDVH KQKALVKNES LLTILSGAAV TVSQSMLTQQ 12215 GVPVVGLSNG KSYCFSLSLE TWTLIADTAD SLVQCADFRN CLPNQDAPMS SGPLAAMQGR 12216 NFNAGRLASR LSSTPHHLQQ SMTLAFLENQ LASALTLQSA QEYRYWLLIY ARFLVNEGSE 12217 YRLRELCKEL LGPVHKSATT SWEPTTLGLR KRDLLREVLP VVGENLRFQR LFTEYQDQLE 12218 LLRNK 12219// 12220ID IFNA2_HUMAN Reviewed; 188 AA. 12221AC P01563; P01564; Q14606; Q96KI6; 12222DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 12223DT 21-JUL-1986, sequence version 1. 12224DT 16-MAY-2012, entry version 128. 12225DE RecName: Full=Interferon alpha-2; 12226DE Short=IFN-alpha-2; 12227DE AltName: Full=Interferon alpha-A; 12228DE Short=LeIF A; 12229DE Flags: Precursor; 12230GN Name=IFNA2; 12231OS Homo sapiens (Human). 12232OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 12233OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 12234OC Catarrhini; Hominidae; Homo. 12235OX NCBI_TaxID=9606; 12236RN [1] 12237RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 12238RX MEDLINE=81052322; PubMed=6159538; DOI=10.1038/287411a0; 12239RA Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G., 12240RA Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R., 12241RA Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M., 12242RA Familletti P.C., Pestka S.; 12243RT "Human leukocyte interferon produced by E. coli is biologically 12244RT active."; 12245RL Nature 287:411-416(1980). 12246RN [2] 12247RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 12248RX MEDLINE=81148795; PubMed=6163083; DOI=10.1038/290020a0; 12249RA Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M., 12250RA McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.; 12251RT "The structure of eight distinct cloned human leukocyte interferon 12252RT cDNAs."; 12253RL Nature 290:20-26(1981). 12254RN [3] 12255RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 12256RX MEDLINE=82060261; PubMed=6170983; DOI=10.1073/pnas.78.9.5435; 12257RA Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.; 12258RT "DNA sequence of a major human leukocyte interferon gene."; 12259RL Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981). 12260RN [4] 12261RP NUCLEOTIDE SEQUENCE [MRNA]. 12262RC TISSUE=Bone marrow tumor; 12263RX MEDLINE=86069501; PubMed=3906813; 12264RA Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.; 12265RT "Cloning of human leukocyte interferon cDNA and a strategy for its 12266RT production in E. coli."; 12267RL Rev. Latinoam. Microbiol. 27:141-150(1985). 12268RN [5] 12269RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12270RC TISSUE=Placenta; 12271RX MEDLINE=98357449; PubMed=9694076; 12272RA Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P., 12273RA Mannoni P., Chabannon C.; 12274RT "A defective retroviral vector encoding human interferon alpha 2 can 12275RT transduce human leukemic cell lines."; 12276RL Cancer Gene Ther. 5:247-256(1998). 12277RN [6] 12278RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188. 12279RX MEDLINE=81015442; PubMed=6158094; DOI=10.1126/science.6158094; 12280RA Streuli M., Nagata S., Weissmann C.; 12281RT "At least three human type alpha interferons: structure of alpha 2."; 12282RL Science 209:1343-1347(1980). 12283RN [7] 12284RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-188. 12285RX MEDLINE=83299241; PubMed=6310510; DOI=10.1093/nar/11.16.5661; 12286RA Weber H., Weissmann C.; 12287RT "Formation of genes coding for hybrid proteins by recombination 12288RT between related, cloned genes in E. coli."; 12289RL Nucleic Acids Res. 11:5661-5669(1983). 12290RN [8] 12291RP PROTEIN SEQUENCE OF 24-112 AND 136-188. 12292RX MEDLINE=81052321; PubMed=6159537; DOI=10.1038/287408a0; 12293RA Allen G., Fantes K.H.; 12294RT "A family of structural genes for human lymphoblastoid (leukocyte- 12295RT type) interferon."; 12296RL Nature 287:408-411(1980). 12297RN [9] 12298RP PROTEIN SEQUENCE OF 24-58. 12299RX MEDLINE=98087498; PubMed=9425112; 12300RA Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.; 12301RT "Identification of nine interferon-alpha subtypes produced by Sendai 12302RT virus-induced human peripheral blood leucocytes."; 12303RL Biochem. J. 329:295-302(1998). 12304RN [10] 12305RP DISULFIDE BONDS. 12306RX MEDLINE=81123083; PubMed=6162107; DOI=10.1038/289606a0; 12307RA Wetzel R.; 12308RT "Assignment of the disulphide bonds of leukocyte interferon."; 12309RL Nature 289:606-607(1981). 12310RN [11] 12311RP GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C. 12312RX MEDLINE=91264809; PubMed=2049076; 12313RA Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.; 12314RT "Natural human interferon-alpha 2 is O-glycosylated."; 12315RL Biochem. J. 276:511-518(1991). 12316RN [12] 12317RP POLYMORPHISM. 12318RX MEDLINE=95353982; PubMed=7627809; DOI=10.1089/jir.1995.15.341; 12319RA Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S., 12320RA Liao M.-J., Testa D.; 12321RT "Interferon-alpha 2 variants in the human genome."; 12322RL J. Interferon Cytokine Res. 15:341-349(1995). 12323RN [13] 12324RP 3D-STRUCTURE MODELING. 12325RX MEDLINE=94052087; PubMed=8234245; DOI=10.1002/prot.340170109; 12326RA Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A., 12327RA Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.; 12328RT "A homology model of human interferon alpha-2."; 12329RL Proteins 17:62-74(1993). 12330RN [14] 12331RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). 12332RX MEDLINE=97148339; PubMed=8994971; DOI=10.1016/S0969-2126(96)00152-9; 12333RA Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P., 12334RA Nagabhushan T.L., Walter M.R.; 12335RT "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray 12336RT crystallography."; 12337RL Structure 4:1453-1463(1996). 12338RN [15] 12339RP STRUCTURE BY NMR. 12340RX MEDLINE=98118493; PubMed=9417943; DOI=10.1006/jmbi.1997.1396; 12341RA Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.; 12342RT "The three-dimensional high resolution structure of human interferon 12343RT alpha-2a determined by heteronuclear NMR spectroscopy in solution."; 12344RL J. Mol. Biol. 274:661-675(1997). 12345RN [16] 12346RP STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND 12347RP DISULFIDE BONDS. 12348RX PubMed=17001036; DOI=10.1110/ps.062283006; 12349RA Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.; 12350RT "Determination of the human type I interferon receptor binding site on 12351RT human interferon-alpha2 by cross saturation and an NMR-based model of 12352RT the complex."; 12353RL Protein Sci. 15:2656-2668(2006). 12354RN [17] 12355RP STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND 12356RP DISULFIDE BONDS. 12357RX PubMed=20496919; DOI=10.1021/bi100041f; 12358RA Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y., 12359RA Yang D., Anglister J.; 12360RT "Intermolecular interactions in a 44 kDa interferon-receptor complex 12361RT detected by asymmetric reverse-protonation and two-dimensional 12362RT NOESY."; 12363RL Biochemistry 49:5117-5133(2010). 12364RN [18] 12365RP VARIANT [LARGE SCALE ANALYSIS] LEU-177. 12366RX PubMed=16959974; DOI=10.1126/science.1133427; 12367RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., 12368RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., 12369RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., 12370RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., 12371RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., 12372RA Vogelstein B., Kinzler K.W., Velculescu V.E.; 12373RT "The consensus coding sequences of human breast and colorectal 12374RT cancers."; 12375RL Science 314:268-274(2006). 12376CC -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral 12377CC activities. 12378CC -!- SUBUNIT: Interacts with IFNAR2. 12379CC -!- SUBCELLULAR LOCATION: Secreted. 12380CC -!- POLYMORPHISM: Three forms exist; alpha-2a (shown here), alpha-2b 12381CC and alpha-2c. 12382CC -!- PHARMACEUTICAL: Available under the names Roferon-A (Roche) or 12383CC Intron-A (Schering-Plough). Used as an anticancer drug for its 12384CC antiproliferative activity. 12385CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. 12386CC ----------------------------------------------------------------------- 12387CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 12388CC Distributed under the Creative Commons Attribution-NoDerivs License 12389CC ----------------------------------------------------------------------- 12390DR EMBL; J00207; AAB59402.1; -; Genomic_DNA. 12391DR EMBL; V00544; CAA23805.1; -; mRNA. 12392DR EMBL; V00548; CAA23809.1; -; mRNA. 12393DR EMBL; V00549; CAA23810.1; -; mRNA. 12394DR EMBL; Y11834; CAA72532.1; -; Genomic_DNA. 12395DR EMBL; M54886; AAA59181.1; -; mRNA. 12396DR EMBL; M29883; AAA52715.1; -; Genomic_DNA. 12397DR IPI; IPI00307184; -. 12398DR PIR; A93234; IVHUA2. 12399DR PIR; I78570; I78570. 12400DR RefSeq; NP_000596.2; NM_000605.3. 12401DR UniGene; Hs.211575; -. 12402DR PDB; 1ITF; NMR; -; A=24-188. 12403DR PDB; 1RH2; X-ray; 2.90 A; A/B/C/D/E/F=24-188. 12404DR PDB; 2HIE; Model; -; A=24-188. 12405DR PDB; 2HYM; NMR; -; B=24-188. 12406DR PDB; 2KZ1; NMR; -; A=24-188. 12407DR PDB; 2LAG; NMR; -; A=24-188. 12408DR PDB; 3S9D; X-ray; 2.00 A; A/C=24-188. 12409DR PDB; 3SE3; X-ray; 4.00 A; B=24-188. 12410DR PDBsum; 1ITF; -. 12411DR PDBsum; 1RH2; -. 12412DR PDBsum; 2HIE; -. 12413DR PDBsum; 2HYM; -. 12414DR PDBsum; 2KZ1; -. 12415DR PDBsum; 2LAG; -. 12416DR PDBsum; 3S9D; -. 12417DR PDBsum; 3SE3; -. 12418DR ProteinModelPortal; P01563; -. 12419DR SMR; P01563; 24-188. 12420DR DIP; DIP-3784N; -. 12421DR DIP; DIP-481N; -. 12422DR IntAct; P01563; 1. 12423DR STRING; P01563; -. 12424DR Allergome; 9876; Hom s IFN alpha. 12425DR GlycoSuiteDB; P01563; -. 12426DR DMDM; 124449; -. 12427DR PRIDE; P01563; -. 12428DR DNASU; 3440; -. 12429DR Ensembl; ENST00000380206; ENSP00000369554; ENSG00000188379. 12430DR GeneID; 3440; -. 12431DR KEGG; hsa:3440; -. 12432DR CTD; 3440; -. 12433DR GeneCards; GC09M021374; -. 12434DR H-InvDB; HIX0034810; -. 12435DR HGNC; HGNC:5423; IFNA2. 12436DR MIM; 147562; gene. 12437DR neXtProt; NX_P01563; -. 12438DR PharmGKB; PA29662; -. 12439DR eggNOG; NOG246451; -. 12440DR HOGENOM; HOG000230500; -. 12441DR HOVERGEN; HBG052086; -. 12442DR InParanoid; P01563; -. 12443DR KO; K05414; -. 12444DR OrthoDB; EOG4KH2W5; -. 12445DR Pathway_Interaction_DB; cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells. 12446DR Reactome; REACT_604; Hemostasis. 12447DR Reactome; REACT_6900; Immune System. 12448DR DrugBank; DB00034; Interferon Alfa-2a, Recombinant. 12449DR DrugBank; DB00105; Interferon Alfa-2b, Recombinant. 12450DR DrugBank; DB00011; Interferon alfa-n1. 12451DR DrugBank; DB00008; Peginterferon alfa-2a. 12452DR DrugBank; DB00022; Peginterferon alfa-2b. 12453DR EvolutionaryTrace; P01563; -. 12454DR NextBio; 13556; -. 12455DR ArrayExpress; P01563; -. 12456DR Bgee; P01563; -. 12457DR CleanEx; HS_IFNA2; -. 12458DR Genevestigator; P01563; -. 12459DR GermOnline; ENSG00000188379; Homo sapiens. 12460DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. 12461DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW. 12462DR GO; GO:0005132; F:interferon-alpha/beta receptor binding; TAS:ProtInc. 12463DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. 12464DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. 12465DR GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc. 12466DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. 12467DR GO; GO:2000666; P:negative regulation of interleukin-13 secretion; IDA:UniProtKB. 12468DR GO; GO:2000663; P:negative regulation of interleukin-5 secretion; IDA:UniProtKB. 12469DR GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:UniProtKB. 12470DR GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IDA:UniProtKB. 12471DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB. 12472DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome. 12473DR GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW. 12474DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome. 12475DR Gene3D; G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1. 12476DR InterPro; IPR009079; 4_helix_cytokine-like_core. 12477DR InterPro; IPR012351; 4_helix_cytokine_core. 12478DR InterPro; IPR000471; Interferon_alpha/beta/delta. 12479DR PANTHER; PTHR11691; Interferon_abd; 1. 12480DR Pfam; PF00143; Interferon; 1. 12481DR PRINTS; PR00266; INTERFERONAB. 12482DR SMART; SM00076; IFabd; 1. 12483DR SUPFAM; SSF47266; 4_helix_cytokine; 1. 12484DR PROSITE; PS00252; INTERFERON_A_B_D; 1. 12485PE 1: Evidence at protein level; 12486KW 3D-structure; Antiviral defense; Complete proteome; Cytokine; 12487KW Direct protein sequencing; Disulfide bond; Glycoprotein; 12488KW Pharmaceutical; Polymorphism; Reference proteome; Secreted; Signal. 12489FT SIGNAL 1 23 12490FT CHAIN 24 188 Interferon alpha-2. 12491FT /FTId=PRO_0000016360. 12492FT CARBOHYD 129 129 O-linked (GalNAc...). 12493FT /FTId=CAR_000049. 12494FT DISULFID 24 121 12495FT DISULFID 52 161 12496FT VARIANT 6 6 A -> D (in dbSNP:rs35971916). 12497FT /FTId=VAR_055972. 12498FT VARIANT 46 46 K -> R (in alpha-2B and alpha-2C; 12499FT dbSNP:rs1061959). 12500FT /FTId=VAR_004012. 12501FT VARIANT 57 57 H -> R (in alpha-2C). 12502FT /FTId=VAR_013001. 12503FT VARIANT 177 177 S -> L (in a breast cancer sample; 12504FT somatic mutation). 12505FT /FTId=VAR_036329. 12506FT HELIX 33 44 12507FT TURN 49 54 12508FT HELIX 63 66 12509FT STRAND 67 69 12510FT STRAND 71 75 12511FT HELIX 76 91 12512FT HELIX 93 98 12513FT HELIX 101 123 12514FT HELIX 134 155 12515FT HELIX 160 178 12516FT TURN 179 182 12517SQ SEQUENCE 188 AA; 21550 MW; 101DD21D394CBF97 CRC64; 12518 MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG 12519 FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA 12520 CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL 12521 QESLRSKE 12522// 12523ID LACI_ECOLI Reviewed; 360 AA. 12524AC P03023; O09196; P71309; Q2MC79; Q47338; 12525DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 12526DT 19-JUL-2003, sequence version 3. 12527DT 13-JUN-2012, entry version 136. 12528DE RecName: Full=Lactose operon repressor; 12529GN Name=lacI; OrderedLocusNames=b0345, JW0336; 12530OS Escherichia coli (strain K12). 12531OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 12532OC Enterobacteriaceae; Escherichia. 12533OX NCBI_TaxID=83333; 12534RN [1] 12535RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12536RX MEDLINE=78246991; PubMed=355891; DOI=10.1038/274765a0; 12537RA Farabaugh P.J.; 12538RT "Sequence of the lacI gene."; 12539RL Nature 274:765-769(1978). 12540RN [2] 12541RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12542RA Chen J., Matthews K.K.S.M.; 12543RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases. 12544RN [3] 12545RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12546RA Marsh S.; 12547RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 12548RN [4] 12549RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12550RC STRAIN=K12 / MG1655 / ATCC 47076; 12551RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., 12552RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., 12553RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; 12554RT "Sequence of minutes 4-25 of Escherichia coli."; 12555RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 12556RN [5] 12557RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12558RC STRAIN=K12 / MG1655 / ATCC 47076; 12559RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; 12560RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., 12561RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., 12562RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., 12563RA Mau B., Shao Y.; 12564RT "The complete genome sequence of Escherichia coli K-12."; 12565RL Science 277:1453-1474(1997). 12566RN [6] 12567RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12568RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 12569RX PubMed=16738553; DOI=10.1038/msb4100049; 12570RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., 12571RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; 12572RT "Highly accurate genome sequences of Escherichia coli K-12 strains 12573RT MG1655 and W3110."; 12574RL Mol. Syst. Biol. 2:E1-E5(2006). 12575RN [7] 12576RP PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360. 12577RX MEDLINE=76091932; PubMed=1107032; 12578RX DOI=10.1111/j.1432-1033.1975.tb02477.x; 12579RA Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.; 12580RT "Amino-acid sequence of lac repressor from Escherichia coli. 12581RT Isolation, sequence analysis and sequence assembly of tryptic peptides 12582RT and cyanogen-bromide fragments."; 12583RL Eur. J. Biochem. 59:491-509(1975). 12584RN [8] 12585RP PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347. 12586RX MEDLINE=73143730; PubMed=4571224; 12587RA Platt T., Files J.G., Weber K.; 12588RT "Lac repressor. Specific proteolytic destruction of the NH 2 -terminal 12589RT region and loss of the deoxyribonucleic acid-binding activity."; 12590RL J. Biol. Chem. 248:110-121(1973). 12591RN [9] 12592RP PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86. 12593RX MEDLINE=74126378; PubMed=4594037; DOI=10.1073/pnas.70.11.3165; 12594RA Ganem D., Miller J.H., Files J.G., Platt T., Weber K.; 12595RT "Reinitiation of a lac repressor fragment at a condon other than 12596RT AUG."; 12597RL Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973). 12598RN [10] 12599RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60. 12600RX MEDLINE=88230449; PubMed=3286877; DOI=10.1016/0022-2836(88)90237-9; 12601RA Gordon A.J.E., Burns P.A., Fix D.F., Yatagai F., Allen F.L., 12602RA Horsfall M.J., Halliday J.A., Gray J., Bernelot-Moens C., 12603RA Glickman B.W.; 12604RT "Missense mutation in the lacI gene of Escherichia coli. Inferences on 12605RT the structure of the repressor protein."; 12606RL J. Mol. Biol. 200:239-251(1988). 12607RN [11] 12608RP PROTEIN SEQUENCE OF 1-35. 12609RX MEDLINE=96087076; PubMed=7498473; DOI=10.1016/0014-5793(95)01153-6; 12610RA Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.; 12611RT "Mechanism of Lac repressor switch-off: orientation of the Lac 12612RT repressor DNA-binding domain is reversed upon inducer binding."; 12613RL FEBS Lett. 375:27-30(1995). 12614RN [12] 12615RP MUTAGENESIS. 12616RX MEDLINE=90183956; PubMed=2178920; 12617RA Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B., 12618RA Mueller-Hill B.; 12619RT "Mutant lac repressors with new specificities hint at rules for 12620RT protein-DNA recognition."; 12621RL EMBO J. 9:615-621(1990). 12622RN [13] 12623RP MUTAGENESIS. 12624RX MEDLINE=94322386; PubMed=8046748; DOI=10.1006/jmbi.1994.1458; 12625RA Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.; 12626RT "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered 12627RT Escherichia coli lac repressors reveals essential and non-essential 12628RT residues, as well as 'spacers' which do not require a specific 12629RT sequence."; 12630RL J. Mol. Biol. 240:421-433(1994). 12631RN [14] 12632RP 3D-STRUCTURE MODELING. 12633RX MEDLINE=91249837; PubMed=2040302; 12634RX DOI=10.1111/j.1432-1033.1991.tb16030.x; 12635RA Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B., 12636RA Mueller-Hill B.; 12637RT "A model of the lac repressor-operator complex based on physical and 12638RT genetic data."; 12639RL Eur. J. Biochem. 198:411-419(1991). 12640RN [15] 12641RP 3D-STRUCTURE MODELING OF 1-56. 12642RX MEDLINE=92020210; PubMed=1923807; DOI=10.1093/nar/19.19.5233; 12643RA Shin J.A., Ebright R.H., Dervan P.B.; 12644RT "Orientation of the Lac repressor DNA binding domain in complex with 12645RT the left lac operator half site characterized by affinity cleaving."; 12646RL Nucleic Acids Res. 19:5233-5236(1991). 12647RN [16] 12648RP STRUCTURE BY NMR. 12649RX MEDLINE=89113344; PubMed=3064080; 12650RA Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H., 12651RA Kaptein R.; 12652RT "The interaction of lac repressor headpiece with its operator: an NMR 12653RT view."; 12654RL Protein Seq. Data Anal. 1:487-498(1988). 12655RN [17] 12656RP STRUCTURE BY NMR. 12657RX MEDLINE=89302886; PubMed=2742823; DOI=10.1021/bi00433a037; 12658RA Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H., 12659RA Kaptein R., Buck F., Fera B., Rueterjans H.; 12660RT "H NMR study of a complex between the lac repressor headpiece and a 22 12661RT base pair symmetric lac operator."; 12662RL Biochemistry 28:2985-2991(1989). 12663RN [18] 12664RP STRUCTURE BY NMR OF 1-56. 12665RX MEDLINE=96275660; PubMed=8683581; DOI=10.1006/jmbi.1996.0356; 12666RA Slijper M., Bonvin A.M., Boelens R., Kaptein R.; 12667RT "Refined structure of lac repressor headpiece (1-56) determined by 12668RT relaxation matrix calculations from 2D and 3D NOE data: change of 12669RT tertiary structure upon binding to the lac operator."; 12670RL J. Mol. Biol. 259:761-773(1996). 12671RN [19] 12672RP STRUCTURE BY NMR OF 1-62. 12673RX MEDLINE=20113476; PubMed=10647179; DOI=10.1016/S0969-2126(00)88339-2; 12674RA Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R., 12675RA Kaptein R.; 12676RT "The solution structure of Lac repressor headpiece 62 complexed to a 12677RT symmetrical lac operator."; 12678RL Structure 7:1483-1492(1999). 12679RN [20] 12680RP X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS). 12681RX MEDLINE=96239623; PubMed=8638105; DOI=10.1126/science.271.5253.1247; 12682RA Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C., 12683RA Schumacher M.A., Brennan R.G., Lu P.; 12684RT "Crystal structure of the lactose operon repressor and its complexes 12685RT with DNA and inducer."; 12686RL Science 271:1247-1254(1996). 12687CC -!- FUNCTION: Repressor of the lactose operon. Binds allolactose as an 12688CC inducer. 12689CC -!- SUBUNIT: Homotetramer. 12690CC -!- MISCELLANEOUS: Removing residues 1-59 results in loss of DNA- 12691CC binding activity but retains tetrameric structure and inducer- 12692CC binding activity. Deleting residues 340-360 results in loss of 12693CC tetramer formation, but retains dimer formation, inducer-binding 12694CC activity, and DNA-binding activity (if residues 1-59 are present). 12695CC -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain. 12696CC -!- SEQUENCE CAUTION: 12697CC Sequence=AAB18069.1; Type=Erroneous initiation; 12698CC Sequence=AAB47270.1; Type=Erroneous initiation; 12699CC ----------------------------------------------------------------------- 12700CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 12701CC Distributed under the Creative Commons Attribution-NoDerivs License 12702CC ----------------------------------------------------------------------- 12703DR EMBL; V00294; CAA23569.1; -; Genomic_DNA. 12704DR EMBL; X58469; CAA41383.1; -; Genomic_DNA. 12705DR EMBL; U86347; AAB47270.1; ALT_INIT; Genomic_DNA. 12706DR EMBL; J01636; AAA24052.1; -; Genomic_DNA. 12707DR EMBL; U72488; AAB36549.1; -; Genomic_DNA. 12708DR EMBL; U78872; AAB37348.1; -; Genomic_DNA. 12709DR EMBL; U78873; AAB37351.1; -; Genomic_DNA. 12710DR EMBL; U78874; AAB37354.1; -; Genomic_DNA. 12711DR EMBL; U73857; AAB18069.1; ALT_INIT; Genomic_DNA. 12712DR EMBL; U00096; AAC73448.1; -; Genomic_DNA. 12713DR EMBL; AP009048; BAE76127.1; -; Genomic_DNA. 12714DR PIR; A93198; RPECL. 12715DR RefSeq; NP_414879.3; NC_000913.2. 12716DR PDB; 1CJG; NMR; -; A/B=1-62. 12717DR PDB; 1EFA; X-ray; 2.60 A; A/B/C=1-333. 12718DR PDB; 1JWL; X-ray; 4.00 A; A/B/C=1-333. 12719DR PDB; 1JYE; X-ray; 1.70 A; A=1-349. 12720DR PDB; 1JYF; X-ray; 3.00 A; A=1-349. 12721DR PDB; 1L1M; NMR; -; A/B=1-62. 12722DR PDB; 1LBG; X-ray; 4.80 A; A/B/C/D=1-360. 12723DR PDB; 1LBH; X-ray; 3.20 A; A/B/C/D=1-360. 12724DR PDB; 1LBI; X-ray; 2.70 A; A/B/C/D=1-360. 12725DR PDB; 1LCC; NMR; -; A=1-51. 12726DR PDB; 1LCD; NMR; -; A=1-51. 12727DR PDB; 1LQC; NMR; -; A=1-56. 12728DR PDB; 1LTP; Model; -; L=62-323. 12729DR PDB; 1OSL; NMR; -; A/B=1-62. 12730DR PDB; 1TLF; X-ray; 2.60 A; A/B/C/D=60-360. 12731DR PDB; 1Z04; Model; -; A/B/C/D=1-357. 12732DR PDB; 2BJC; NMR; -; A/B=1-62. 12733DR PDB; 2KEI; NMR; -; A/B=1-62. 12734DR PDB; 2KEJ; NMR; -; A/B=1-62. 12735DR PDB; 2KEK; NMR; -; A/B=1-62. 12736DR PDB; 2P9H; X-ray; 2.00 A; A/B=62-330. 12737DR PDB; 2PAF; X-ray; 3.50 A; A/B=62-330. 12738DR PDB; 2PE5; X-ray; 3.50 A; A/B/C=2-331. 12739DR PDB; 3EDC; X-ray; 2.10 A; A/B/C/D=1-360. 12740DR PDBsum; 1CJG; -. 12741DR PDBsum; 1EFA; -. 12742DR PDBsum; 1JWL; -. 12743DR PDBsum; 1JYE; -. 12744DR PDBsum; 1JYF; -. 12745DR PDBsum; 1L1M; -. 12746DR PDBsum; 1LBG; -. 12747DR PDBsum; 1LBH; -. 12748DR PDBsum; 1LBI; -. 12749DR PDBsum; 1LCC; -. 12750DR PDBsum; 1LCD; -. 12751DR PDBsum; 1LQC; -. 12752DR PDBsum; 1LTP; -. 12753DR PDBsum; 1OSL; -. 12754DR PDBsum; 1TLF; -. 12755DR PDBsum; 1Z04; -. 12756DR PDBsum; 2BJC; -. 12757DR PDBsum; 2KEI; -. 12758DR PDBsum; 2KEJ; -. 12759DR PDBsum; 2KEK; -. 12760DR PDBsum; 2P9H; -. 12761DR PDBsum; 2PAF; -. 12762DR PDBsum; 2PE5; -. 12763DR PDBsum; 3EDC; -. 12764DR DisProt; DP00433; -. 12765DR ProteinModelPortal; P03023; -. 12766DR SMR; P03023; 1-360. 12767DR DIP; DIP-10079N; -. 12768DR IntAct; P03023; 5. 12769DR ECO2DBASE; H039.0; 6TH EDITION. 12770DR EnsemblBacteria; EBESCT00000002264; EBESCP00000002264; EBESCG00000001853. 12771DR EnsemblBacteria; EBESCT00000002265; EBESCP00000002265; EBESCG00000001853. 12772DR EnsemblBacteria; EBESCT00000014841; EBESCP00000014132; EBESCG00000013901. 12773DR GeneID; 945007; -. 12774DR GenomeReviews; AP009048_GR; JW0336. 12775DR GenomeReviews; U00096_GR; b0345. 12776DR KEGG; eco:b0345; -. 12777DR PATRIC; 32115823; VBIEscCol129921_0353. 12778DR EchoBASE; EB0520; -. 12779DR EcoGene; EG10525; lacI. 12780DR eggNOG; COG1609; -. 12781DR HOGENOM; HOG000220179; -. 12782DR OMA; DIVPTAM; -. 12783DR ProtClustDB; PRK09526; -. 12784DR BioCyc; EcoCyc:PD00763; -. 12785DR EvolutionaryTrace; P03023; -. 12786DR Genevestigator; P03023; -. 12787DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. 12788DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 12789DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. 12790DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 12791DR Gene3D; G3DSA:1.10.260.40; G3DSA:1.10.260.40; 1. 12792DR InterPro; IPR010982; Lambda_DNA-bd_dom. 12793DR InterPro; IPR000843; Tscrpt_reg_HTH_LacI. 12794DR Pfam; PF00356; LacI; 1. 12795DR PRINTS; PR00036; HTHLACI. 12796DR SMART; SM00354; HTH_LACI; 1. 12797DR SUPFAM; SSF47413; Lambda_like_DNA; 1. 12798DR PROSITE; PS00356; HTH_LACI_1; 1. 12799DR PROSITE; PS50932; HTH_LACI_2; 1. 12800PE 1: Evidence at protein level; 12801KW 3D-structure; Complete proteome; Direct protein sequencing; 12802KW DNA-binding; Reference proteome; Repressor; Transcription; 12803KW Transcription regulation. 12804FT CHAIN 1 360 Lactose operon repressor. 12805FT /FTId=PRO_0000107963. 12806FT DOMAIN 1 58 HTH lacI-type. 12807FT DNA_BIND 6 25 H-T-H motif. 12808FT VARIANT 282 282 Y -> D (in T41 mutant). 12809FT MUTAGEN 17 17 Y->H: Broadening of specificity. 12810FT MUTAGEN 22 22 R->N: Recognizes an operator variant. 12811FT CONFLICT 286 286 L -> S (in Ref. 1, 4 and 7). 12812FT HELIX 6 11 12813FT TURN 12 14 12814FT HELIX 17 24 12815FT HELIX 33 45 12816FT HELIX 51 56 12817FT STRAND 63 69 12818FT HELIX 74 89 12819FT STRAND 93 98 12820FT STRAND 101 103 12821FT HELIX 104 115 12822FT TURN 116 118 12823FT STRAND 122 126 12824FT HELIX 130 139 12825FT TURN 140 142 12826FT STRAND 145 150 12827FT STRAND 154 156 12828FT STRAND 158 161 12829FT HELIX 163 177 12830FT STRAND 181 186 12831FT HELIX 192 207 12832FT STRAND 213 217 12833FT HELIX 222 234 12834FT STRAND 240 246 12835FT HELIX 247 259 12836FT TURN 265 267 12837FT STRAND 268 271 12838FT HELIX 277 281 12839FT STRAND 282 284 12840FT STRAND 287 290 12841FT HELIX 293 308 12842FT STRAND 314 319 12843FT STRAND 322 324 12844FT STRAND 334 338 12845FT HELIX 343 353 12846FT HELIX 354 356 12847SQ SEQUENCE 360 AA; 38590 MW; 347A8DEE92D736CB CRC64; 12848 MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ 12849 SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS 12850 GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ 12851 QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT 12852 AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS 12853 VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ 12854// 12855ID LACY_ECOLI Reviewed; 417 AA. 12856AC P02920; Q2MC81; 12857DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. 12858DT 21-JUL-1986, sequence version 1. 12859DT 16-MAY-2012, entry version 124. 12860DE RecName: Full=Lactose permease; 12861DE AltName: Full=Lactose-proton symport; 12862GN Name=lacY; OrderedLocusNames=b0343, JW0334; 12863OS Escherichia coli (strain K12). 12864OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 12865OC Enterobacteriaceae; Escherichia. 12866OX NCBI_TaxID=83333; 12867RN [1] 12868RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12869RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; 12870RA Buechel D.E., Gronenborn B., Mueller-Hill B.; 12871RT "Sequence of the lactose permease gene."; 12872RL Nature 283:541-545(1980). 12873RN [2] 12874RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 12875RC STRAIN=K12; 12876RA Pastore J.C., Larigan J.D., Consler T.G., Kaback H.R.; 12877RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases. 12878RN [3] 12879RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12880RC STRAIN=K12 / MG1655 / ATCC 47076; 12881RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., 12882RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., 12883RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; 12884RT "Sequence of minutes 4-25 of Escherichia coli."; 12885RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 12886RN [4] 12887RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12888RC STRAIN=K12 / MG1655 / ATCC 47076; 12889RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; 12890RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., 12891RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., 12892RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., 12893RA Mau B., Shao Y.; 12894RT "The complete genome sequence of Escherichia coli K-12."; 12895RL Science 277:1453-1474(1997). 12896RN [5] 12897RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 12898RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 12899RX PubMed=16738553; DOI=10.1038/msb4100049; 12900RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., 12901RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; 12902RT "Highly accurate genome sequences of Escherichia coli K-12 strains 12903RT MG1655 and W3110."; 12904RL Mol. Syst. Biol. 2:E1-E5(2006). 12905RN [6] 12906RP TOPOLOGY. 12907RX PubMed=16453726; 12908RA von Heijne G.; 12909RT "The distribution of positively charged residues in bacterial inner 12910RT membrane proteins correlates with the trans-membrane topology."; 12911RL EMBO J. 5:3021-3027(1986). 12912RN [7] 12913RP TOPOLOGY. 12914RX MEDLINE=90311318; PubMed=2164211; DOI=10.1073/pnas.87.13.4937; 12915RA Calamia J., Manoil C.; 12916RT "lac permease of Escherichia coli: topology and sequence elements 12917RT promoting membrane insertion."; 12918RL Proc. Natl. Acad. Sci. U.S.A. 87:4937-4941(1990). 12919RN [8] 12920RP TOPOLOGY. 12921RX MEDLINE=96066665; PubMed=7578103; DOI=10.1021/bi00045a036; 12922RA Ujwal M.L., Jung H., Bibi E., Manoil C., Altenbach C., Hubbell W.L., 12923RA Kaback H.R.; 12924RT "Membrane topology of helices VII and XI in the lactose permease of 12925RT Escherichia coli studied by lacY-phoA fusion analysis and site- 12926RT directed spectroscopy."; 12927RL Biochemistry 34:14909-14917(1995). 12928RN [9] 12929RP MUTAGENESIS. 12930RX MEDLINE=91167519; PubMed=1848449; DOI=10.1016/0005-2736(91)90390-T; 12931RA King S.C., Hansen C.L., Wilson T.H.; 12932RT "The interaction between aspartic acid 237 and lysine 358 in the 12933RT lactose carrier of Escherichia coli."; 12934RL Biochim. Biophys. Acta 1062:177-186(1991). 12935RN [10] 12936RP MUTAGENESIS. 12937RX MEDLINE=92355521; PubMed=1644770; 12938RA Huang A.-M., Lee J.-I., King S.C., Wilson T.H.; 12939RT "Amino acid substitution in the lactose carrier protein with the use 12940RT of amber suppressors."; 12941RL J. Bacteriol. 174:5436-5441(1992). 12942RN [11] 12943RP REVIEW. 12944RX MEDLINE=90366577; PubMed=2203471; DOI=10.1016/0005-2728(90)90239-Z; 12945RA Kaback H.R.; 12946RT "The lac permease of Escherichia coli: a prototypic energy-transducing 12947RT membrane protein."; 12948RL Biochim. Biophys. Acta 1018:160-162(1990). 12949RN [12] 12950RP MASS SPECTROMETRY OF FORMYLATED FORM. 12951RX MEDLINE=99415921; PubMed=10485888; DOI=10.1073/pnas.96.19.10695; 12952RA Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G., 12953RA Faull K.F., Kaback H.R.; 12954RT "Toward the bilayer proteome, electrospray ionization-mass 12955RT spectrometry of large, intact transmembrane proteins."; 12956RL Proc. Natl. Acad. Sci. U.S.A. 96:10695-10698(1999). 12957RN [13] 12958RP TOPOLOGY [LARGE SCALE ANALYSIS]. 12959RC STRAIN=K12 / MG1655 / ATCC 47076; 12960RX PubMed=15919996; DOI=10.1126/science.1109730; 12961RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; 12962RT "Global topology analysis of the Escherichia coli inner membrane 12963RT proteome."; 12964RL Science 308:1321-1323(2005). 12965RN [14] 12966RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF MUTANT GLY-154. 12967RX MEDLINE=22776143; PubMed=12893935; DOI=10.1126/science.1088196; 12968RA Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., Iwata S.; 12969RT "Structure and mechanism of the lactose permease of Escherichia 12970RT coli."; 12971RL Science 301:610-615(2003). 12972CC -!- FUNCTION: Responsible for transport of beta-galactosides into the 12973CC cell, with the concomitant import of a proton (symport system). 12974CC -!- SUBUNIT: Monomer. 12975CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane 12976CC protein. 12977CC -!- MASS SPECTROMETRY: Mass=47357; Method=Electrospray; Range=1-417; 12978CC Source=PubMed:10485888; 12979CC -!- SIMILARITY: Belongs to the lacY/rafB permease family. 12980CC ----------------------------------------------------------------------- 12981CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 12982CC Distributed under the Creative Commons Attribution-NoDerivs License 12983CC ----------------------------------------------------------------------- 12984DR EMBL; J01636; AAA24054.1; -; Genomic_DNA. 12985DR EMBL; V00295; CAA23571.1; -; Genomic_DNA. 12986DR EMBL; X56095; CAA39575.1; -; Genomic_DNA. 12987DR EMBL; U73857; AAB18067.1; -; Genomic_DNA. 12988DR EMBL; U00096; AAC73446.1; -; Genomic_DNA. 12989DR EMBL; AP009048; BAE76125.1; -; Genomic_DNA. 12990DR PIR; A03418; GREC. 12991DR RefSeq; NP_414877.1; NC_000913.2. 12992DR PDB; 1M2U; Model; -; A=1-417. 12993DR PDB; 1PV6; X-ray; 3.50 A; A/B=1-417. 12994DR PDB; 1PV7; X-ray; 3.60 A; A/B=1-417. 12995DR PDB; 2CFP; X-ray; 3.30 A; A=1-417. 12996DR PDB; 2CFQ; X-ray; 2.95 A; A=1-417. 12997DR PDB; 2V8N; X-ray; 3.60 A; A/B=1-417. 12998DR PDB; 2Y5Y; X-ray; 3.38 A; A/B=1-417. 12999DR PDBsum; 1M2U; -. 13000DR PDBsum; 1PV6; -. 13001DR PDBsum; 1PV7; -. 13002DR PDBsum; 2CFP; -. 13003DR PDBsum; 2CFQ; -. 13004DR PDBsum; 2V8N; -. 13005DR PDBsum; 2Y5Y; -. 13006DR ProteinModelPortal; P02920; -. 13007DR SMR; P02920; 1-417. 13008DR DIP; DIP-10080N; -. 13009DR TCDB; 2.A.1.5.1; major facilitator superfamily (MFS). 13010DR EnsemblBacteria; EBESCT00000004293; EBESCP00000004293; EBESCG00000003502. 13011DR EnsemblBacteria; EBESCT00000004294; EBESCP00000004294; EBESCG00000003502. 13012DR EnsemblBacteria; EBESCT00000004295; EBESCP00000004295; EBESCG00000003502. 13013DR EnsemblBacteria; EBESCT00000004296; EBESCP00000004296; EBESCG00000003502. 13014DR EnsemblBacteria; EBESCT00000017446; EBESCP00000016737; EBESCG00000016502. 13015DR GeneID; 949083; -. 13016DR GenomeReviews; AP009048_GR; JW0334. 13017DR GenomeReviews; U00096_GR; b0343. 13018DR KEGG; eco:b0343; -. 13019DR PATRIC; 32115819; VBIEscCol129921_0351. 13020DR EchoBASE; EB0521; -. 13021DR EcoGene; EG10526; lacY. 13022DR eggNOG; COG0477; -. 13023DR HOGENOM; HOG000114363; -. 13024DR KO; K02532; -. 13025DR OMA; WAICASI; -. 13026DR ProtClustDB; PRK09528; -. 13027DR BioCyc; EcoCyc:LACY-MONOMER; -. 13028DR EvolutionaryTrace; P02920; -. 13029DR Genevestigator; P02920; -. 13030DR GO; GO:0005887; C:integral to plasma membrane; IDA:EcoCyc. 13031DR GO; GO:0030395; F:lactose binding; IDA:EcoliWiki. 13032DR GO; GO:0015528; F:lactose:hydrogen symporter activity; IDA:EcoCyc. 13033DR InterPro; IPR022814; LacY_symp. 13034DR InterPro; IPR000576; LacY_symport_bac. 13035DR InterPro; IPR018457; LacY_symport_CS. 13036DR InterPro; IPR020846; MFS_dom. 13037DR InterPro; IPR016196; MFS_dom_general_subst_transpt. 13038DR PANTHER; PTHR24003:SF271; PTHR24003:SF271; 1. 13039DR Pfam; PF01306; LacY_symp; 1. 13040DR PRINTS; PR00174; LACYSMPORT. 13041DR SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1. 13042DR TIGRFAMs; TIGR00882; 2A0105; 1. 13043DR PROSITE; PS00896; LACY_1; 1. 13044DR PROSITE; PS00897; LACY_2; 1. 13045DR PROSITE; PS50850; MFS; 1. 13046PE 1: Evidence at protein level; 13047KW 3D-structure; Cell inner membrane; Cell membrane; Complete proteome; 13048KW Formylation; Membrane; Reference proteome; Sugar transport; Symport; 13049KW Transmembrane; Transmembrane helix; Transport. 13050FT CHAIN 1 417 Lactose permease. 13051FT /FTId=PRO_0000196184. 13052FT TOPO_DOM 1 7 Cytoplasmic. 13053FT TRANSMEM 8 34 Helical; Name=1. 13054FT TOPO_DOM 35 41 Periplasmic. 13055FT TRANSMEM 42 70 Helical; Name=2. 13056FT TOPO_DOM 71 74 Cytoplasmic. 13057FT TRANSMEM 75 100 Helical; Name=3. 13058FT TOPO_DOM 101 104 Periplasmic. 13059FT TRANSMEM 105 129 Helical; Name=4. 13060FT TOPO_DOM 130 140 Cytoplasmic. 13061FT TRANSMEM 141 163 Helical; Name=5. 13062FT TOPO_DOM 164 166 Periplasmic. 13063FT TRANSMEM 167 186 Helical; Name=6. 13064FT TOPO_DOM 187 220 Cytoplasmic. 13065FT TRANSMEM 221 249 Helical; Name=7. 13066FT TOPO_DOM 250 253 Periplasmic. 13067FT TRANSMEM 254 278 Helical; Name=8. 13068FT TOPO_DOM 279 288 Cytoplasmic. 13069FT TRANSMEM 289 308 Helical; Name=9. 13070FT TOPO_DOM 309 311 Periplasmic. 13071FT TRANSMEM 312 334 Helical; Name=10. 13072FT TOPO_DOM 335 346 Cytoplasmic. 13073FT TRANSMEM 347 374 Helical; Name=11. 13074FT TOPO_DOM 375 377 Periplasmic. 13075FT TRANSMEM 378 398 Helical; Name=12. 13076FT TOPO_DOM 399 417 Cytoplasmic. 13077FT SITE 126 126 Substrate binding. 13078FT SITE 144 144 Substrate binding. 13079FT SITE 269 269 Substrate binding and proton 13080FT translocation. 13081FT SITE 302 302 Proton translocation. 13082FT SITE 322 322 Proton translocation. 13083FT SITE 325 325 Proton translocation. 13084FT MOD_RES 1 1 N-formylmethionine; partial. 13085FT MUTAGEN 237 237 D->N,G: Defect in melibiose transport. 13086FT MUTAGEN 358 358 K->T: Defect in melibiose transport. 13087FT TURN 2 4 13088FT HELIX 8 12 13089FT TURN 13 16 13090FT HELIX 17 23 13091FT TURN 24 28 13092FT HELIX 31 38 13093FT HELIX 42 54 13094FT TURN 55 57 13095FT HELIX 60 67 13096FT HELIX 68 70 13097FT HELIX 76 79 13098FT TURN 80 83 13099FT STRAND 84 87 13100FT HELIX 88 93 13101FT HELIX 96 99 13102FT TURN 100 102 13103FT HELIX 105 109 13104FT TURN 114 120 13105FT HELIX 121 135 13106FT HELIX 140 142 13107FT HELIX 144 164 13108FT HELIX 168 171 13109FT HELIX 173 177 13110FT HELIX 178 183 13111FT STRAND 201 203 13112FT HELIX 210 216 13113FT HELIX 220 231 13114FT TURN 232 235 13115FT HELIX 236 242 13116FT HELIX 245 249 13117FT STRAND 251 254 13118FT HELIX 257 267 13119FT HELIX 270 276 13120FT HELIX 279 286 13121FT HELIX 289 307 13122FT HELIX 312 320 13123FT HELIX 322 324 13124FT HELIX 326 340 13125FT TURN 343 345 13126FT HELIX 346 349 13127FT HELIX 351 356 13128FT HELIX 357 399 13129FT STRAND 408 411 13130FT TURN 414 416 13131SQ SEQUENCE 417 AA; 46503 MW; 24A8062F628CDA32 CRC64; 13132 MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA AISLFSLLFQ 13133 PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ YNILVGSIVG GIYLGFCFNA 13134 GAPAVEAFIE KVSRRSNFEF GRARMFGCVG WALCASIVGI MFTINNQFVF WLGSGCALIL 13135 AVLLFFAKTD APSSATVANA VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD 13136 QQFANFFTSF FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS 13137 VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY LVCFCFFKQL 13138 AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL SGPGPLSLLR RQVNEVA 13139// 13140ID OPS2_DROME Reviewed; 381 AA. 13141AC P08099; Q9VE29; 13142DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. 13143DT 01-AUG-1988, sequence version 1. 13144DT 22-FEB-2012, entry version 112. 13145DE RecName: Full=Opsin Rh2; 13146DE AltName: Full=Ocellar opsin; 13147GN Name=Rh2; ORFNames=CG16740; 13148OS Drosophila melanogaster (Fruit fly). 13149OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 13150OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; 13151OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. 13152OX NCBI_TaxID=7227; 13153RN [1] 13154RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 13155RX MEDLINE=86133563; PubMed=2936466; DOI=10.1016/0092-8674(86)90836-6; 13156RA Cowman A.F., Zuker C.S., Rubin G.M.; 13157RT "An opsin gene expressed in only one photoreceptor cell type of the 13158RT Drosophila eye."; 13159RL Cell 44:705-710(1986). 13160RN [2] 13161RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 13162RC STRAIN=Berkeley; 13163RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; 13164RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., 13165RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., 13166RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., 13167RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., 13168RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., 13169RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 13170RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., 13171RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., 13172RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., 13173RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., 13174RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., 13175RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., 13176RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., 13177RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., 13178RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., 13179RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., 13180RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., 13181RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., 13182RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., 13183RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., 13184RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., 13185RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., 13186RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., 13187RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., 13188RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., 13189RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., 13190RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., 13191RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., 13192RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., 13193RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., 13194RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., 13195RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., 13196RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., 13197RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., 13198RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., 13199RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; 13200RT "The genome sequence of Drosophila melanogaster."; 13201RL Science 287:2185-2195(2000). 13202RN [3] 13203RP GENOME REANNOTATION. 13204RC STRAIN=Berkeley; 13205RX MEDLINE=22426069; PubMed=12537572; 13206RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., 13207RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., 13208RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., 13209RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., 13210RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., 13211RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., 13212RA Lewis S.E.; 13213RT "Annotation of the Drosophila melanogaster euchromatic genome: a 13214RT systematic review."; 13215RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). 13216RN [4] 13217RP LOCALIZATION OF OPSIN RH2, AND BIOPHYSICOCHEMICAL PROPERTIES. 13218RX MEDLINE=88261498; PubMed=2455230; DOI=10.1038/333737a0; 13219RA Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.; 13220RT "Targeted misexpression of a Drosophila opsin gene leads to altered 13221RT visual function."; 13222RL Nature 333:737-741(1988). 13223RN [5] 13224RP LOCALIZATION OF OPSIN RH2. 13225RX MEDLINE=88261503; PubMed=2968518; DOI=10.1038/333779a0; 13226RA Pollock J.A., Benzer S.; 13227RT "Transcript localization of four opsin genes in the three visual 13228RT organs of Drosophila; RH2 is ocellus specific."; 13229RL Nature 333:779-782(1988). 13230CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 13231CC mediate vision. They consist of an apoprotein, opsin, covalently 13232CC linked to cis-retinal. 13233CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 13234CC Absorption: 13235CC Abs(max)=420 nm; 13236CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 13237CC -!- TISSUE SPECIFICITY: Predominant opsin expressed in the dorsal 13238CC ocelli. 13239CC -!- PTM: Phosphorylated on some or all of the serine and threonine 13240CC residues present in the C-terminal region. 13241CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 13242CC Opsin subfamily. 13243CC ----------------------------------------------------------------------- 13244CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 13245CC Distributed under the Creative Commons Attribution-NoDerivs License 13246CC ----------------------------------------------------------------------- 13247DR EMBL; M12896; AAA28734.1; -; Genomic_DNA. 13248DR EMBL; AE014297; AAF55601.1; -; Genomic_DNA. 13249DR PIR; A24058; OOFF2. 13250DR RefSeq; NP_524398.1; NM_079674.3. 13251DR ProteinModelPortal; P08099; -. 13252DR SMR; P08099; 39-360. 13253DR DIP; DIP-22447N; -. 13254DR IntAct; P08099; 1. 13255DR MINT; MINT-844888; -. 13256DR STRING; P08099; -. 13257DR PRIDE; P08099; -. 13258DR EnsemblMetazoa; FBtr0083697; FBpp0083111; FBgn0003248. 13259DR GeneID; 42261; -. 13260DR KEGG; dme:Dmel_CG16740; -. 13261DR CTD; 42261; -. 13262DR FlyBase; FBgn0003248; Rh2. 13263DR eggNOG; NOG255465; -. 13264DR GeneTree; ENSGT00550000074069; -. 13265DR InParanoid; P08099; -. 13266DR KO; K04255; -. 13267DR OMA; RSSEDCD; -. 13268DR OrthoDB; EOG451C6G; -. 13269DR PhylomeDB; P08099; -. 13270DR NextBio; 827942; -. 13271DR Bgee; P08099; -. 13272DR GermOnline; CG16740; Drosophila melanogaster. 13273DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 13274DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA:FlyBase. 13275DR GO; GO:0007602; P:phototransduction; IGI:FlyBase. 13276DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 13277DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 13278DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 13279DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 13280DR InterPro; IPR001760; Opsin. 13281DR InterPro; IPR001735; Opsin_RH1/RH2. 13282DR Pfam; PF00001; 7tm_1; 1. 13283DR PRINTS; PR00237; GPCRRHODOPSN. 13284DR PRINTS; PR00238; OPSIN. 13285DR PRINTS; PR00576; OPSINRH1RH2. 13286DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 13287DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 13288DR PROSITE; PS00238; OPSIN; 1. 13289PE 1: Evidence at protein level; 13290KW Chromophore; Complete proteome; Disulfide bond; 13291KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; 13292KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein; 13293KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix; 13294KW Vision. 13295FT CHAIN 1 381 Opsin Rh2. 13296FT /FTId=PRO_0000197625. 13297FT TOPO_DOM 1 56 Extracellular. 13298FT TRANSMEM 57 81 Helical; Name=1; (Potential). 13299FT TOPO_DOM 82 93 Cytoplasmic. 13300FT TRANSMEM 94 119 Helical; Name=2; (Potential). 13301FT TOPO_DOM 120 133 Extracellular. 13302FT TRANSMEM 134 153 Helical; Name=3; (Potential). 13303FT TOPO_DOM 154 172 Cytoplasmic. 13304FT TRANSMEM 173 196 Helical; Name=4; (Potential). 13305FT TOPO_DOM 197 220 Extracellular. 13306FT TRANSMEM 221 248 Helical; Name=5; (Potential). 13307FT TOPO_DOM 249 283 Cytoplasmic. 13308FT TRANSMEM 284 307 Helical; Name=6; (Potential). 13309FT TOPO_DOM 308 314 Extracellular. 13310FT TRANSMEM 315 339 Helical; Name=7; (Potential). 13311FT TOPO_DOM 340 381 Cytoplasmic. 13312FT MOD_RES 326 326 N6-(retinylidene)lysine. 13313FT CARBOHYD 27 27 N-linked (GlcNAc...) (Probable). 13314FT DISULFID 130 207 Potential. 13315SQ SEQUENCE 381 AA; 42722 MW; 628322D228396F9D CRC64; 13316 MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL 13317 GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY 13318 ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI 13319 WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS 13320 YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL 13321 VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD 13322 EPKPDAPASD TETTSEADSK A 13323// 13324ID OPS2_DROPS Reviewed; 381 AA. 13325AC P28679; Q298F1; 13326DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. 13327DT 13-JUN-2006, sequence version 3. 13328DT 18-APR-2012, entry version 85. 13329DE RecName: Full=Opsin Rh2; 13330DE AltName: Full=Ocellar opsin; 13331GN Name=Rh2; ORFNames=GA14120; 13332OS Drosophila pseudoobscura pseudoobscura (Fruit fly). 13333OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 13334OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; 13335OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. 13336OX NCBI_TaxID=46245; 13337RN [1] 13338RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 13339RC STRAIN=Apple Hill; 13340RX MEDLINE=93012921; PubMed=1398053; 13341RA Carulli J.P., Hartl D.L.; 13342RT "Variable rates of evolution among Drosophila opsin genes."; 13343RL Genetics 132:193-204(1992). 13344RN [2] 13345RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 13346RC STRAIN=MV2-25 / Tucson 14011-0121.94; 13347RX PubMed=15632085; DOI=10.1101/gr.3059305; 13348RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., 13349RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., 13350RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., 13351RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., 13352RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., 13353RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., 13354RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., 13355RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., 13356RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., 13357RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., 13358RA Weinstock G.M., Gibbs R.A.; 13359RT "Comparative genome sequencing of Drosophila pseudoobscura: 13360RT chromosomal, gene, and cis-element evolution."; 13361RL Genome Res. 15:1-18(2005). 13362CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 13363CC mediate vision. They consist of an apoprotein, opsin, covalently 13364CC linked to cis-retinal. 13365CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 13366CC Absorption: 13367CC Abs(max)=420 nm; 13368CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 13369CC -!- PTM: Some or all of the Ser/Thr residues present in the C-terminal 13370CC part may be phosphorylated. 13371CC -!- MISCELLANEOUS: Opsin Rh2 is the predominant opsin expressed in the 13372CC dorsal ocelli. 13373CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 13374CC Opsin subfamily. 13375CC -!- SEQUENCE CAUTION: 13376CC Sequence=EAL28004.1; Type=Erroneous gene model prediction; 13377CC ----------------------------------------------------------------------- 13378CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 13379CC Distributed under the Creative Commons Attribution-NoDerivs License 13380CC ----------------------------------------------------------------------- 13381DR EMBL; X65878; CAA46709.1; -; Genomic_DNA. 13382DR EMBL; CM000070; EAL28004.1; ALT_SEQ; Genomic_DNA. 13383DR PIR; S40692; S40692. 13384DR RefSeq; XP_001358861.1; XM_001358824.2. 13385DR ProteinModelPortal; P28679; -. 13386DR GeneID; 4801828; -. 13387DR GenomeReviews; CM000070_GR; Rh2. 13388DR KEGG; dpo:Dpse_GA14120; -. 13389DR FlyBase; FBgn0012708; Dpse\Rh2. 13390DR eggNOG; NOG255465; -. 13391DR InParanoid; P28679; -. 13392DR KO; K04255; -. 13393DR OMA; RSSEDCD; -. 13394DR OrthoDB; EOG451C6G; -. 13395DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 13396DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 13397DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 13398DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 13399DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 13400DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 13401DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 13402DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 13403DR InterPro; IPR001760; Opsin. 13404DR InterPro; IPR001735; Opsin_RH1/RH2. 13405DR Pfam; PF00001; 7tm_1; 1. 13406DR PRINTS; PR00237; GPCRRHODOPSN. 13407DR PRINTS; PR00238; OPSIN. 13408DR PRINTS; PR00576; OPSINRH1RH2. 13409DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 13410DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 13411DR PROSITE; PS00238; OPSIN; 1. 13412PE 1: Evidence at protein level; 13413KW Chromophore; Complete proteome; Disulfide bond; 13414KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; 13415KW Photoreceptor protein; Receptor; Reference proteome; Retinal protein; 13416KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix; 13417KW Vision. 13418FT CHAIN 1 381 Opsin Rh2. 13419FT /FTId=PRO_0000197626. 13420FT TOPO_DOM 1 56 Extracellular. 13421FT TRANSMEM 57 81 Helical; Name=1; (Potential). 13422FT TOPO_DOM 82 93 Cytoplasmic. 13423FT TRANSMEM 94 119 Helical; Name=2; (Potential). 13424FT TOPO_DOM 120 133 Extracellular. 13425FT TRANSMEM 134 153 Helical; Name=3; (Potential). 13426FT TOPO_DOM 154 172 Cytoplasmic. 13427FT TRANSMEM 173 196 Helical; Name=4; (Potential). 13428FT TOPO_DOM 197 220 Extracellular. 13429FT TRANSMEM 221 248 Helical; Name=5; (Potential). 13430FT TOPO_DOM 249 283 Cytoplasmic. 13431FT TRANSMEM 284 307 Helical; Name=6; (Potential). 13432FT TOPO_DOM 308 314 Extracellular. 13433FT TRANSMEM 315 339 Helical; Name=7; (Potential). 13434FT TOPO_DOM 340 381 Cytoplasmic. 13435FT MOD_RES 326 326 N6-(retinylidene)lysine. 13436FT CARBOHYD 27 27 N-linked (GlcNAc...) (Probable). 13437FT DISULFID 130 207 Potential. 13438FT CONFLICT 45 45 Y -> H (in Ref. 1; CAA46709). 13439FT CONFLICT 342 343 KY -> ND (in Ref. 1; CAA46709). 13440FT CONFLICT 358 358 S -> T (in Ref. 1; CAA46709). 13441FT CONFLICT 381 381 A -> D (in Ref. 1; CAA46709). 13442SQ SEQUENCE 381 AA; 42733 MW; 2033C05C4503FEAF CRC64; 13443 MERSLLPEPP LAMALLGPRF EAQTGGNRSV LDNVLPDMAP LVNPYWSRFA PMDPTMSKIL 13444 GLFTLVILII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY 13445 ETWVLGPLWC DIYAACGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKIAFI 13446 WMMAVFWTIM PLIGWSSYVP EGNLTACSID YMTRQWNPRS YLITYSLFVY YTPLFMICYS 13447 YWFIIATVAA HEKAMRDQAK KMNVKSLRSS EDCDKSAENK LAKVALTTIS LWFMAWTPYL 13448 IICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRLVLKEK CPMCVCGSTD 13449 EPKPDAPPSD TETTSEAESK A 13450// 13451ID OPS2_SCHGR Reviewed; 380 AA. 13452AC Q26495; 13453DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 13454DT 01-NOV-1997, sequence version 1. 13455DT 21-SEP-2011, entry version 61. 13456DE RecName: Full=Opsin-2; 13457GN Name=Lo2; 13458OS Schistocerca gregaria (Desert locust). 13459OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; 13460OC Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha; 13461OC Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca. 13462OX NCBI_TaxID=7010; 13463RN [1] 13464RP NUCLEOTIDE SEQUENCE [MRNA]. 13465RX MEDLINE=97301174; PubMed=9156194; DOI=10.1016/S0042-6989(96)00198-8; 13466RA Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.; 13467RT "Primary structure of locust opsins: a speculative model which may 13468RT account for ultraviolet wavelength light detection."; 13469RL Vision Res. 37:495-503(1997). 13470CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 13471CC mediate vision. They consist of an apoprotein, opsin, covalently 13472CC linked to cis-retinal. 13473CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 13474CC -!- PTM: Phosphorylated on some or all of the serine and threonine 13475CC residues present in the C-terminal region (By similarity). 13476CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 13477CC Opsin subfamily. 13478CC ----------------------------------------------------------------------- 13479CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 13480CC Distributed under the Creative Commons Attribution-NoDerivs License 13481CC ----------------------------------------------------------------------- 13482DR EMBL; X80072; CAA56378.1; -; mRNA. 13483DR ProteinModelPortal; Q26495; -. 13484DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 13485DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 13486DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 13487DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 13488DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 13489DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 13490DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 13491DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 13492DR InterPro; IPR001760; Opsin. 13493DR InterPro; IPR000856; Opsin_RH3/RH4. 13494DR Pfam; PF00001; 7tm_1; 1. 13495DR PRINTS; PR00237; GPCRRHODOPSN. 13496DR PRINTS; PR00577; OPSINRH3RH4. 13497DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 13498DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 13499DR PROSITE; PS00238; OPSIN; 1. 13500PE 2: Evidence at transcript level; 13501KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; 13502KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; 13503KW Retinal protein; Sensory transduction; Transducer; Transmembrane; 13504KW Transmembrane helix; Vision. 13505FT CHAIN 1 380 Opsin-2. 13506FT /FTId=PRO_0000197636. 13507FT TOPO_DOM 1 51 Extracellular. 13508FT TRANSMEM 52 76 Helical; Name=1; (Potential). 13509FT TOPO_DOM 77 88 Cytoplasmic. 13510FT TRANSMEM 89 115 Helical; Name=2; (Potential). 13511FT TOPO_DOM 116 128 Extracellular. 13512FT TRANSMEM 129 148 Helical; Name=3; (Potential). 13513FT TOPO_DOM 149 166 Cytoplasmic. 13514FT TRANSMEM 167 191 Helical; Name=4; (Potential). 13515FT TOPO_DOM 192 215 Extracellular. 13516FT TRANSMEM 216 243 Helical; Name=5; (Potential). 13517FT TOPO_DOM 244 279 Cytoplasmic. 13518FT TRANSMEM 280 303 Helical; Name=6; (Potential). 13519FT TOPO_DOM 304 311 Extracellular. 13520FT TRANSMEM 312 336 Helical; Name=7; (Potential). 13521FT TOPO_DOM 337 380 Cytoplasmic. 13522FT MOD_RES 323 323 N6-(retinylidene)lysine (By similarity). 13523FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). 13524FT DISULFID 125 202 Potential. 13525SQ SEQUENCE 380 AA; 42531 MW; 113504F71027C07A CRC64; 13526 MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF 13527 MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG 13528 WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP 13529 FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI 13530 GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM 13531 IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS 13532 KSDTSSTATD RTVGNVSASA 13533// 13534ID OPSC2_HEMSA Reviewed; 377 AA. 13535AC Q25158; 13536DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 13537DT 01-NOV-1997, sequence version 1. 13538DT 21-SEP-2011, entry version 60. 13539DE RecName: Full=Compound eye opsin BCRH2; 13540OS Hemigrapsus sanguineus (Asian shore crab). 13541OC Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca; 13542OC Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; 13543OC Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus. 13544OX NCBI_TaxID=40176; 13545RN [1] 13546RP NUCLEOTIDE SEQUENCE [MRNA]. 13547RC TISSUE=Eye; 13548RX PubMed=9318091; 13549RA Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.; 13550RT "Two opsins from the compound eye of the crab Hemigrapsus 13551RT sanguineus."; 13552RL J. Exp. Biol. 199:441-450(1996). 13553CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 13554CC mediate vision. They consist of an apoprotein, opsin, covalently 13555CC linked to cis-retinal. This opsin produces visual pigments with 13556CC maximal absorption in the blue-green region of the spectrum. 13557CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 13558CC -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells 13559CC (R1-R7) forming the main rhabdom in each ommatidium. 13560CC -!- PTM: Phosphorylated on some or all of the serine and threonine 13561CC residues present in the C-terminal region (By similarity). 13562CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 13563CC Opsin subfamily. 13564CC ----------------------------------------------------------------------- 13565CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 13566CC Distributed under the Creative Commons Attribution-NoDerivs License 13567CC ----------------------------------------------------------------------- 13568DR EMBL; D50584; BAA09133.1; -; mRNA. 13569DR ProteinModelPortal; Q25158; -. 13570DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 13571DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 13572DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 13573DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 13574DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 13575DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 13576DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 13577DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 13578DR InterPro; IPR001760; Opsin. 13579DR InterPro; IPR000856; Opsin_RH3/RH4. 13580DR Pfam; PF00001; 7tm_1; 1. 13581DR PRINTS; PR00237; GPCRRHODOPSN. 13582DR PRINTS; PR00238; OPSIN. 13583DR PRINTS; PR00577; OPSINRH3RH4. 13584DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 13585DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 13586DR PROSITE; PS00238; OPSIN; 1. 13587PE 2: Evidence at transcript level; 13588KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; 13589KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; 13590KW Retinal protein; Sensory transduction; Transducer; Transmembrane; 13591KW Transmembrane helix; Vision. 13592FT CHAIN 1 377 Compound eye opsin BCRH2. 13593FT /FTId=PRO_0000197750. 13594FT TOPO_DOM 1 53 Extracellular. 13595FT TRANSMEM 54 78 Helical; Name=1; (Potential). 13596FT TOPO_DOM 79 90 Cytoplasmic. 13597FT TRANSMEM 91 115 Helical; Name=2; (Potential). 13598FT TOPO_DOM 116 131 Extracellular. 13599FT TRANSMEM 132 151 Helical; Name=3; (Potential). 13600FT TOPO_DOM 152 170 Cytoplasmic. 13601FT TRANSMEM 171 194 Helical; Name=4; (Potential). 13602FT TOPO_DOM 195 218 Extracellular. 13603FT TRANSMEM 219 246 Helical; Name=5; (Potential). 13604FT TOPO_DOM 247 281 Cytoplasmic. 13605FT TRANSMEM 282 305 Helical; Name=6; (Potential). 13606FT TOPO_DOM 306 313 Extracellular. 13607FT TRANSMEM 314 338 Helical; Name=7; (Potential). 13608FT TOPO_DOM 339 377 Cytoplasmic. 13609FT MOD_RES 325 325 N6-(retinylidene)lysine (By similarity). 13610FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). 13611FT DISULFID 128 205 By similarity. 13612SQ SEQUENCE 377 AA; 42114 MW; FD6CC2E0E199A256 CRC64; 13613 MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI 13614 YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV 13615 WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV 13616 IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV 13617 FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI 13618 SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET 13619 KSNDDSQSNS TVAQDKA 13620// 13621ID OPSD2_MIZYE Reviewed; 399 AA. 13622AC O15974; 13623DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. 13624DT 01-JAN-1998, sequence version 1. 13625DT 21-SEP-2011, entry version 58. 13626DE RecName: Full=Rhodopsin, G0-coupled; 13627DE AltName: Full=G0-rhodopsin; 13628GN Name=SCOP2; 13629OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis). 13630OC Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida; 13631OC Pectinoidea; Pectinidae; Mizuhopecten. 13632OX NCBI_TaxID=6573; 13633RN [1] 13634RP NUCLEOTIDE SEQUENCE [MRNA]. 13635RC TISSUE=Eye; 13636RX MEDLINE=97435252; PubMed=9287291; DOI=10.1074/jbc.272.37.22979; 13637RA Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A., 13638RA Shichida Y.; 13639RT "A novel Go-mediated phototransduction cascade in scallop visual 13640RT cells."; 13641RL J. Biol. Chem. 272:22979-22982(1997). 13642CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 13643CC mediate vision. They consist of an apoprotein, opsin, covalently 13644CC linked to cis-retinal. 13645CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 13646CC -!- TISSUE SPECIFICITY: Retina. Expressed in the hyperpolarizing cell 13647CC layer of the photoreceptor cells with its photoreceptive region 13648CC adjacent to the lens. 13649CC -!- PTM: Phosphorylated on some or all of the serine and threonine 13650CC residues present in the C-terminal region (By similarity). 13651CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 13652CC Opsin subfamily. 13653CC ----------------------------------------------------------------------- 13654CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 13655CC Distributed under the Creative Commons Attribution-NoDerivs License 13656CC ----------------------------------------------------------------------- 13657DR EMBL; AB006455; BAA22218.1; -; mRNA. 13658DR ProteinModelPortal; O15974; -. 13659DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 13660DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 13661DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 13662DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 13663DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 13664DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 13665DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 13666DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 13667DR InterPro; IPR001760; Opsin. 13668DR InterPro; IPR002962; Peropsin. 13669DR Pfam; PF00001; 7tm_1; 1. 13670DR PRINTS; PR00237; GPCRRHODOPSN. 13671DR PRINTS; PR01244; PEROPSIN. 13672DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. 13673DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 13674DR PROSITE; PS00238; OPSIN; 1. 13675PE 1: Evidence at protein level; 13676KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; 13677KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; 13678KW Retinal protein; Sensory transduction; Transducer; Transmembrane; 13679KW Transmembrane helix; Vision. 13680FT CHAIN 1 399 Rhodopsin, G0-coupled. 13681FT /FTId=PRO_0000197736. 13682FT TOPO_DOM 1 17 Extracellular. 13683FT TRANSMEM 18 43 Helical; Name=1; (Potential). 13684FT TOPO_DOM 44 55 Cytoplasmic. 13685FT TRANSMEM 56 81 Helical; Name=2; (Potential). 13686FT TOPO_DOM 82 95 Extracellular. 13687FT TRANSMEM 96 115 Helical; Name=3; (Potential). 13688FT TOPO_DOM 116 134 Cytoplasmic. 13689FT TRANSMEM 135 158 Helical; Name=4; (Potential). 13690FT TOPO_DOM 159 182 Extracellular. 13691FT TRANSMEM 183 210 Helical; Name=5; (Potential). 13692FT TOPO_DOM 211 240 Cytoplasmic. 13693FT TRANSMEM 241 263 Helical; Name=6; (Potential). 13694FT TOPO_DOM 264 271 Extracellular. 13695FT TRANSMEM 272 295 Helical; Name=7; (Potential). 13696FT TOPO_DOM 296 399 Cytoplasmic. 13697FT MOD_RES 282 282 N6-(retinylidene)lysine. 13698FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). 13699FT DISULFID 92 169 By similarity. 13700SQ SEQUENCE 399 AA; 45097 MW; 5AA6857ABC912100 CRC64; 13701 MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN 13702 LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII 13703 ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD 13704 VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF 13705 ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR 13706 DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV 13707 KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI 13708// 13709ID OPSD_HUMAN Reviewed; 348 AA. 13710AC P08100; Q16414; Q2M249; 13711DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. 13712DT 01-AUG-1988, sequence version 1. 13713DT 13-JUN-2012, entry version 145. 13714DE RecName: Full=Rhodopsin; 13715DE AltName: Full=Opsin-2; 13716GN Name=RHO; Synonyms=OPN2; 13717OS Homo sapiens (Human). 13718OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 13719OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 13720OC Catarrhini; Hominidae; Homo. 13721OX NCBI_TaxID=9606; 13722RN [1] 13723RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 13724RX MEDLINE=84272729; PubMed=6589631; DOI=10.1073/pnas.81.15.4851; 13725RA Nathans J., Hogness D.S.; 13726RT "Isolation and nucleotide sequence of the gene encoding human 13727RT rhodopsin."; 13728RL Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984). 13729RN [2] 13730RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 13731RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., 13732RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; 13733RT "Genome-wide discovery and analysis of human seven transmembrane helix 13734RT receptor genes."; 13735RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. 13736RN [3] 13737RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 13738RC TISSUE=Retina; 13739RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; 13740RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., 13741RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., 13742RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., 13743RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; 13744RT "The full-ORF clone resource of the German cDNA consortium."; 13745RL BMC Genomics 8:399-399(2007). 13746RN [4] 13747RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 13748RX PubMed=15489334; DOI=10.1101/gr.2596504; 13749RG The MGC Project Team; 13750RT "The status, quality, and expansion of the NIH full-length cDNA 13751RT project: the Mammalian Gene Collection (MGC)."; 13752RL Genome Res. 14:2121-2127(2004). 13753RN [5] 13754RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120. 13755RX PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5; 13756RA Bennett J., Beller B., Sun D., Kariko K.; 13757RT "Sequence analysis of the 5.34-kb 5' flanking region of the human 13758RT rhodopsin-encoding gene."; 13759RL Gene 167:317-320(1995). 13760RN [6] 13761RP REVIEW ON RP4 VARIANTS. 13762RX MEDLINE=94004905; PubMed=8401533; DOI=10.1002/humu.1380020403; 13763RA Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A., 13764RA Bhattacharya S.; 13765RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa."; 13766RL Hum. Mutat. 2:249-255(1993). 13767RN [7] 13768RP VARIANTS RP4. 13769RX MEDLINE=91051574; PubMed=2239971; 13770RA Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G., 13771RA Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., 13772RA Watty A., Ludwig M., Schinzel A., Samanns C., Gal A., 13773RA Bhattacharya S.S., Humphries P.; 13774RT "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin 13775RT proline-->histidine substitution (codon 23) in pedigrees from 13776RT Europe."; 13777RL Am. J. Hum. Genet. 47:941-945(1990). 13778RN [8] 13779RP VARIANT RP4 HIS-23. 13780RX MEDLINE=90136922; PubMed=2137202; DOI=10.1038/343364a0; 13781RA Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., 13782RA Yandell D.W., Sandberg M.A., Berson E.L.; 13783RT "A point mutation of the rhodopsin gene in one form of retinitis 13784RT pigmentosa."; 13785RL Nature 343:364-366(1990). 13786RN [9] 13787RP VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347. 13788RX MEDLINE=91015273; PubMed=2215617; 13789RA Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., 13790RA Reichel E., Sandberg M.A., Berson E.L.; 13791RT "Mutations within the rhodopsin gene in patients with autosomal 13792RT dominant retinitis pigmentosa."; 13793RL N. Engl. J. Med. 323:1302-1307(1990). 13794RN [10] 13795RP VARIANT RP4 ILE-255 DEL. 13796RX MEDLINE=91090106; PubMed=1985460; 13797RA Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C., 13798RA Bhattacharya S.S.; 13799RT "A 3-bp deletion in the rhodopsin gene in a family with autosomal 13800RT dominant retinitis pigmentosa."; 13801RL Am. J. Hum. Genet. 48:26-30(1991). 13802RN [11] 13803RP VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267. 13804RX MEDLINE=91377732; PubMed=1897520; 13805RA Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.; 13806RT "Identification of novel rhodopsin mutations associated with retinitis 13807RT pigmentosa by GC-clamped denaturing gradient gel electrophoresis."; 13808RL Am. J. Hum. Genet. 49:699-706(1991). 13809RN [12] 13810RP VARIANT RP4 ARG-347. 13811RX MEDLINE=92120672; PubMed=1840561; 13812RA Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E., 13813RA Schinzel A.; 13814RT "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant 13815RT retinitis pigmentosa."; 13816RL Genomics 11:468-470(1991). 13817RN [13] 13818RP VARIANTS RP4. 13819RX MEDLINE=91319709; PubMed=1862076; DOI=10.1073/pnas.88.15.6481; 13820RA Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., 13821RA Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G., 13822RA Gouras P., Nathans J.; 13823RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa."; 13824RL Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991). 13825RN [14] 13826RP VARIANTS RP4. 13827RX MEDLINE=92021049; PubMed=1833777; DOI=10.1073/pnas.88.20.9370; 13828RA Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.; 13829RT "Mutation spectrum of the rhodopsin gene among patients with autosomal 13830RT dominant retinitis pigmentosa."; 13831RL Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991). 13832RN [15] 13833RP VARIANT RP4 ARG-207. 13834RX MEDLINE=93258325; PubMed=1302614; DOI=10.1093/hmg/1.9.769; 13835RA Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M., 13836RA Sharpe E., Humphries P.; 13837RT "Autosomal dominant retinitis pigmentosa: a novel mutation in the 13838RT rhodopsin gene in the original 3q linked family."; 13839RL Hum. Mol. Genet. 1:769-771(1992). 13840RN [16] 13841RP VARIANTS RP4 MET-17 AND LEU-347. 13842RX MEDLINE=93004784; PubMed=1391967; DOI=10.1007/BF01899733; 13843RA Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., 13844RA Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., 13845RA Kanai A.; 13846RT "Point mutations of rhodopsin gene found in Japanese families with 13847RT autosomal dominant retinitis pigmentosa (ADRP)."; 13848RL Jpn. J. Hum. Genet. 37:125-132(1992). 13849RN [17] 13850RP VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND 13851RP VARIANTS ALA-51; ILE-104 AND MET-209. 13852RX MEDLINE=93304432; PubMed=8317502; 13853RA Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C., 13854RA Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R., 13855RA Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.; 13856RT "Identification of novel rhodopsin mutations responsible for retinitis 13857RT pigmentosa: implications for the structure and function of 13858RT rhodopsin."; 13859RL Am. J. Hum. Genet. 53:80-89(1993). 13860RN [18] 13861RP VARIANT RP4 SER-15. 13862RX MEDLINE=93357759; PubMed=8353500; DOI=10.1093/hmg/2.6.813; 13863RA Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P., 13864RA Duvigneau C., Gal A.; 13865RT "Autosomal dominant 'sector' retinitis pigmentosa due to a point 13866RT mutation predicting an Asn-15-Ser substitution of rhodopsin."; 13867RL Hum. Mol. Genet. 2:813-814(1993). 13868RN [19] 13869RP VARIANT CSNBAD1 GLU-292. 13870RX MEDLINE=93364423; PubMed=8358437; DOI=10.1038/ng0793-280; 13871RA Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.; 13872RT "Heterozygous missense mutation in the rhodopsin gene as a cause of 13873RT congenital stationary night blindness."; 13874RL Nat. Genet. 4:280-283(1993). 13875RN [20] 13876RP VARIANTS RP4. 13877RX MEDLINE=94375083; PubMed=8088850; DOI=10.1006/geno.1994.1301; 13878RA Vaithinathan R., Berson E.L., Dryja T.P.; 13879RT "Further screening of the rhodopsin gene in patients with autosomal 13880RT dominant retinitis pigmentosa."; 13881RL Genomics 21:461-463(1994). 13882RN [21] 13883RP VARIANT RP4 THR-44. 13884RX MEDLINE=94357587; PubMed=8076945; DOI=10.1007/BF00208284; 13885RA Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C., 13886RA Carballo M.; 13887RT "Identification of a novel rhodopsin mutation (Met-44-Thr) in a 13888RT simplex case of retinitis pigmentosa."; 13889RL Hum. Genet. 94:283-286(1994). 13890RN [22] 13891RP VARIANTS RP4 PHE-110; PRO-131 AND VAL-164. 13892RX MEDLINE=95072600; PubMed=7981701; DOI=10.1093/hmg/3.7.1203; 13893RA Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S., 13894RA Humphries P., Gal A.; 13895RT "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients 13896RT with autosomal dominant retinitis pigmentosa."; 13897RL Hum. Mol. Genet. 3:1203-1203(1994). 13898RN [23] 13899RP VARIANT RP4 GLN-171. 13900RX MEDLINE=95078852; PubMed=7987326; DOI=10.1093/hmg/3.8.1421; 13901RA Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., 13902RA Cabeza J.C.; 13903RT "Identification of a new mutation at codon 171 of rhodopsin gene 13904RT causing autosomal dominant retinitis pigmentosa."; 13905RL Hum. Mol. Genet. 3:1421-1421(1994). 13906RN [24] 13907RP VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297. 13908RX MEDLINE=95078858; PubMed=7987331; DOI=10.1093/hmg/3.8.1433; 13909RA Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I., 13910RA Philip N., Soubrane G., Coscas G., Munnich A.; 13911RT "Five novel missense mutations of the rhodopsin gene in autosomal 13912RT dominant retinitis pigmentosa."; 13913RL Hum. Mol. Genet. 3:1433-1434(1994). 13914RN [25] 13915RP VARIANTS RP4 ARG-40 AND LYS-216. 13916RX MEDLINE=94362717; PubMed=8081400; DOI=10.1002/humu.1380030417; 13917RA Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., 13918RA Bhattacharya S.; 13919RT "Two new rhodopsin transversion mutations (L40R; M216K) in families 13920RT with autosomal dominant retinitis pigmentosa."; 13921RL Hum. Mutat. 3:409-410(1994). 13922RN [26] 13923RP VARIANT RP4 LEU-345. 13924RX MEDLINE=94321123; PubMed=8045708; 13925RA Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.; 13926RT "Autosomal dominant retinitis pigmentosa in a large family: a clinical 13927RT and molecular genetic study."; 13928RL Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994). 13929RN [27] 13930RP VARIANT ARRP LYS-150. 13931RX MEDLINE=95078913; PubMed=7987385; DOI=10.1038/ng0994-10; 13932RA Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R., 13933RA Orth U., Oehlmann R., Gal A.; 13934RT "Missense rhodopsin mutation in a family with recessive RP."; 13935RL Nat. Genet. 8:10-11(1994). 13936RN [28] 13937RP VARIANT RP4 ALA-347. 13938RX MEDLINE=95359993; PubMed=7633434; DOI=10.1093/hmg/4.4.775; 13939RA Macke J.P., Hennessey J.C., Nathans J.; 13940RT "Rhodopsin mutation proline347-to-alanine in a family with autosomal 13941RT dominant retinitis pigmentosa indicates an important role for proline 13942RT at position 347."; 13943RL Hum. Mol. Genet. 4:775-776(1995). 13944RN [29] 13945RP VARIANT CSNBAD1 ASP-90. 13946RX MEDLINE=95148641; PubMed=7846071; DOI=10.1073/pnas.92.3.880; 13947RA Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., 13948RA Alpern M.; 13949RT "Dark-light: model for nightblindness from the human rhodopsin Gly- 13950RT 90-->Asp mutation."; 13951RL Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995). 13952RN [30] 13953RP VARIANT RP4 TRP-135. 13954RX MEDLINE=96142043; PubMed=8554077; 13955RA Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., 13956RA Munnich A., Kaplan J.; 13957RT "Retinitis punctata albescens associated with the Arg135Trp mutation 13958RT in the rhodopsin gene."; 13959RL Am. J. Ophthalmol. 121:19-25(1996). 13960RN [31] 13961RP VARIANT RP4 ARG-109. 13962RX MEDLINE=98112414; PubMed=9452035; 13963RA Goliath R., Bardien S., September A., Martin R., Ramesar R., 13964RA Greenberg J.; 13965RT "Rhodopsin mutation G109R in a family with autosomal dominant 13966RT retinitis pigmentosa."; 13967RL Hum. Mutat. Suppl. 1:S40-S41(1998). 13968RN [32] 13969RP VARIANT CSNBAD1 ILE-94. 13970RX MEDLINE=99103467; PubMed=9888392; 13971RX DOI=10.1002/(SICI)1098-1004(1999)13:1<75::AID-HUMU9>3.0.CO;2-4; 13972RA Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N., 13973RA Findlay J.B.C., Humphries P., Kenna P.F.; 13974RT "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing 13975RT autosomal dominant congenital stationary night blindness."; 13976RL Hum. Mutat. 13:75-81(1999). 13977RN [33] 13978RP CHARACTERIZATION OF VARIANT RP4 HIS-23, AND SUBCELLULAR LOCATION. 13979RX PubMed=19934218; DOI=10.1242/jcs.055228; 13980RA Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.; 13981RT "A dual role for EDEM1 in the processing of rod opsin."; 13982RL J. Cell Sci. 122:4465-4472(2009). 13983RN [34] 13984RP VARIANT RP4 LYS-150. 13985RX PubMed=19960070; 13986RA Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., 13987RA Sadeque A., Bokhari H., Collin R.W., Orth U., van Genderen M.M., 13988RA den Hollander A.I., Cremers F.P., Qamar R.; 13989RT "A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani 13990RT families with autosomal recessive retinitis pigmentosa."; 13991RL Mol. Vis. 15:2526-2534(2009). 13992CC -!- FUNCTION: Photoreceptor required for image-forming vision at low 13993CC light intensity. Required for photoreceptor cell viability after 13994CC birth. Light-induced isomerization of 11-cis to all-trans retinal 13995CC triggers a conformational change leading to G-protein activation 13996CC and release of all-trans retinal. 13997CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 13998CC Absorption: 13999CC Abs(max)=495 nm; 14000CC -!- SUBUNIT: Homodimer (By similarity). 14001CC -!- INTERACTION: 14002CC O95405:ZFYVE9; NbExp=2; IntAct=EBI-1394177, EBI-296817; 14003CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 14004CC Note=Synthesized in the inner segment (IS) of rod photoreceptor 14005CC cells before vectorial transport to the rod outer segment (OS) 14006CC photosensory cilia. 14007CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates 14008CC vision in dim light. 14009CC -!- PTM: Phosphorylated on some or all of the serine and threonine 14010CC residues present in the C-terminal region. 14011CC -!- PTM: Contains one covalently linked retinal chromophore (By 14012CC similarity). 14013CC -!- DISEASE: Defects in RHO are the cause of retinitis pigmentosa type 14014CC 4 (RP4) [MIM:613731]. RP leads to degeneration of retinal 14015CC photoreceptor cells. Patients typically have night vision 14016CC blindness and loss of midperipheral visual field. As their 14017CC condition progresses, they lose their far peripheral visual field 14018CC and eventually central vision as well. 14019CC -!- DISEASE: Defects in RHO are the cause of congenital stationary 14020CC night blindness autosomal dominant type 1 (CSNBAD1) [MIM:610445]; 14021CC also known as rhodopsin-related congenital stationary night 14022CC blindness. Congenital stationary night blindness is a non- 14023CC progressive retinal disorder characterized by impaired night 14024CC vision. 14025CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 14026CC Opsin subfamily. 14027CC -!- WEB RESOURCE: Name=Mutations of the RHO gene; Note=Retina 14028CC International's Scientific Newsletter; 14029CC URL="http://www.retina-international.org/files/sci-news/rhomut.htm"; 14030CC -!- WEB RESOURCE: Name=GeneReviews; 14031CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/RHO"; 14032CC -!- WEB RESOURCE: Name=Wikipedia; Note=Rhodopsin entry; 14033CC URL="http://en.wikipedia.org/wiki/Rhodopsin"; 14034CC ----------------------------------------------------------------------- 14035CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 14036CC Distributed under the Creative Commons Attribution-NoDerivs License 14037CC ----------------------------------------------------------------------- 14038DR EMBL; U49742; AAC31763.1; -; Genomic_DNA. 14039DR EMBL; AB065668; BAC05894.1; -; Genomic_DNA. 14040DR EMBL; BX537381; CAD97623.1; -; mRNA. 14041DR EMBL; BC112104; AAI12105.1; -; mRNA. 14042DR EMBL; BC112106; AAI12107.1; -; mRNA. 14043DR EMBL; U16824; AAA97436.1; -; Genomic_DNA. 14044DR EMBL; S81166; AAB35906.1; -; Genomic_DNA. 14045DR IPI; IPI00027391; -. 14046DR PIR; A41200; OOHU. 14047DR RefSeq; NP_000530.1; NM_000539.3. 14048DR UniGene; Hs.247565; -. 14049DR ProteinModelPortal; P08100; -. 14050DR SMR; P08100; 1-348. 14051DR IntAct; P08100; 3. 14052DR STRING; P08100; -. 14053DR GlycoSuiteDB; P08100; -. 14054DR PhosphoSite; P08100; -. 14055DR DMDM; 129207; -. 14056DR PRIDE; P08100; -. 14057DR DNASU; 6010; -. 14058DR Ensembl; ENST00000296271; ENSP00000296271; ENSG00000163914. 14059DR GeneID; 6010; -. 14060DR KEGG; hsa:6010; -. 14061DR UCSC; uc003emt.3; human. 14062DR CTD; 6010; -. 14063DR GeneCards; GC03P129247; -. 14064DR HGNC; HGNC:10012; RHO. 14065DR MIM; 180380; gene. 14066DR MIM; 610445; phenotype. 14067DR MIM; 613731; phenotype. 14068DR neXtProt; NX_P08100; -. 14069DR Orphanet; 215; Congenital stationary night blindness. 14070DR Orphanet; 791; Retinitis pigmentosa. 14071DR Orphanet; 52427; Retinitis punctata albescens. 14072DR PharmGKB; PA34390; -. 14073DR eggNOG; NOG311294; -. 14074DR GeneTree; ENSGT00550000074069; -. 14075DR HOGENOM; HOG000253932; -. 14076DR HOVERGEN; HBG107442; -. 14077DR InParanoid; P08100; -. 14078DR KO; K04250; -. 14079DR OMA; KSSSIYN; -. 14080DR OrthoDB; EOG4P5K9D; -. 14081DR PhylomeDB; P08100; -. 14082DR Pathway_Interaction_DB; rhodopsin_pathway; Visual signal transduction: Rods. 14083DR Reactome; REACT_111102; Signal Transduction. 14084DR DrugBank; DB01159; Halothane. 14085DR NextBio; 23449; -. 14086DR ArrayExpress; P08100; -. 14087DR Bgee; P08100; -. 14088DR CleanEx; HS_RHO; -. 14089DR Genevestigator; P08100; -. 14090DR GermOnline; ENSG00000163914; Homo sapiens. 14091DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. 14092DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. 14093DR GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:UniProtKB. 14094DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB. 14095DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc. 14096DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 14097DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 14098DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. 14099DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 14100DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:ProtInc. 14101DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 14102DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 14103DR InterPro; IPR001760; Opsin. 14104DR InterPro; IPR000732; Rhodopsin. 14105DR InterPro; IPR019477; Rhodopsin_N. 14106DR Pfam; PF00001; 7tm_1; 1. 14107DR Pfam; PF10413; Rhodopsin_N; 1. 14108DR PRINTS; PR00237; GPCRRHODOPSN. 14109DR PRINTS; PR00238; OPSIN. 14110DR PRINTS; PR00579; RHODOPSIN. 14111DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 14112DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 14113DR PROSITE; PS00238; OPSIN; 1. 14114PE 1: Evidence at protein level; 14115KW Acetylation; Chromophore; Complete proteome; 14116KW Congenital stationary night blindness; Disease mutation; 14117KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein; 14118KW Membrane; Metal-binding; Palmitate; Phosphoprotein; 14119KW Photoreceptor protein; Polymorphism; Receptor; Reference proteome; 14120KW Retinal protein; Retinitis pigmentosa; Sensory transduction; 14121KW Transducer; Transmembrane; Transmembrane helix; Vision; Zinc. 14122FT CHAIN 1 348 Rhodopsin. 14123FT /FTId=PRO_0000197677. 14124FT TOPO_DOM 1 36 Extracellular. 14125FT TRANSMEM 37 61 Helical; Name=1; (Potential). 14126FT TOPO_DOM 62 73 Cytoplasmic. 14127FT TRANSMEM 74 98 Helical; Name=2; (Potential). 14128FT TOPO_DOM 99 113 Extracellular. 14129FT TRANSMEM 114 133 Helical; Name=3; (Potential). 14130FT TOPO_DOM 134 152 Cytoplasmic. 14131FT TRANSMEM 153 176 Helical; Name=4; (Potential). 14132FT TOPO_DOM 177 202 Extracellular. 14133FT TRANSMEM 203 230 Helical; Name=5; (Potential). 14134FT TOPO_DOM 231 252 Cytoplasmic. 14135FT TRANSMEM 253 276 Helical; Name=6; (Potential). 14136FT TOPO_DOM 277 284 Extracellular. 14137FT TRANSMEM 285 309 Helical; Name=7; (Potential). 14138FT TOPO_DOM 310 348 Cytoplasmic. 14139FT REGION 113 125 Retinal chromophore binding (By 14140FT similarity). 14141FT REGION 207 212 Retinal chromophore binding (By 14142FT similarity). 14143FT MOTIF 134 137 'Ionic lock' involved in activated form 14144FT stabilization. 14145FT METAL 201 201 Zinc (By similarity). 14146FT METAL 279 279 Zinc (By similarity). 14147FT BINDING 265 265 Retinal chromophore (By similarity). 14148FT BINDING 296 296 Retinal chromophore (covalent) (By 14149FT similarity). 14150FT MOD_RES 1 1 N-acetylmethionine (By similarity). 14151FT MOD_RES 296 296 N6-(retinylidene)lysine. 14152FT MOD_RES 334 334 Phosphoserine (By similarity). 14153FT MOD_RES 336 336 Phosphothreonine (By similarity). 14154FT MOD_RES 338 338 Phosphoserine (By similarity). 14155FT MOD_RES 340 340 Phosphothreonine (By similarity). 14156FT MOD_RES 342 342 Phosphothreonine (By similarity). 14157FT MOD_RES 343 343 Phosphoserine (By similarity). 14158FT LIPID 322 322 S-palmitoyl cysteine (By similarity). 14159FT LIPID 323 323 S-palmitoyl cysteine (By similarity). 14160FT CARBOHYD 2 2 N-linked (GlcNAc...) (By similarity). 14161FT CARBOHYD 15 15 N-linked (GlcNAc...) (By similarity). 14162FT DISULFID 110 187 By similarity. 14163FT VARIANT 4 4 T -> K (in RP4). 14164FT /FTId=VAR_004765. 14165FT VARIANT 15 15 N -> S (in RP4). 14166FT /FTId=VAR_004766. 14167FT VARIANT 17 17 T -> M (in RP4). 14168FT /FTId=VAR_004767. 14169FT VARIANT 23 23 P -> H (in RP4; most common variant, 14170FT leads to interaction with EDEM1 followed 14171FT by degradation by the ERAD system). 14172FT /FTId=VAR_004768. 14173FT VARIANT 23 23 P -> L (in RP4). 14174FT /FTId=VAR_004769. 14175FT VARIANT 28 28 Q -> H (in RP4). 14176FT /FTId=VAR_004770. 14177FT VARIANT 40 40 L -> R (in RP4). 14178FT /FTId=VAR_004771. 14179FT VARIANT 44 44 M -> T (in RP4). 14180FT /FTId=VAR_004772. 14181FT VARIANT 45 45 F -> L (in RP4). 14182FT /FTId=VAR_004773. 14183FT VARIANT 46 46 L -> R (in RP4). 14184FT /FTId=VAR_004774. 14185FT VARIANT 51 51 G -> A. 14186FT /FTId=VAR_004775. 14187FT VARIANT 51 51 G -> R (in RP4). 14188FT /FTId=VAR_004776. 14189FT VARIANT 51 51 G -> V (in RP4). 14190FT /FTId=VAR_004777. 14191FT VARIANT 53 53 P -> R (in RP4; dbSNP:rs28933395). 14192FT /FTId=VAR_004778. 14193FT VARIANT 58 58 T -> R (in RP4; dbSNP:rs28933394). 14194FT /FTId=VAR_004779. 14195FT VARIANT 68 71 Missing (in RP4). 14196FT /FTId=VAR_004780. 14197FT VARIANT 87 87 V -> D (in RP4). 14198FT /FTId=VAR_004781. 14199FT VARIANT 89 89 G -> D (in RP4). 14200FT /FTId=VAR_004782. 14201FT VARIANT 90 90 G -> D (in CSNBAD1). 14202FT /FTId=VAR_004783. 14203FT VARIANT 94 94 T -> I (in CSNBAD1). 14204FT /FTId=VAR_004784. 14205FT VARIANT 104 104 V -> I. 14206FT /FTId=VAR_004785. 14207FT VARIANT 106 106 G -> R (in RP4; dbSNP:rs28933994). 14208FT /FTId=VAR_004786. 14209FT VARIANT 106 106 G -> W (in RP4). 14210FT /FTId=VAR_004787. 14211FT VARIANT 109 109 G -> R (in RP4). 14212FT /FTId=VAR_004788. 14213FT VARIANT 110 110 C -> F (in RP4). 14214FT /FTId=VAR_004789. 14215FT VARIANT 110 110 C -> Y (in RP4). 14216FT /FTId=VAR_004790. 14217FT VARIANT 114 114 G -> D (in RP4). 14218FT /FTId=VAR_004791. 14219FT VARIANT 125 125 L -> R (in RP4). 14220FT /FTId=VAR_004792. 14221FT VARIANT 127 127 S -> F (in RP4). 14222FT /FTId=VAR_004793. 14223FT VARIANT 131 131 L -> P (in RP4). 14224FT /FTId=VAR_004794. 14225FT VARIANT 135 135 R -> G (in RP4). 14226FT /FTId=VAR_004795. 14227FT VARIANT 135 135 R -> L (in RP4). 14228FT /FTId=VAR_004796. 14229FT VARIANT 135 135 R -> W (in RP4). 14230FT /FTId=VAR_004797. 14231FT VARIANT 140 140 C -> S (in RP4). 14232FT /FTId=VAR_004798. 14233FT VARIANT 150 150 E -> K (in RP4; autosomal recessive). 14234FT /FTId=VAR_004799. 14235FT VARIANT 164 164 A -> E (in RP4). 14236FT /FTId=VAR_004800. 14237FT VARIANT 164 164 A -> V (in RP4). 14238FT /FTId=VAR_004801. 14239FT VARIANT 167 167 C -> R (in RP4). 14240FT /FTId=VAR_004802. 14241FT VARIANT 171 171 P -> L (in RP4). 14242FT /FTId=VAR_004803. 14243FT VARIANT 171 171 P -> Q (in RP4). 14244FT /FTId=VAR_004804. 14245FT VARIANT 171 171 P -> S (in RP4). 14246FT /FTId=VAR_004805. 14247FT VARIANT 178 178 Y -> C (in RP4). 14248FT /FTId=VAR_004806. 14249FT VARIANT 178 178 Y -> N (in RP4). 14250FT /FTId=VAR_004807. 14251FT VARIANT 181 181 E -> K (in RP4). 14252FT /FTId=VAR_004808. 14253FT VARIANT 182 182 G -> S (in RP4). 14254FT /FTId=VAR_004809. 14255FT VARIANT 186 186 S -> P (in RP4). 14256FT /FTId=VAR_004810. 14257FT VARIANT 188 188 G -> E (in RP4). 14258FT /FTId=VAR_004811. 14259FT VARIANT 188 188 G -> R (in RP4). 14260FT /FTId=VAR_004812. 14261FT VARIANT 190 190 D -> G (in RP4). 14262FT /FTId=VAR_004814. 14263FT VARIANT 190 190 D -> N (in RP4; dbSNP:rs28933992). 14264FT /FTId=VAR_004813. 14265FT VARIANT 190 190 D -> Y (in RP4). 14266FT /FTId=VAR_004815. 14267FT VARIANT 207 207 M -> R (in RP4; dbSNP:rs28933995). 14268FT /FTId=VAR_004816. 14269FT VARIANT 209 209 V -> M (effect not known). 14270FT /FTId=VAR_004817. 14271FT VARIANT 211 211 H -> P (in RP4; dbSNP:rs28933993). 14272FT /FTId=VAR_004818. 14273FT VARIANT 211 211 H -> R (in RP4). 14274FT /FTId=VAR_004819. 14275FT VARIANT 216 216 M -> K (in RP4). 14276FT /FTId=VAR_004820. 14277FT VARIANT 220 220 F -> C (in RP4). 14278FT /FTId=VAR_004821. 14279FT VARIANT 222 222 C -> R (in RP4). 14280FT /FTId=VAR_004822. 14281FT VARIANT 255 255 Missing (in RP4). 14282FT /FTId=VAR_004823. 14283FT VARIANT 264 264 Missing (in RP4). 14284FT /FTId=VAR_004824. 14285FT VARIANT 267 267 P -> L (in RP4). 14286FT /FTId=VAR_004825. 14287FT VARIANT 267 267 P -> R (in RP4). 14288FT /FTId=VAR_004826. 14289FT VARIANT 292 292 A -> E (in CSNBAD1). 14290FT /FTId=VAR_004827. 14291FT VARIANT 296 296 K -> E (in RP4; dbSNP:rs29001653). 14292FT /FTId=VAR_004828. 14293FT VARIANT 297 297 S -> R (in RP4). 14294FT /FTId=VAR_004829. 14295FT VARIANT 342 342 T -> M (in RP4). 14296FT /FTId=VAR_004830. 14297FT VARIANT 345 345 V -> L (in RP4). 14298FT /FTId=VAR_004831. 14299FT VARIANT 345 345 V -> M (in RP4). 14300FT /FTId=VAR_004832. 14301FT VARIANT 347 347 P -> A (in RP4). 14302FT /FTId=VAR_004833. 14303FT VARIANT 347 347 P -> L (in RP4; common variant). 14304FT /FTId=VAR_004834. 14305FT VARIANT 347 347 P -> Q (in RP4). 14306FT /FTId=VAR_004835. 14307FT VARIANT 347 347 P -> R (in RP4; dbSNP:rs29001566). 14308FT /FTId=VAR_004836. 14309FT VARIANT 347 347 P -> S (in RP4; dbSNP:rs29001637). 14310FT /FTId=VAR_004837. 14311SQ SEQUENCE 348 AA; 38893 MW; 6F4F6FCBA34265B2 CRC64; 14312 MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY 14313 VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG 14314 GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP 14315 EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES 14316 ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI 14317 YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA 14318// 14319ID OPSD_XENLA Reviewed; 354 AA. 14320AC P29403; 14321DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. 14322DT 01-APR-1993, sequence version 1. 14323DT 30-NOV-2010, entry version 75. 14324DE RecName: Full=Rhodopsin; 14325GN Name=rho; 14326OS Xenopus laevis (African clawed frog). 14327OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 14328OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; 14329OC Xenopodinae; Xenopus; Xenopus. 14330OX NCBI_TaxID=8355; 14331RN [1] 14332RP NUCLEOTIDE SEQUENCE [MRNA]. 14333RX MEDLINE=93287804; PubMed=8510503; DOI=10.1016/0169-328X(93)90016-I; 14334RA Saha M.S., Grainger R.M.; 14335RT "Early opsin expression in Xenopus embryos precedes photoreceptor 14336RT differentiation."; 14337RL Brain Res. Mol. Brain Res. 17:307-318(1993). 14338RN [2] 14339RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 14340RX MEDLINE=96216396; PubMed=8621718; DOI=10.1074/jbc.271.6.3179; 14341RA Batni S., Scalzetti L.C., Moody S.A., Knox B.E.; 14342RT "Characterization of the Xenopus rhodopsin gene."; 14343RL J. Biol. Chem. 271:3179-3186(1996). 14344CC -!- FUNCTION: Visual pigments such as rhodopsin and porphyropsin are 14345CC light-absorbing molecules that mediate vision. Rhodopsin consists 14346CC of an apoprotein, opsin, covalently linked to 11-cis-retinal. This 14347CC receptor is coupled to the activation of phospholipase C. 14348CC Porphyropsin consists of opsin covalently linked to 11-cis 3,4- 14349CC didehydroretinal. 14350CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 14351CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates 14352CC vision in dim light. 14353CC -!- PTM: Phosphorylated on some or all of the serine and threonine 14354CC residues present in the C-terminal region. 14355CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 14356CC Opsin subfamily. 14357CC ----------------------------------------------------------------------- 14358CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 14359CC Distributed under the Creative Commons Attribution-NoDerivs License 14360CC ----------------------------------------------------------------------- 14361DR EMBL; S62229; AAB27128.2; -; mRNA. 14362DR EMBL; L04692; AAB59950.1; -; mRNA. 14363DR EMBL; L07770; AAC42232.1; -; mRNA. 14364DR EMBL; U23808; AAC59901.1; -; Genomic_DNA. 14365DR PIR; I51200; I51200. 14366DR UniGene; Xl.326; -. 14367DR ProteinModelPortal; P29403; -. 14368DR SMR; P29403; 1-354. 14369DR MINT; MINT-6824795; -. 14370DR Xenbase; XB-GENE-966893; rho. 14371DR HOVERGEN; HBG107442; -. 14372DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 14373DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 14374DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 14375DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 14376DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 14377DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 14378DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 14379DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 14380DR InterPro; IPR001760; Opsin. 14381DR InterPro; IPR000732; Rhodopsin. 14382DR InterPro; IPR019477; Rhodopsin_N. 14383DR Pfam; PF00001; 7tm_1; 1. 14384DR Pfam; PF10413; Rhodopsin_N; 1. 14385DR PRINTS; PR00237; GPCRRHODOPSN. 14386DR PRINTS; PR00238; OPSIN. 14387DR PRINTS; PR00579; RHODOPSIN. 14388DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 14389DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 14390DR PROSITE; PS00238; OPSIN; 1. 14391PE 1: Evidence at protein level; 14392KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; 14393KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; 14394KW Photoreceptor protein; Receptor; Retinal protein; 14395KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix; 14396KW Vision. 14397FT CHAIN 1 354 Rhodopsin. 14398FT /FTId=PRO_0000197727. 14399FT TOPO_DOM 1 36 Extracellular. 14400FT TRANSMEM 37 61 Helical; Name=1; (Potential). 14401FT TOPO_DOM 62 73 Cytoplasmic. 14402FT TRANSMEM 74 98 Helical; Name=2; (Potential). 14403FT TOPO_DOM 99 113 Extracellular. 14404FT TRANSMEM 114 133 Helical; Name=3; (Potential). 14405FT TOPO_DOM 134 152 Cytoplasmic. 14406FT TRANSMEM 153 176 Helical; Name=4; (Potential). 14407FT TOPO_DOM 177 202 Extracellular. 14408FT TRANSMEM 203 230 Helical; Name=5; (Potential). 14409FT TOPO_DOM 231 252 Cytoplasmic. 14410FT TRANSMEM 253 276 Helical; Name=6; (Potential). 14411FT TOPO_DOM 277 284 Extracellular. 14412FT TRANSMEM 285 309 Helical; Name=7; (Potential). 14413FT TOPO_DOM 310 354 Cytoplasmic. 14414FT MOD_RES 296 296 N6-(retinylidene)lysine. 14415FT LIPID 322 322 S-palmitoyl cysteine (By similarity). 14416FT LIPID 323 323 S-palmitoyl cysteine (By similarity). 14417FT CARBOHYD 2 2 N-linked (GlcNAc...) (By similarity). 14418FT CARBOHYD 15 15 N-linked (GlcNAc...) (By similarity). 14419FT DISULFID 110 187 By similarity. 14420FT CONFLICT 107 107 P -> Q (in Ref. 2; AAC42232/AAC59901). 14421FT CONFLICT 137 137 I -> M (in Ref. 2; AAC42232/AAC59901). 14422FT CONFLICT 241 241 L -> A (in Ref. 2; AAC42232/AAC59901). 14423SQ SEQUENCE 354 AA; 39787 MW; CD18F49EC63D8FFE CRC64; 14424 MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF 14425 VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG 14426 GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP 14427 EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES 14428 LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI 14429 YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA 14430// 14431ID OPSO_LIMPO Reviewed; 376 AA. 14432AC P35361; 14433DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. 14434DT 01-JUN-1994, sequence version 1. 14435DT 21-SEP-2011, entry version 61. 14436DE RecName: Full=Ocellar opsin; 14437OS Limulus polyphemus (Atlantic horseshoe crab). 14438OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura; 14439OC Limulidae; Limulus. 14440OX NCBI_TaxID=6850; 14441RN [1] 14442RP NUCLEOTIDE SEQUENCE [MRNA]. 14443RC TISSUE=Median ocelli; 14444RX MEDLINE=93317641; PubMed=8327495; DOI=10.1073/pnas.90.13.6150; 14445RA Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.; 14446RT "Opsins from the lateral eyes and ocelli of the horseshoe crab, 14447RT Limulus polyphemus."; 14448RL Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993). 14449CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that 14450CC mediate vision. They consist of an apoprotein, opsin, covalently 14451CC linked to cis-retinal. 14452CC -!- BIOPHYSICOCHEMICAL PROPERTIES: 14453CC Absorption: 14454CC Abs(max)=530 nm; 14455CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. 14456CC -!- TISSUE SPECIFICITY: Ocellar cells; median ocelli. 14457CC -!- PTM: Phosphorylated on some or all of the serine and threonine 14458CC residues present in the C-terminal region (By similarity). 14459CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 14460CC Opsin subfamily. 14461CC ----------------------------------------------------------------------- 14462CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 14463CC Distributed under the Creative Commons Attribution-NoDerivs License 14464CC ----------------------------------------------------------------------- 14465DR EMBL; L03792; AAA28274.1; -; mRNA. 14466DR EMBL; L03782; AAA02499.1; -; mRNA. 14467DR PIR; A48197; A48197. 14468DR ProteinModelPortal; P35361; -. 14469DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 14470DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 14471DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. 14472DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW. 14473DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 14474DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW. 14475DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 14476DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 14477DR InterPro; IPR001760; Opsin. 14478DR InterPro; IPR001391; Opsin_lateye. 14479DR Pfam; PF00001; 7tm_1; 1. 14480DR PRINTS; PR00237; GPCRRHODOPSN. 14481DR PRINTS; PR00238; OPSIN. 14482DR PRINTS; PR00578; OPSINLTRLEYE. 14483DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 14484DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 14485DR PROSITE; PS00238; OPSIN; 1. 14486PE 1: Evidence at protein level; 14487KW Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein; 14488KW Membrane; Phosphoprotein; Photoreceptor protein; Receptor; 14489KW Retinal protein; Sensory transduction; Transducer; Transmembrane; 14490KW Transmembrane helix; Vision. 14491FT CHAIN 1 376 Ocellar opsin. 14492FT /FTId=PRO_0000197752. 14493FT TOPO_DOM 1 46 Extracellular. 14494FT TRANSMEM 47 71 Helical; Name=1; (Potential). 14495FT TOPO_DOM 72 83 Cytoplasmic. 14496FT TRANSMEM 84 108 Helical; Name=2; (Potential). 14497FT TOPO_DOM 109 123 Extracellular. 14498FT TRANSMEM 124 143 Helical; Name=3; (Potential). 14499FT TOPO_DOM 144 162 Cytoplasmic. 14500FT TRANSMEM 163 186 Helical; Name=4; (Potential). 14501FT TOPO_DOM 187 210 Extracellular. 14502FT TRANSMEM 211 238 Helical; Name=5; (Potential). 14503FT TOPO_DOM 239 274 Cytoplasmic. 14504FT TRANSMEM 275 298 Helical; Name=6; (Potential). 14505FT TOPO_DOM 299 306 Extracellular. 14506FT TRANSMEM 307 331 Helical; Name=7; (Potential). 14507FT TOPO_DOM 332 376 Cytoplasmic. 14508FT MOD_RES 318 318 N6-(retinylidene)lysine (By similarity). 14509FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). 14510FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential). 14511FT DISULFID 120 197 By similarity. 14512SQ SEQUENCE 376 AA; 42112 MW; FA9647C40531CBF8 CRC64; 14513 MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII 14514 CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC 14515 EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL 14516 PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE 14517 HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS 14518 SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE 14519 ASATMTMEEK PKSPEA 14520// 14521ID PAX1_HUMAN Reviewed; 534 AA. 14522AC P15863; B4E0D6; Q642X9; Q6NTC0; Q9Y558; 14523DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. 14524DT 18-MAY-2010, sequence version 4. 14525DT 13-JUN-2012, entry version 116. 14526DE RecName: Full=Paired box protein Pax-1; 14527DE AltName: Full=HuP48; 14528GN Name=PAX1; Synonyms=HUP48; 14529OS Homo sapiens (Human). 14530OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 14531OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 14532OC Catarrhini; Hominidae; Homo. 14533OX NCBI_TaxID=9606; 14534RN [1] 14535RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 14536RC TISSUE=Thymus; 14537RX PubMed=14702039; DOI=10.1038/ng1285; 14538RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., 14539RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., 14540RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., 14541RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., 14542RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., 14543RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., 14544RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., 14545RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., 14546RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., 14547RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., 14548RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., 14549RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., 14550RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., 14551RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., 14552RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., 14553RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., 14554RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., 14555RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., 14556RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., 14557RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., 14558RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., 14559RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., 14560RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., 14561RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., 14562RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., 14563RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., 14564RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., 14565RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; 14566RT "Complete sequencing and characterization of 21,243 full-length human 14567RT cDNAs."; 14568RL Nat. Genet. 36:40-45(2004). 14569RN [2] 14570RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS ARG-439; 14571RP LEU-453 AND LEU-504. 14572RG NIEHS SNPs program; 14573RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. 14574RN [3] 14575RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 14576RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; 14577RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., 14578RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., 14579RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., 14580RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., 14581RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., 14582RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., 14583RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., 14584RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., 14585RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., 14586RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., 14587RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., 14588RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., 14589RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., 14590RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., 14591RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., 14592RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., 14593RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., 14594RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., 14595RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., 14596RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., 14597RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., 14598RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., 14599RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., 14600RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 14601RA Rogers J.; 14602RT "The DNA sequence and comparative analysis of human chromosome 20."; 14603RL Nature 414:865-871(2001). 14604RN [4] 14605RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-534 (ISOFORM 1). 14606RX PubMed=15489334; DOI=10.1101/gr.2596504; 14607RG The MGC Project Team; 14608RT "The status, quality, and expansion of the NIH full-length cDNA 14609RT project: the Mammalian Gene Collection (MGC)."; 14610RL Genome Res. 14:2121-2127(2004). 14611RN [5] 14612RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2/3). 14613RX MEDLINE=89305521; PubMed=2501086; 14614RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; 14615RT "Conservation of the paired domain in metazoans and its structure in 14616RT three isolated human genes."; 14617RL EMBO J. 8:1183-1190(1989). 14618RN [6] 14619RP VARIANT HIS-139. 14620RX MEDLINE=97016531; PubMed=8863157; 14621RA Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R., 14622RA Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J., 14623RA Mariman E.C.M.; 14624RT "PAX genes and human neural tube defects: an amino acid substitution 14625RT in PAX1 in a patient with spina bifida."; 14626RL J. Med. Genet. 33:655-660(1996). 14627CC -!- FUNCTION: This protein is a transcriptional activator. It may play 14628CC a role in the formation of segmented structures of the embryo. May 14629CC play an important role in the normal development of the vertebral 14630CC column (By similarity). 14631CC -!- SUBCELLULAR LOCATION: Nucleus. 14632CC -!- ALTERNATIVE PRODUCTS: 14633CC Event=Alternative splicing; Named isoforms=3; 14634CC Name=1; 14635CC IsoId=P15863-1; Sequence=Displayed; 14636CC Name=2; 14637CC IsoId=P15863-2; Sequence=VSP_039095, VSP_039096; 14638CC Name=3; 14639CC IsoId=P15863-3; Sequence=VSP_039095; 14640CC Note=No experimental confirmation available; 14641CC -!- SIMILARITY: Contains 1 paired domain. 14642CC -!- SEQUENCE CAUTION: 14643CC Sequence=AAH69134.1; Type=Erroneous initiation; Note=Translation N-terminally extended; 14644CC Sequence=AAU21037.1; Type=Erroneous initiation; Note=Translation N-terminally extended; 14645CC -!- WEB RESOURCE: Name=NIEHS-SNPs; 14646CC URL="http://egp.gs.washington.edu/data/pax1/"; 14647CC ----------------------------------------------------------------------- 14648CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 14649CC Distributed under the Creative Commons Attribution-NoDerivs License 14650CC ----------------------------------------------------------------------- 14651DR EMBL; AK303335; BAG64398.1; -; mRNA. 14652DR EMBL; AY740018; AAU21037.1; ALT_INIT; Genomic_DNA. 14653DR EMBL; AL035562; CAX12115.1; -; Genomic_DNA. 14654DR EMBL; AL035562; CAB46996.2; -; Genomic_DNA. 14655DR EMBL; BC069134; AAH69134.1; ALT_INIT; mRNA. 14656DR EMBL; X15044; CAA33146.1; -; Genomic_DNA. 14657DR IPI; IPI00013473; -. 14658DR IPI; IPI00419577; -. 14659DR IPI; IPI00963849; -. 14660DR PIR; S06961; S06961. 14661DR RefSeq; NP_006183.2; NM_006192.4. 14662DR UniGene; Hs.349082; -. 14663DR ProteinModelPortal; P15863; -. 14664DR SMR; P15863; 102-224. 14665DR MINT; MINT-202824; -. 14666DR STRING; P15863; -. 14667DR DMDM; 296439493; -. 14668DR PRIDE; P15863; -. 14669DR Ensembl; ENST00000377123; ENSP00000366327; ENSG00000125813. 14670DR Ensembl; ENST00000398485; ENSP00000381499; ENSG00000125813. 14671DR Ensembl; ENST00000444366; ENSP00000410355; ENSG00000125813. 14672DR GeneID; 5075; -. 14673DR KEGG; hsa:5075; -. 14674DR UCSC; uc002wsj.2; human. 14675DR UCSC; uc010zsm.2; human. 14676DR CTD; 5075; -. 14677DR GeneCards; GC20P021634; -. 14678DR H-InvDB; HIX0040597; -. 14679DR HGNC; HGNC:8615; PAX1. 14680DR MIM; 167411; gene. 14681DR neXtProt; NX_P15863; -. 14682DR PharmGKB; PA32955; -. 14683DR eggNOG; NOG252808; -. 14684DR GeneTree; ENSGT00650000093055; -. 14685DR HOGENOM; HOG000230938; -. 14686DR HOVERGEN; HBG009115; -. 14687DR InParanoid; P15863; -. 14688DR KO; K09382; -. 14689DR OMA; AMAFKHP; -. 14690DR OrthoDB; EOG4W6NW9; -. 14691DR NextBio; 19556; -. 14692DR ArrayExpress; P15863; -. 14693DR Bgee; P15863; -. 14694DR CleanEx; HS_PAX1; -. 14695DR Genevestigator; P15863; -. 14696DR GermOnline; ENSG00000125813; Homo sapiens. 14697DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 14698DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 14699DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 14700DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 14701DR InterPro; IPR009057; Homeodomain-like. 14702DR InterPro; IPR001523; Paired_box_N. 14703DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 14704DR Pfam; PF00292; PAX; 1. 14705DR PRINTS; PR00027; PAIREDBOX. 14706DR SMART; SM00351; PAX; 1. 14707DR SUPFAM; SSF46689; Homeodomain_like; 1. 14708DR PROSITE; PS00034; PAIRED_1; 1. 14709DR PROSITE; PS51057; PAIRED_2; 1. 14710PE 2: Evidence at transcript level; 14711KW Activator; Alternative splicing; Complete proteome; 14712KW Developmental protein; DNA-binding; Nucleus; Paired box; Polymorphism; 14713KW Reference proteome; Transcription; Transcription regulation. 14714FT CHAIN 1 534 Paired box protein Pax-1. 14715FT /FTId=PRO_0000050172. 14716FT DOMAIN 98 224 Paired. 14717FT VAR_SEQ 1 95 MKFTLGLGSRAWRVSWEGAAAAAAGPGAGGSALRCRAQRVS 14718FT SPRLGRRGSRLSGALPLCLSRGGGGAQALPDCAGPSPGHPG 14719FT HPGARQLAGPLAM -> MRRAPLRGSSAPLPTPSQTQAVCP 14720FT WTPSCLGTHRSPLEVRLGAVPRSAWGPLANPPGVFSPSGSL 14721FT LSGASA (in isoform 2 and isoform 3). 14722FT /FTId=VSP_039095. 14723FT VAR_SEQ 428 534 GSLPAPAARPRTPSVAYTDCPSRPRPPRGSSPRTRARRERQ 14724FT ADPGAQVCAAAPAIGTGRIGGLAEEEASAGPRGARPASPQA 14725FT QPCLWPDPPHFLYWSGFLGFSELGF -> VADRKPPSSGSK 14726FT APDALSSLHGLPIPASTS (in isoform 2). 14727FT /FTId=VSP_039096. 14728FT VARIANT 139 139 Q -> H (in a patient with neural tube 14729FT defects, but not clearly linked to the 14730FT disease). 14731FT /FTId=VAR_003787. 14732FT VARIANT 439 439 T -> R (in dbSNP:rs17861058). 14733FT /FTId=VAR_055369. 14734FT VARIANT 453 453 P -> L (in dbSNP:rs17861059). 14735FT /FTId=VAR_055370. 14736FT VARIANT 504 504 P -> L (in dbSNP:rs17861061). 14737FT /FTId=VAR_055371. 14738SQ SEQUENCE 534 AA; 55499 MW; 6B06A2AD302FDEEA CRC64; 14739 MKFTLGLGSR AWRVSWEGAA AAAAGPGAGG SALRCRAQRV SSPRLGRRGS RLSGALPLCL 14740 SRGGGGAQAL PDCAGPSPGH PGHPGARQLA GPLAMEQTYG EVNQLGGVFV NGRPLPNAIR 14741 LRIVELAQLG IRPCDISRQL RVSHGCVSKI LARYNETGSI LPGAIGGSKP RVTTPNVVKH 14742 IRDYKQGDPG IFAWEIRDRL LADGVCDKYN VPSVSSISRI LRNKIGSLAQ PGPYEASKQP 14743 PSQPTLPYNH IYQYPYPSPV SPTGAKMGSH PGVPGTAGHV SIPRSWPSAH SVSNILGIRT 14744 FMEQTGALAG SEGTAYSPKM EDWAGVNRTA FPATPAVNGL EKPALEADIK YTQSASTLSA 14745 VGGFLPACAY PASNQHGVYS APGGGYLAPG PPWPPAQGPP LAPPGAGVAV HGGELAAAMT 14746 FKHPSREGSL PAPAARPRTP SVAYTDCPSR PRPPRGSSPR TRARRERQAD PGAQVCAAAP 14747 AIGTGRIGGL AEEEASAGPR GARPASPQAQ PCLWPDPPHF LYWSGFLGFS ELGF 14748// 14749ID PAX2_HUMAN Reviewed; 417 AA. 14750AC Q02962; Q15105; Q15110; Q15837; Q5SZP2; Q5SZP3; 14751DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. 14752DT 10-FEB-2009, sequence version 4. 14753DT 13-JUN-2012, entry version 133. 14754DE RecName: Full=Paired box protein Pax-2; 14755GN Name=PAX2; 14756OS Homo sapiens (Human). 14757OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 14758OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 14759OC Catarrhini; Hominidae; Homo. 14760OX NCBI_TaxID=9606; 14761RN [1] 14762RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). 14763RC TISSUE=Kidney; 14764RX MEDLINE=92338102; PubMed=1378753; 14765RA Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K., Goodfellow P.J., 14766RA Reeve A.E.; 14767RT "Expression of the PAX2 gene in human fetal kidney and Wilms' tumor."; 14768RL Cell Growth Differ. 3:279-289(1992). 14769RN [2] 14770RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). 14771RC TISSUE=Kidney cortex; 14772RX PubMed=7819127; 14773RA Ward T.A., Nebel A., Reeve A.E., Eccles M.R.; 14774RT "Alternative messenger RNA forms and open reading frames within an 14775RT additional conserved region of the human PAX-2 gene."; 14776RL Cell Growth Differ. 5:1015-1021(1994). 14777RN [3] 14778RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 14779RP 1). 14780RX MEDLINE=96299768; PubMed=8661132; DOI=10.1006/geno.1996.0350; 14781RA Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A., 14782RA Eccles M.R.; 14783RT "Genomic structure of the human PAX2 gene."; 14784RL Genomics 35:258-261(1996). 14785RN [4] 14786RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 14787RX PubMed=15164054; DOI=10.1038/nature02462; 14788RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., 14789RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., 14790RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., 14791RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., 14792RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., 14793RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., 14794RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., 14795RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., 14796RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., 14797RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., 14798RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., 14799RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., 14800RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., 14801RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., 14802RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., 14803RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., 14804RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., 14805RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., 14806RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., 14807RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., 14808RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., 14809RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., 14810RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., 14811RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., 14812RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., 14813RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; 14814RT "The DNA sequence and comparative analysis of human chromosome 10."; 14815RL Nature 429:375-381(2004). 14816RN [5] 14817RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 14818RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 14819RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 14820RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 14821RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 14822RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 14823RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 14824RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 14825RA Venter J.C.; 14826RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. 14827RN [6] 14828RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136. 14829RX MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292; 14830RA Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.; 14831RT "Chromosomal localization of seven PAX genes and cloning of a novel 14832RT family member, PAX-9."; 14833RL Nat. Genet. 3:292-298(1993). 14834RN [7] 14835RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, AND MASS 14836RP SPECTROMETRY. 14837RC TISSUE=Leukemic T-cell; 14838RX PubMed=19690332; DOI=10.1126/scisignal.2000007; 14839RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., 14840RA Rodionov V., Han D.K.; 14841RT "Quantitative phosphoproteomic analysis of T cell receptor signaling 14842RT reveals system-wide modulation of protein-protein interactions."; 14843RL Sci. Signal. 2:RA46-RA46(2009). 14844RN [8] 14845RP INTERACTION WITH EGLN3. 14846RX PubMed=21575608; DOI=10.1016/j.bbrc.2011.05.012; 14847RA Yan B., Jiao S., Zhang H.S., Lv D.D., Xue J., Fan L., Wu G.H., 14848RA Fang J.; 14849RT "Prolyl hydroxylase domain protein 3 targets Pax2 for destruction."; 14850RL Biochem. Biophys. Res. Commun. 409:315-320(2011). 14851RN [9] 14852RP VARIANTS RCS GLU-THR-75 INS AND SER-76. 14853RX MEDLINE=98430997; PubMed=9760197; DOI=10.1007/s004390050798; 14854RA Devriendt K., Matthijs G., van Damme B., van Caesbroeck D., 14855RA Eccles M.R., Vanrenterghem Y., Fryns J.-P., Leys A.; 14856RT "Missense mutation and hexanucleotide duplication in the PAX2 gene in 14857RT two unrelated families with renal-coloboma syndrome (MIM 120330)."; 14858RL Hum. Genet. 103:149-153(1998). 14859RN [10] 14860RP VARIANT VAL-334. 14861RX MEDLINE=21113232; PubMed=11180607; 14862RX DOI=10.1002/1098-1004(200102)17:2<155::AID-HUMU16>3.0.CO;2-9; 14863RA Gelb A.C., Manligas G.S., Gharaybeh S., Schimmenti L.A.; 14864RT "Identification of two novel polymorphisms (g.903C>T and g.1544C>T) in 14865RT the PAX2 gene."; 14866RL Hum. Mutat. 17:155-155(2001). 14867RN [11] 14868RP VARIANT OMN 39-GLN-ARG-40 DEL. 14869RX MEDLINE=21105676; PubMed=11168927; 14870RX DOI=10.1046/j.1523-1755.2001.059002457.x; 14871RA Salomon R., Tellier A.-L., Attie-Bitach T., Amiel J., Vekemans M., 14872RA Lyonnet S., Dureau P., Niaudet P., Gubler M.-C., Broyer M.; 14873RT "PAX2 mutations in oligomeganephronia."; 14874RL Kidney Int. 59:457-462(2001). 14875CC -!- FUNCTION: Probable transcription factor that may have a role in 14876CC kidney cell differentiation. Has a critical role in the 14877CC development of the urogenital tract, the eyes, and the CNS. 14878CC -!- SUBUNIT: Interacts with ELGN3; the interaction targets PAX2 for 14879CC destruction. 14880CC -!- SUBCELLULAR LOCATION: Nucleus. 14881CC -!- ALTERNATIVE PRODUCTS: 14882CC Event=Alternative splicing; Named isoforms=4; 14883CC Name=1; 14884CC IsoId=Q02962-1; Sequence=Displayed; 14885CC Name=2; Synonyms=Fetal kidney; 14886CC IsoId=Q02962-2; Sequence=VSP_002346; 14887CC Name=3; 14888CC IsoId=Q02962-3; Sequence=VSP_002345; 14889CC Name=4; 14890CC IsoId=Q02962-4; Sequence=VSP_002345, VSP_002346; 14891CC -!- TISSUE SPECIFICITY: Expressed in primitive cells of the kidney, 14892CC ureter, eye, ear and central nervous system. 14893CC -!- DEVELOPMENTAL STAGE: Mainly in fetal kidney and juvenile 14894CC nephrogenic rests. 14895CC -!- DISEASE: Defects in PAX2 are the cause of renal-coloboma syndrome 14896CC (RCS) [MIM:120330]; also known as papillorenal syndrome or optic 14897CC nerve coloboma with renal disease. RCS is an autosomal dominant 14898CC disease characterized by the association of renal hypoplasia, 14899CC vesicoureteral reflux and dysplasia of the retina and optic disk. 14900CC -!- DISEASE: Note=Defects in PAX2 may be responsible for isolated 14901CC renal hypoplasia as observed in oligomeganephronia, a rare 14902CC congenital and usually sporadic anomaly characterized by bilateral 14903CC renal hypoplasia, with a reduced number of enlarged nephrons and 14904CC without urinary tract abnormalities. 14905CC -!- SIMILARITY: Contains 1 paired domain. 14906CC -!- WEB RESOURCE: Name=PAX2 mutation db; 14907CC URL="http://www.hgu.mrc.ac.uk/Softdata/PAX2/"; 14908CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology 14909CC and Haematology; 14910CC URL="http://atlasgeneticsoncology.org/Genes/PAX2ID41642ch10q24.html"; 14911CC -!- WEB RESOURCE: Name=GeneReviews; 14912CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX2"; 14913CC ----------------------------------------------------------------------- 14914CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 14915CC Distributed under the Creative Commons Attribution-NoDerivs License 14916CC ----------------------------------------------------------------------- 14917DR EMBL; M89470; AAA60024.1; -; mRNA. 14918DR EMBL; L25597; AAA36417.1; -; mRNA. 14919DR EMBL; U45255; AAC63385.1; -; Genomic_DNA. 14920DR EMBL; U45245; AAC63385.1; JOINED; Genomic_DNA. 14921DR EMBL; U45246; AAC63385.1; JOINED; Genomic_DNA. 14922DR EMBL; U45247; AAC63385.1; JOINED; Genomic_DNA. 14923DR EMBL; U45248; AAC63385.1; JOINED; Genomic_DNA. 14924DR EMBL; U45249; AAC63385.1; JOINED; Genomic_DNA. 14925DR EMBL; U45250; AAC63385.1; JOINED; Genomic_DNA. 14926DR EMBL; U45251; AAC63385.1; JOINED; Genomic_DNA. 14927DR EMBL; U45253; AAC63385.1; JOINED; Genomic_DNA. 14928DR EMBL; U45254; AAC63385.1; JOINED; Genomic_DNA. 14929DR EMBL; AL138762; CAH70951.1; -; Genomic_DNA. 14930DR EMBL; AL589862; CAH70951.1; JOINED; Genomic_DNA. 14931DR EMBL; AL138762; CAH70952.1; -; Genomic_DNA. 14932DR EMBL; AL589862; CAH70952.1; JOINED; Genomic_DNA. 14933DR EMBL; AL589862; CAI17855.1; -; Genomic_DNA. 14934DR EMBL; AL138762; CAI17855.1; JOINED; Genomic_DNA. 14935DR EMBL; AL589862; CAI17856.1; -; Genomic_DNA. 14936DR EMBL; AL138762; CAI17856.1; JOINED; Genomic_DNA. 14937DR EMBL; CH471066; EAW49812.1; -; Genomic_DNA. 14938DR EMBL; CH471066; EAW49813.1; -; Genomic_DNA. 14939DR EMBL; L09747; AAC41711.1; -; Genomic_DNA. 14940DR EMBL; L09748; AAC41711.1; JOINED; Genomic_DNA. 14941DR EMBL; L09746; AAC41711.1; JOINED; Genomic_DNA. 14942DR IPI; IPI00179609; -. 14943DR IPI; IPI00220545; -. 14944DR IPI; IPI00375134; -. 14945DR IPI; IPI00395548; -. 14946DR PIR; A49008; A49008. 14947DR RefSeq; NP_000269.2; NM_000278.3. 14948DR RefSeq; NP_003978.2; NM_003987.3. 14949DR RefSeq; NP_003979.2; NM_003988.3. 14950DR RefSeq; NP_003980.2; NM_003989.3. 14951DR RefSeq; NP_003981.2; NM_003990.3. 14952DR UniGene; Hs.155644; -. 14953DR ProteinModelPortal; Q02962; -. 14954DR SMR; Q02962; 19-142, 250-311. 14955DR IntAct; Q02962; 4. 14956DR STRING; Q02962; -. 14957DR PhosphoSite; Q02962; -. 14958DR DMDM; 223590261; -. 14959DR PRIDE; Q02962; -. 14960DR DNASU; 5076; -. 14961DR Ensembl; ENST00000355243; ENSP00000347385; ENSG00000075891. 14962DR Ensembl; ENST00000361791; ENSP00000355069; ENSG00000075891. 14963DR Ensembl; ENST00000370294; ENSP00000359317; ENSG00000075891. 14964DR Ensembl; ENST00000370296; ENSP00000359319; ENSG00000075891. 14965DR Ensembl; ENST00000428433; ENSP00000396259; ENSG00000075891. 14966DR GeneID; 5076; -. 14967DR KEGG; hsa:5076; -. 14968DR UCSC; uc001krk.4; human. 14969DR UCSC; uc001krl.4; human. 14970DR UCSC; uc001krm.4; human. 14971DR UCSC; uc001krn.4; human. 14972DR CTD; 5076; -. 14973DR GeneCards; GC10P102495; -. 14974DR HGNC; HGNC:8616; PAX2. 14975DR HPA; CAB013024; -. 14976DR MIM; 120330; phenotype. 14977DR MIM; 167409; gene. 14978DR neXtProt; NX_Q02962; -. 14979DR Orphanet; 2260; Oligomeganephronia. 14980DR Orphanet; 1475; Papillo-renal syndrome. 14981DR PharmGKB; PA32956; -. 14982DR eggNOG; NOG326044; -. 14983DR GeneTree; ENSGT00650000093055; -. 14984DR HOGENOM; HOG000230938; -. 14985DR HOVERGEN; HBG009115; -. 14986DR KO; K15608; -. 14987DR OMA; FSAMHRH; -. 14988DR OrthoDB; EOG49S66H; -. 14989DR PhylomeDB; Q02962; -. 14990DR NextBio; 19560; -. 14991DR ArrayExpress; Q02962; -. 14992DR Bgee; Q02962; -. 14993DR CleanEx; HS_PAX2; -. 14994DR Genevestigator; Q02962; -. 14995DR GermOnline; ENSG00000075891; Homo sapiens. 14996DR GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL. 14997DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 14998DR GO; GO:0043234; C:protein complex; ISS:UniProtKB. 14999DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB. 15000DR GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:UniProtKB. 15001DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; ISS:UniProtKB. 15002DR GO; GO:0006916; P:anti-apoptosis; IMP:UniProtKB. 15003DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc. 15004DR GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB. 15005DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEP:UniProtKB. 15006DR GO; GO:0001709; P:cell fate determination; ISS:UniProtKB. 15007DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB. 15008DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB. 15009DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB. 15010DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB. 15011DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB. 15012DR GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB. 15013DR GO; GO:0007501; P:mesodermal cell fate specification; ISS:UniProtKB. 15014DR GO; GO:0001823; P:mesonephros development; ISS:UniProtKB. 15015DR GO; GO:0072205; P:metanephric collecting duct development; ISS:UniProtKB. 15016DR GO; GO:0072221; P:metanephric distal convoluted tubule development; ISS:UniProtKB. 15017DR GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB. 15018DR GO; GO:0072289; P:metanephric nephron tubule formation; ISS:UniProtKB. 15019DR GO; GO:1900215; P:negative regulation of apoptotic process involved in metanephric collecting duct development; ISS:UniProtKB. 15020DR GO; GO:1900218; P:negative regulation of apoptotic process involved in metanephric nephron tubule development; ISS:UniProtKB. 15021DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. 15022DR GO; GO:0045918; P:negative regulation of cytolysis; IMP:UniProtKB. 15023DR GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; ISS:UniProtKB. 15024DR GO; GO:0072305; P:negative regulation of mesenchymal stem cell apoptotic process involved in metanephric nephron morphogenesis; ISS:UniProtKB. 15025DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB. 15026DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB. 15027DR GO; GO:0072179; P:nephric duct formation; ISS:UniProtKB. 15028DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB. 15029DR GO; GO:0061360; P:optic chiasma development; ISS:UniProtKB. 15030DR GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; ISS:UniProtKB. 15031DR GO; GO:0021633; P:optic nerve structural organization; ISS:UniProtKB. 15032DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB. 15033DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB. 15034DR GO; GO:0072108; P:positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB. 15035DR GO; GO:2000594; P:positive regulation of metanephric DCT cell differentiation; ISS:UniProtKB. 15036DR GO; GO:0072300; P:positive regulation of metanephric glomerulus development; ISS:UniProtKB. 15037DR GO; GO:2000597; P:positive regulation of optic nerve formation; ISS:UniProtKB. 15038DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. 15039DR GO; GO:0039003; P:pronephric field specification; ISS:UniProtKB. 15040DR GO; GO:0043491; P:protein kinase B signaling cascade; ISS:UniProtKB. 15041DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB. 15042DR GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB. 15043DR GO; GO:0035566; P:regulation of metanephros size; IMP:UniProtKB. 15044DR GO; GO:0003406; P:retinal pigment epithelium development; ISS:UniProtKB. 15045DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB. 15046DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 15047DR GO; GO:0035799; P:ureter maturation; ISS:UniProtKB. 15048DR GO; GO:0021650; P:vestibulocochlear nerve formation; ISS:UniProtKB. 15049DR GO; GO:0007601; P:visual perception; TAS:ProtInc. 15050DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. 15051DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 15052DR InterPro; IPR009057; Homeodomain-like. 15053DR InterPro; IPR001523; Paired_box_N. 15054DR InterPro; IPR022130; Pax2_C. 15055DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 15056DR Pfam; PF00292; PAX; 1. 15057DR Pfam; PF12403; Pax2_C; 1. 15058DR PRINTS; PR00027; PAIREDBOX. 15059DR SMART; SM00351; PAX; 1. 15060DR SUPFAM; SSF46689; Homeodomain_like; 1. 15061DR PROSITE; PS00034; PAIRED_1; 1. 15062DR PROSITE; PS51057; PAIRED_2; 1. 15063PE 1: Evidence at protein level; 15064KW Alternative splicing; Complete proteome; Developmental protein; 15065KW Differentiation; Disease mutation; DNA-binding; Nucleus; Paired box; 15066KW Phosphoprotein; Polymorphism; Reference proteome; Transcription; 15067KW Transcription regulation. 15068FT CHAIN 1 417 Paired box protein Pax-2. 15069FT /FTId=PRO_0000050175. 15070FT DOMAIN 16 142 Paired. 15071FT MOD_RES 226 226 Phosphothreonine. 15072FT VAR_SEQ 206 228 Missing (in isoform 3 and isoform 4). 15073FT /FTId=VSP_002345. 15074FT VAR_SEQ 364 417 GSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRG 15075FT SAPAAAAAAYDRH -> EAAVGPSSSLMSKPGRKLAEVPPC 15076FT VQPTGASSPATRTATPSTRPTTRLGDSATPPY (in 15077FT isoform 2 and isoform 4). 15078FT /FTId=VSP_002346. 15079FT VARIANT 39 40 Missing (in OMN; with bilateral 15080FT coloboma). 15081FT /FTId=VAR_012442. 15082FT VARIANT 75 75 T -> TET (in RCS). 15083FT /FTId=VAR_003788. 15084FT VARIANT 76 76 G -> S (in RCS). 15085FT /FTId=VAR_003789. 15086FT VARIANT 334 334 A -> V. 15087FT /FTId=VAR_012443. 15088FT CONFLICT 15 16 PG -> R (in Ref. 6; AAC41711). 15089FT CONFLICT 404 404 Missing (in Ref. 1; AAA60024 and 3; 15090FT AAC63385). 15091FT CONFLICT 410 410 A -> R (in Ref. 1; AAA60024 and 3; 15092FT AAC63385). 15093SQ SEQUENCE 417 AA; 44706 MW; 7EA24F9EB8C843F8 CRC64; 15094 MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV 15095 SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA 15096 EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND 15097 PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS 15098 QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL 15099 DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG 15100 MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRGSAPAAA AAAYDRH 15101// 15102ID PAX3_HUMAN Reviewed; 479 AA. 15103AC P23760; Q16448; Q494Z3; Q494Z4; Q53T90; Q6GSJ9; Q86UQ2; Q86UQ3; 15104DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. 15105DT 01-NOV-1995, sequence version 2. 15106DT 13-JUN-2012, entry version 145. 15107DE RecName: Full=Paired box protein Pax-3; 15108DE AltName: Full=HuP2; 15109GN Name=PAX3; Synonyms=HUP2; 15110OS Homo sapiens (Human). 15111OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 15112OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 15113OC Catarrhini; Hominidae; Homo. 15114OX NCBI_TaxID=9606; 15115RN [1] 15116RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PAX3G AND PAX3H), AND ALTERNATIVE 15117RP SPLICING. 15118RX MEDLINE=22999378; PubMed=14639621; DOI=10.1002/ijc.11527; 15119RA Parker C.J., Shawcross S.G., Li H., Wang Q.-Y., Herrington C.S., 15120RA Kumar S., MacKie R.M., Prime W., Renne I.G., Sisley K., Kumar P.; 15121RT "Expression of PAX 3 alternatively spliced transcripts and 15122RT identification of two new isoforms in human tumors of neural crest 15123RT origin."; 15124RL Int. J. Cancer 108:314-320(2004). 15125RN [2] 15126RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 15127RX PubMed=14702039; DOI=10.1038/ng1285; 15128RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., 15129RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., 15130RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., 15131RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., 15132RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., 15133RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., 15134RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., 15135RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., 15136RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., 15137RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., 15138RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., 15139RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., 15140RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., 15141RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., 15142RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., 15143RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., 15144RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., 15145RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., 15146RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., 15147RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., 15148RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., 15149RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., 15150RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., 15151RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., 15152RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., 15153RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., 15154RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., 15155RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; 15156RT "Complete sequencing and characterization of 21,243 full-length human 15157RT cDNAs."; 15158RL Nat. Genet. 36:40-45(2004). 15159RN [3] 15160RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 15161RX PubMed=15815621; DOI=10.1038/nature03466; 15162RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., 15163RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., 15164RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., 15165RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., 15166RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., 15167RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., 15168RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., 15169RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., 15170RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., 15171RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., 15172RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., 15173RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., 15174RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., 15175RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., 15176RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., 15177RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., 15178RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., 15179RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., 15180RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., 15181RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., 15182RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., 15183RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., 15184RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., 15185RA Waterston R.H., Wilson R.K.; 15186RT "Generation and annotation of the DNA sequences of human chromosomes 2 15187RT and 4."; 15188RL Nature 434:724-731(2005). 15189RN [4] 15190RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 15191RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 15192RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 15193RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 15194RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 15195RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 15196RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 15197RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 15198RA Venter J.C.; 15199RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 15200RN [5] 15201RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PAX3B; 6 AND 7). 15202RC TISSUE=Skin; 15203RX PubMed=15489334; DOI=10.1101/gr.2596504; 15204RG The MGC Project Team; 15205RT "The status, quality, and expansion of the NIH full-length cDNA 15206RT project: the Mammalian Gene Collection (MGC)."; 15207RL Genome Res. 14:2121-2127(2004). 15208RN [6] 15209RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 197-479. 15210RX MEDLINE=95301273; PubMed=7782066; DOI=10.1016/0888-7543(95)80076-X; 15211RA Macina R.A., Barr F.G., Galili N., Riethman H.C.; 15212RT "Genomic organization of the human PAX3 gene: DNA sequence analysis of 15213RT the region disrupted in alveolar rhabdomyosarcoma."; 15214RL Genomics 26:1-8(1995). 15215RN [7] 15216RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-195. 15217RX MEDLINE=89305521; PubMed=2501086; 15218RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; 15219RT "Conservation of the paired domain in metazoans and its structure in 15220RT three isolated human genes."; 15221RL EMBO J. 8:1183-1190(1989). 15222RN [8] 15223RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-392, AND VARIANTS WS1 LEU-45 15224RP AND ASP-99. 15225RX MEDLINE=95072569; PubMed=7981674; DOI=10.1093/hmg/3.7.1069; 15226RA Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E., 15227RA Kunze J., Sperling K., Strachan T., Read A.P.; 15228RT "PAX3 gene structure and mutations: close analogies between 15229RT Waardenburg syndrome and the Splotch mouse."; 15230RL Hum. Mol. Genet. 3:1069-1074(1994). 15231RN [9] 15232RP NUCLEOTIDE SEQUENCE [MRNA] (PAX3A AND PAX3B). 15233RX MEDLINE=94171226; PubMed=7545913; DOI=10.1007/BF00212021; 15234RA Tsukamoto K., Nakamura Y., Niikawa N.; 15235RT "Isolation of two isoforms of the PAX3 gene transcripts and their 15236RT tissue-specific alternative expression in human adult tissues."; 15237RL Hum. Genet. 93:270-274(1994). 15238RN [10] 15239RP NUCLEOTIDE SEQUENCE OF 1-319 (ISOFORM 6/7), AND CHROMOSOMAL 15240RP TRANSLOCATION WITH NCOA1. 15241RX PubMed=15313887; DOI=10.1158/0008-5472.CAN-04-0844; 15242RA Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J., 15243RA Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.; 15244RT "Gene expression signatures identify rhabdomyosarcoma subtypes and 15245RT detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1."; 15246RL Cancer Res. 64:5539-5545(2004). 15247RN [11] 15248RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-74, AND VARIANT WS1 15249RP 63-ALA--ILE-67 DEL. 15250RX MEDLINE=92168113; PubMed=1347148; DOI=10.1038/355635a0; 15251RA Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R., 15252RA Gruss P., Strachan T.; 15253RT "Waardenburg's syndrome patients have mutations in the human homologue 15254RT of the Pax-3 paired box gene."; 15255RL Nature 355:635-636(1992). 15256RN [12] 15257RP NUCLEOTIDE SEQUENCE OF 265-319. 15258RA Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.B., 15259RA Wilcox E.R.; 15260RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. 15261RN [13] 15262RP CHROMOSOMAL TRANSLOCATION WITH FOXO1. 15263RX MEDLINE=94100975; PubMed=8275086; DOI=10.1038/ng1193-230; 15264RA Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S., 15265RA Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G.; 15266RT "Fusion of a fork head domain gene to PAX3 in the solid tumour 15267RT alveolar rhabdomyosarcoma."; 15268RL Nat. Genet. 5:230-235(1993). 15269RN [14] 15270RP INTERACTION WITH DAXX. 15271RX MEDLINE=99321757; PubMed=10393185; DOI=10.1093/emboj/18.13.3702; 15272RA Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.; 15273RT "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated 15274RT repressor hDaxx."; 15275RL EMBO J. 18:3702-3711(1999). 15276RN [15] 15277RP INVOLVEMENT IN WS1. 15278RX PubMed=1303193; DOI=10.1093/hmg/1.4.243; 15279RA Morell R., Friedman T.B., Moeljopawiro S., Hartono S., Asher J.H. Jr.; 15280RT "A frameshift mutation in the HuP2 paired domain of the probable human 15281RT homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1 15282RT in an Indonesian family."; 15283RL Hum. Mol. Genet. 1:243-247(1992). 15284RN [16] 15285RP PHOSPHORYLATION AT SER-201; SER-205 AND SER-209. 15286RX PubMed=21440083; DOI=10.1016/j.biocel.2011.03.010; 15287RA Dietz K.N., Miller P.J., Iyengar A.S., Loupe J.M., Hollenbach A.D.; 15288RT "Identification of serines 201 and 209 as sites of Pax3 15289RT phosphorylation and the altered phosphorylation status of Pax3-FOXO1 15290RT during early myogenic differentiation."; 15291RL Int. J. Biochem. Cell Biol. 43:936-945(2011). 15292RN [17] 15293RP VARIANT WS1 LEU-50. 15294RX MEDLINE=92168114; PubMed=1347149; DOI=10.1038/355637a0; 15295RA Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.; 15296RT "An exonic mutation in the HuP2 paired domain gene causes 15297RT Waardenburg's syndrome."; 15298RL Nature 355:637-638(1992). 15299RN [18] 15300RP VARIANT WS1 ALA-81. 15301RX MEDLINE=93258399; PubMed=8490648; DOI=10.1038/ng0193-26; 15302RA Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R., 15303RA Strachan T.; 15304RT "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and 15305RT type 2."; 15306RL Nat. Genet. 3:26-30(1993). 15307RN [19] 15308RP VARIANTS WS3 HIS-47 AND WS1 LEU-56. 15309RX MEDLINE=93190976; PubMed=8447316; 15310RA Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K., 15311RA Baldwin C.T.; 15312RT "Mutations in the paired domain of the human PAX3 gene cause Klein- 15313RT Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I 15314RT (WS-I)."; 15315RL Am. J. Hum. Genet. 52:455-462(1993). 15316RN [20] 15317RP VARIANT WS1 VAL-62. 15318RX MEDLINE=95135456; PubMed=7833953; DOI=10.1002/humu.1380040310; 15319RA Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.; 15320RT "A single base pair substitution within the paired box of PAX3 in an 15321RT individual with Waardenburg syndrome type 1 (WS1)."; 15322RL Hum. Mutat. 4:227-228(1994). 15323RN [21] 15324RP VARIANTS WS1 PHE-265 AND GLY-271. 15325RX MEDLINE=95126143; PubMed=7825605; 15326RA Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B., 15327RA San Agustin T.B., Wilcox E.R.; 15328RT "Further elucidation of the genomic structure of PAX3, and 15329RT identification of two different point mutations within the PAX3 15330RT homeobox that cause Waardenburg syndrome type 1 in two families."; 15331RL Am. J. Hum. Genet. 56:75-83(1995). 15332RN [22] 15333RP VARIANT WS3 PHE-84. 15334RX MEDLINE=95243235; PubMed=7726174; 15335RA Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.; 15336RT "Homozygosity for Waardenburg syndrome."; 15337RL Am. J. Hum. Genet. 56:1173-1178(1995). 15338RN [23] 15339RP VARIANTS WS1 MET-60; GLU-85 AND SER-238. 15340RX MEDLINE=96042708; PubMed=8533800; DOI=10.1002/ajmg.1320580205; 15341RA Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.; 15342RT "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new 15343RT mutations and review of the literature."; 15344RL Am. J. Med. Genet. 58:115-122(1995). 15345RN [24] 15346RP VARIANTS WS1 MET-78; ALA-81; ASP-99; CYS-266; CYS-270; CYS-271 AND 15347RP HIS-271, AND VARIANT LYS-315. 15348RX MEDLINE=96154685; PubMed=8589691; DOI=10.1093/hmg/4.11.2131; 15349RA Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D., 15350RA Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W., 15351RA Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R., 15352RA Read A.P.; 15353RT "The mutational spectrum in Waardenburg syndrome."; 15354RL Hum. Mol. Genet. 4:2131-2137(1995). 15355RN [25] 15356RP VARIANTS WS1 ARG-48; CYS-270 AND HIS-271, AND VARIANTS LYS-273 AND 15357RP LYS-315. 15358RX PubMed=8845842; DOI=10.1093/hmg/5.4.497; 15359RA Pandya A., Xia X.-J., Landa B.L., Arnos K.S., Israel J., Lloyd J., 15360RA James A.L., Diehl S.R., Blanton S.H., Nance W.E.; 15361RT "Phenotypic variation in Waardenburg syndrome: mutational 15362RT heterogeneity, modifier genes or polygenic background?"; 15363RL Hum. Mol. Genet. 5:497-502(1996). 15364RN [26] 15365RP VARIANT CDHS LYS-47. 15366RX MEDLINE=96263735; PubMed=8664898; 15367RX DOI=10.1002/(SICI)1098-1004(1996)7:1<30::AID-HUMU4>3.3.CO;2-H; 15368RA Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.; 15369RT "Missense mutation in the paired domain of PAX3 causes craniofacial- 15370RT deafness-hand syndrome."; 15371RL Hum. Mutat. 7:30-35(1996). 15372RN [27] 15373RP VARIANT LYS-315. 15374RX MEDLINE=97016531; PubMed=8863157; 15375RA Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R., 15376RA Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J., 15377RA Mariman E.C.M.; 15378RT "PAX genes and human neural tube defects: an amino acid substitution 15379RT in PAX1 in a patient with spina bifida."; 15380RL J. Med. Genet. 33:655-660(1996). 15381RN [28] 15382RP VARIANT WS1 PHE-59. 15383RX MEDLINE=97220597; PubMed=9067759; 15384RX DOI=10.1002/(SICI)1098-1004(1997)9:2<177::AID-HUMU11>3.3.CO;2-Z; 15385RA Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K., 15386RA Fukushima Y., Jinno Y., Niikawa N.; 15387RT "Three novel PAX3 mutations observed in patients with Waardenburg 15388RT syndrome type 1."; 15389RL Hum. Mutat. 9:177-180(1997). 15390RN [29] 15391RP VARIANT WS1 VAL-62. 15392RX MEDLINE=98112449; PubMed=9452070; 15393RA Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J., 15394RA Mariman E.C.M.; 15395RT "Identification of two PAX3 mutations causing Waardenburg syndrome, 15396RT one within the paired domain (M62V) and the other downstream of the 15397RT homeodomain (Q282X)."; 15398RL Hum. Mutat. Suppl. 1:S145-S147(1998). 15399RN [30] 15400RP VARIANT WS1 HIS-391. 15401RX MEDLINE=98200183; PubMed=9541113; 15402RA Carey M.L., Friedman T.B., Asher J.H. Jr., Innis J.W.; 15403RT "Septo-optic dysplasia and WS1 in the proband of a WS1 family 15404RT segregating for a novel mutation in PAX3 exon 7."; 15405RL J. Med. Genet. 35:248-250(1998). 15406RN [31] 15407RP VARIANT LYS-315. 15408RX MEDLINE=98250826; PubMed=9584079; DOI=10.1006/mcpr.1997.0149; 15409RA Wang C., Kim E., Attaie A., Smith T.N., Wilcox E.R., Lalwani A.K.; 15410RT "A PAX3 polymorphism (T315K) in a family exhibiting Waardenburg 15411RT syndrome type 2."; 15412RL Mol. Cell. Probes 12:55-57(1998). 15413RN [32] 15414RP VARIANT WS1 ASN-59. 15415RA Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A., 15416RA Schwartz E.I.; 15417RT "A novel missense mutation Ile59Asn in the PAX3 gene in a family with 15418RT Waardenburg syndrome type I."; 15419RL Hum. Mutat. 13:85-85(1999). 15420RN [33] 15421RP VARIANT WS3 CYS-270. 15422RA Bottani A., Antonarakis S.E., Blouin J.-L.; 15423RL Submitted (MAY-1999) to UniProtKB. 15424RN [34] 15425RP VARIANT WS1 LEU-73. 15426RX MEDLINE=20243823; PubMed=10779847; 15427RX DOI=10.1076/1381-6810(200003)21:1;1-I;FT025; 15428RA Sotirova V.N., Rezaie T.M., Khoshsorour M.M., Sarfarazi M.; 15429RT "Identification of a novel mutation in the paired domain of PAX3 in an 15430RT Iranian family with waardenburg syndrome type I."; 15431RL Ophthalmic Genet. 21:25-28(2000). 15432RN [35] 15433RP VARIANT WS1 MET-60, AND VARIANT WS3 HIS-90. 15434RX MEDLINE=22829208; PubMed=12949970; DOI=10.1002/ajmg.a.20260; 15435RA Wollnik B., Tukel T., Uyguner O., Ghanbari A., Kayserili H., 15436RA Emiroglu M., Yuksel-Apak M.; 15437RT "Homozygous and heterozygous inheritance of PAX3 mutations causes 15438RT different types of Waardenburg syndrome."; 15439RL Am. J. Med. Genet. A 122:42-45(2003). 15440CC -!- FUNCTION: Probable transcription factor associated with 15441CC development of alveolar rhabdomyosarcoma. 15442CC -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX7. Interacts 15443CC with DAXX. 15444CC -!- INTERACTION: 15445CC P20265:POU3F2; NbExp=2; IntAct=EBI-1167564, EBI-1167176; 15446CC P56693:SOX10; NbExp=2; IntAct=EBI-1167564, EBI-1167533; 15447CC -!- SUBCELLULAR LOCATION: Nucleus. 15448CC -!- ALTERNATIVE PRODUCTS: 15449CC Event=Alternative splicing; Named isoforms=7; 15450CC Name=Pax3; 15451CC IsoId=P23760-1; Sequence=Displayed; 15452CC Name=Pax3A; 15453CC IsoId=P23760-2; Sequence=VSP_002355, VSP_002356; 15454CC Name=Pax3B; 15455CC IsoId=P23760-3; Sequence=VSP_002357, VSP_002358; 15456CC Name=Pax3G; 15457CC IsoId=P23760-4; Sequence=VSP_042004; 15458CC Name=Pax3H; 15459CC IsoId=P23760-5; Sequence=VSP_042005; 15460CC Name=6; 15461CC IsoId=P23760-6; Sequence=VSP_043634, VSP_043635; 15462CC Note=No experimental confirmation available; 15463CC Name=7; 15464CC IsoId=P23760-7; Sequence=VSP_043635; 15465CC -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome 15466CC type 1 (WS1) [MIM:193500]. WS1 is an autosomal dominant disorder 15467CC characterized by wide bridge of nose owing to lateral displacement 15468CC of the inner canthus of each eye (dystopia canthorum), pigmentary 15469CC disturbances such as frontal white blaze of hair, heterochromia of 15470CC irides, white eyelashes, leukoderma and sensorineural deafness. 15471CC The syndrome shows variable clinical expression and some affected 15472CC individuals do not manifest hearing impairment. 15473CC -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome 15474CC type 3 (WS3) [MIM:148820]; also known as Klein-Waardenburg 15475CC syndrome or Waardenburg syndrome with upper limb anomalies or 15476CC white forelock with malformations. WS3 is a very rare autosomal 15477CC dominant disorder, which shares many of the characteristics of 15478CC WS1. Patients additionally present with musculoskeletal 15479CC abnormalities. 15480CC -!- DISEASE: Defects in PAX3 are the cause of craniofacial-deafness- 15481CC hand syndrome (CDHS) [MIM:122880]. CDHS is thought to be an 15482CC autosomal dominant disease which comprises absence or hypoplasia 15483CC of the nasal bones, hypoplastic maxilla, small and short nose with 15484CC thin nares, limited movement of the wrist, short palpebral 15485CC fissures, ulnar deviation of the fingers, hypertelorism and 15486CC profound sensory-neural deafness. 15487CC -!- DISEASE: Defects in PAX3 are a cause of rhabdomyosarcoma type 2 15488CC (RMS2) [MIM:268220]. It is a form of rhabdomyosarcoma, a highly 15489CC malignant tumor of striated muscle derived from primitive 15490CC mesenchimal cells and exhibiting differentiation along 15491CC rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most 15492CC frequently occurring soft tissue sarcomas and the most common in 15493CC children. It occurs in four forms: alveolar, pleomorphic, 15494CC embryonal and botryoidal rhabdomyosarcomas. Note=A chromosomal 15495CC aberration involving PAX3 is found in rhabdomyosarcoma. 15496CC Translocation (2;13)(q35;q14) with FOXO1. The resulting protein is 15497CC a transcriptional activator. 15498CC -!- DISEASE: Note=A chromosomal aberration involving PAX3 is a cause 15499CC of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1 15500CC generates the NCOA1-PAX3 oncogene consisting of the N-terminus 15501CC part of PAX3 and the C-terminus part of NCOA1. The fusion protein 15502CC acts as a transcriptional activator. Rhabdomyosarcoma is the most 15503CC common soft tissue carcinoma in childhood, representing 5-8% of 15504CC all malignancies in children. 15505CC -!- SIMILARITY: Belongs to the paired homeobox family. 15506CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. 15507CC -!- SIMILARITY: Contains 1 paired domain. 15508CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology 15509CC and Haematology; 15510CC URL="http://atlasgeneticsoncology.org/Genes/PAX3ID70ch2q35.html"; 15511CC -!- WEB RESOURCE: Name=GeneReviews; 15512CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX3"; 15513CC ----------------------------------------------------------------------- 15514CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 15515CC Distributed under the Creative Commons Attribution-NoDerivs License 15516CC ----------------------------------------------------------------------- 15517DR EMBL; AY251279; AAP13872.1; -; mRNA. 15518DR EMBL; AY251280; AAP13873.1; -; mRNA. 15519DR EMBL; AK291278; BAF83967.1; -; mRNA. 15520DR EMBL; AC010980; AAY14900.1; -; Genomic_DNA. 15521DR EMBL; AC012591; -; NOT_ANNOTATED_CDS; Genomic_DNA. 15522DR EMBL; CH471063; EAW70789.1; -; Genomic_DNA. 15523DR EMBL; CH471063; EAW70791.1; -; Genomic_DNA. 15524DR EMBL; CH471063; EAW70794.1; -; Genomic_DNA. 15525DR EMBL; BC063547; AAH63547.1; -; mRNA. 15526DR EMBL; BC101299; AAI01300.1; -; mRNA. 15527DR EMBL; BC101300; AAI01301.1; -; mRNA. 15528DR EMBL; BC101301; AAI01302.1; -; mRNA. 15529DR EMBL; BC101302; AAI01303.1; -; mRNA. 15530DR EMBL; BC114363; AAI14364.1; -; mRNA. 15531DR EMBL; U12263; AAA80573.1; -; Genomic_DNA. 15532DR EMBL; U12259; AAA80574.1; -; Genomic_DNA. 15533DR EMBL; U12258; AAA80574.1; JOINED; Genomic_DNA. 15534DR EMBL; U12260; AAA80574.1; JOINED; Genomic_DNA. 15535DR EMBL; U12262; AAA80574.1; JOINED; Genomic_DNA. 15536DR EMBL; X15043; CAA33145.1; -; Genomic_DNA. 15537DR EMBL; X15252; CAA33145.1; JOINED; Genomic_DNA. 15538DR EMBL; X15253; CAA33145.1; JOINED; Genomic_DNA. 15539DR EMBL; Z29972; -; NOT_ANNOTATED_CDS; Genomic_DNA. 15540DR EMBL; Z29973; -; NOT_ANNOTATED_CDS; Genomic_DNA. 15541DR EMBL; Z29974; -; NOT_ANNOTATED_CDS; Genomic_DNA. 15542DR EMBL; S69369; AAB30167.1; -; mRNA. 15543DR EMBL; S69370; AAB30168.1; -; mRNA. 15544DR EMBL; AY633656; AAT47737.1; -; mRNA. 15545DR EMBL; S83614; AAB21476.1; -; Genomic_DNA. 15546DR EMBL; L10614; AAA91849.1; -; Genomic_DNA. 15547DR IPI; IPI00012896; -. 15548DR IPI; IPI00219092; -. 15549DR IPI; IPI00219093; -. 15550DR IPI; IPI00375387; -. 15551DR IPI; IPI00895878; -. 15552DR PIR; I54276; I54276. 15553DR PIR; I68547; I68547. 15554DR PIR; S06960; S06960. 15555DR RefSeq; NP_000429.2; NM_000438.5. 15556DR RefSeq; NP_001120838.1; NM_001127366.2. 15557DR RefSeq; NP_039230.1; NM_013942.4. 15558DR RefSeq; NP_852122.1; NM_181457.3. 15559DR RefSeq; NP_852123.1; NM_181458.3. 15560DR RefSeq; NP_852124.1; NM_181459.3. 15561DR RefSeq; NP_852125.1; NM_181460.3. 15562DR RefSeq; NP_852126.1; NM_181461.3. 15563DR UniGene; Hs.42146; -. 15564DR PDB; 3CMY; X-ray; 1.95 A; A=219-278. 15565DR PDBsum; 3CMY; -. 15566DR ProteinModelPortal; P23760; -. 15567DR SMR; P23760; 35-158, 219-277. 15568DR IntAct; P23760; 7. 15569DR MINT; MINT-202884; -. 15570DR STRING; P23760; -. 15571DR PhosphoSite; P23760; -. 15572DR DMDM; 1172022; -. 15573DR PRIDE; P23760; -. 15574DR DNASU; 5077; -. 15575DR Ensembl; ENST00000258387; ENSP00000258387; ENSG00000135903. 15576DR Ensembl; ENST00000336840; ENSP00000338767; ENSG00000135903. 15577DR Ensembl; ENST00000344493; ENSP00000342092; ENSG00000135903. 15578DR Ensembl; ENST00000350526; ENSP00000343052; ENSG00000135903. 15579DR Ensembl; ENST00000392070; ENSP00000375922; ENSG00000135903. 15580DR Ensembl; ENST00000409551; ENSP00000386750; ENSG00000135903. 15581DR Ensembl; ENST00000409828; ENSP00000386817; ENSG00000135903. 15582DR GeneID; 5077; -. 15583DR KEGG; hsa:5077; -. 15584DR UCSC; uc002vmw.2; human. 15585DR UCSC; uc002vmz.2; human. 15586DR UCSC; uc002vna.2; human. 15587DR CTD; 5077; -. 15588DR GeneCards; GC02M223029; -. 15589DR HGNC; HGNC:8617; PAX3. 15590DR HPA; CAB013466; -. 15591DR MIM; 122880; phenotype. 15592DR MIM; 148820; phenotype. 15593DR MIM; 193500; phenotype. 15594DR MIM; 268220; phenotype. 15595DR MIM; 606597; gene. 15596DR neXtProt; NX_P23760; -. 15597DR Orphanet; 99756; Alveolar rhabdomyosarcoma. 15598DR Orphanet; 1529; Craniofacial-deafness-hand syndrome. 15599DR Orphanet; 894; Waardenburg syndrome type 1. 15600DR Orphanet; 896; Waardenburg syndrome type 3. 15601DR PharmGKB; PA32957; -. 15602DR eggNOG; NOG326044; -. 15603DR GeneTree; ENSGT00650000093130; -. 15604DR HOGENOM; HOG000230939; -. 15605DR HOVERGEN; HBG009115; -. 15606DR KO; K09381; -. 15607DR EvolutionaryTrace; P23760; -. 15608DR NextBio; 19572; -. 15609DR ArrayExpress; P23760; -. 15610DR Bgee; P23760; -. 15611DR CleanEx; HS_PAX3; -. 15612DR Genevestigator; P23760; -. 15613DR GermOnline; ENSG00000135903; Homo sapiens. 15614DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 15615DR GO; GO:0005515; F:protein binding; IPI:IntAct. 15616DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. 15617DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc. 15618DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. 15619DR GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. 15620DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. 15621DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI. 15622DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. 15623DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 15624DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 15625DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. 15626DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 15627DR InterPro; IPR017970; Homeobox_CS. 15628DR InterPro; IPR001356; Homeodomain. 15629DR InterPro; IPR009057; Homeodomain-like. 15630DR InterPro; IPR001523; Paired_box_N. 15631DR InterPro; IPR022106; Pax7. 15632DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 15633DR Pfam; PF00046; Homeobox; 1. 15634DR Pfam; PF00292; PAX; 1. 15635DR Pfam; PF12360; Pax7; 1. 15636DR PRINTS; PR00027; PAIREDBOX. 15637DR SMART; SM00389; HOX; 1. 15638DR SMART; SM00351; PAX; 1. 15639DR SUPFAM; SSF46689; Homeodomain_like; 2. 15640DR PROSITE; PS00027; HOMEOBOX_1; 1. 15641DR PROSITE; PS50071; HOMEOBOX_2; 1. 15642DR PROSITE; PS00034; PAIRED_1; 1. 15643DR PROSITE; PS51057; PAIRED_2; 1. 15644PE 1: Evidence at protein level; 15645KW 3D-structure; Alternative splicing; Chromosomal rearrangement; 15646KW Complete proteome; Deafness; Developmental protein; Disease mutation; 15647KW DNA-binding; Homeobox; Nucleus; Paired box; Phosphoprotein; 15648KW Polymorphism; Proto-oncogene; Reference proteome; Transcription; 15649KW Transcription regulation; Waardenburg syndrome. 15650FT CHAIN 1 479 Paired box protein Pax-3. 15651FT /FTId=PRO_0000050178. 15652FT DOMAIN 34 161 Paired. 15653FT DNA_BIND 219 278 Homeobox. 15654FT SITE 319 320 Breakpoint for translocation to form 15655FT PAX3-NCOA1 oncogene. 15656FT MOD_RES 201 201 Phosphoserine. 15657FT MOD_RES 205 205 Phosphoserine. 15658FT MOD_RES 209 209 Phosphoserine. 15659FT VAR_SEQ 108 108 Missing (in isoform 6). 15660FT /FTId=VSP_043634. 15661FT VAR_SEQ 196 215 ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRA 15662FT SAS (in isoform Pax3A). 15663FT /FTId=VSP_002355. 15664FT VAR_SEQ 196 206 ASAPQSDEGSD -> GKALVSGVSSH (in isoform 15665FT Pax3B). 15666FT /FTId=VSP_002357. 15667FT VAR_SEQ 207 479 Missing (in isoform Pax3B). 15668FT /FTId=VSP_002358. 15669FT VAR_SEQ 216 479 Missing (in isoform Pax3A). 15670FT /FTId=VSP_002356. 15671FT VAR_SEQ 393 479 MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRL 15672FT DHMKSLDSLPTSQSYCPPTYSTTGYSMDPVTGYQYGQYGQS 15673FT KPWTF -> PFIISSQISRK (in isoform Pax3G). 15674FT /FTId=VSP_042004. 15675FT VAR_SEQ 393 479 MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRL 15676FT DHMKSLDSLPTSQSYCPPTYSTTGYSMDPVTGYQYGQYGQS 15677FT KPWTF -> PFIISSQISLGFKSF (in isoform 15678FT Pax3H). 15679FT /FTId=VSP_042005. 15680FT VAR_SEQ 475 479 KPWTF -> AFHYLKPDIA (in isoform 6 and 15681FT isoform 7). 15682FT /FTId=VSP_043635. 15683FT VARIANT 45 45 F -> L (in WS1). 15684FT /FTId=VAR_003790. 15685FT VARIANT 47 47 N -> H (in WS3). 15686FT /FTId=VAR_003791. 15687FT VARIANT 47 47 N -> K (in CDHS). 15688FT /FTId=VAR_003792. 15689FT VARIANT 48 48 G -> R (in WS1). 15690FT /FTId=VAR_017533. 15691FT VARIANT 50 50 P -> L (in WS1; important hearing loss). 15692FT /FTId=VAR_003793. 15693FT VARIANT 56 56 R -> L (in WS1; associated with 15694FT meningomyelocele). 15695FT /FTId=VAR_003794. 15696FT VARIANT 59 59 I -> F (in WS1). 15697FT /FTId=VAR_003795. 15698FT VARIANT 59 59 I -> N (in WS1). 15699FT /FTId=VAR_003796. 15700FT VARIANT 60 60 V -> M (in WS1). 15701FT /FTId=VAR_003797. 15702FT VARIANT 62 62 M -> V (in WS1). 15703FT /FTId=VAR_003798. 15704FT VARIANT 63 67 Missing (in WS1). 15705FT /FTId=VAR_003799. 15706FT VARIANT 73 73 S -> L (in WS1). 15707FT /FTId=VAR_013640. 15708FT VARIANT 78 78 V -> M (in WS1). 15709FT /FTId=VAR_017534. 15710FT VARIANT 81 81 G -> A (in WS1; originally classified as 15711FT Waardenburg syndrome type 2). 15712FT /FTId=VAR_003800. 15713FT VARIANT 84 84 S -> F (in WS3). 15714FT /FTId=VAR_003801. 15715FT VARIANT 85 85 K -> E (in WS1). 15716FT /FTId=VAR_003802. 15717FT VARIANT 90 90 Y -> H (in WS3; dbSNP:rs28939096). 15718FT /FTId=VAR_017535. 15719FT VARIANT 99 99 G -> D (in WS1). 15720FT /FTId=VAR_003803. 15721FT VARIANT 238 238 F -> S (in WS1). 15722FT /FTId=VAR_003804. 15723FT VARIANT 265 265 V -> F (in WS1). 15724FT /FTId=VAR_003805. 15725FT VARIANT 266 266 W -> C (in WS1). 15726FT /FTId=VAR_017536. 15727FT VARIANT 270 270 R -> C (in WS1 and WS3). 15728FT /FTId=VAR_013619. 15729FT VARIANT 271 271 R -> C (in WS1). 15730FT /FTId=VAR_017537. 15731FT VARIANT 271 271 R -> G (in WS1). 15732FT /FTId=VAR_003806. 15733FT VARIANT 271 271 R -> H (in WS1; associated with Lys-273 15734FT in one family). 15735FT /FTId=VAR_017538. 15736FT VARIANT 273 273 R -> K (associated with His-271 in one 15737FT Waardenburg syndrome type I family). 15738FT /FTId=VAR_017539. 15739FT VARIANT 315 315 T -> K (in dbSNP:rs2234675). 15740FT /FTId=VAR_003807. 15741FT VARIANT 391 391 Q -> H (in WS1). 15742FT /FTId=VAR_013641. 15743FT CONFLICT 358 358 S -> R (in Ref. 1; AAP13872/AAP13873). 15744FT HELIX 228 240 15745FT HELIX 246 256 15746FT HELIX 260 276 15747SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; 15748 MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV 15749 EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE 15750 YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES 15751 EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER 15752 THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP 15753 TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR 15754 HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE 15755 PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF 15756// 15757ID PAX4_HUMAN Reviewed; 350 AA. 15758AC O43316; O95161; Q6B0H0; 15759DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. 15760DT 01-JUN-1998, sequence version 1. 15761DT 13-JUN-2012, entry version 118. 15762DE RecName: Full=Paired box protein Pax-4; 15763GN Name=PAX4; 15764OS Homo sapiens (Human). 15765OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 15766OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 15767OC Catarrhini; Hominidae; Homo. 15768OX NCBI_TaxID=9606; 15769RN [1] 15770RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 15771RX MEDLINE=98102804; PubMed=9439631; DOI=10.1006/bbrc.1997.7935; 15772RA Matsushita T., Yamaoka T., Otsuka S., Moritani M., Matsumoto T., 15773RA Itakura M.; 15774RT "Molecular cloning of mouse paired-box-containing gene (Pax-4) from an 15775RT islet beta cell line and deduced sequence of human Pax-4."; 15776RL Biochem. Biophys. Res. Commun. 242:176-180(1998). 15777RN [2] 15778RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). 15779RC TISSUE=Placenta; 15780RX MEDLINE=98424228; PubMed=9753306; 15781RA Tao T., Wasson J., Bernal-Mizrachi E., Behn P.S., Chayen S., 15782RA Duprat L., Meyer J., Glaser B., Permutt M.A.; 15783RT "Isolation and characterization of the human PAX4 gene."; 15784RL Diabetes 47:1650-1653(1998). 15785RN [3] 15786RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 15787RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; 15788RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., 15789RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., 15790RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., 15791RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., 15792RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., 15793RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., 15794RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., 15795RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., 15796RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., 15797RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., 15798RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., 15799RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., 15800RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., 15801RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., 15802RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., 15803RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., 15804RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., 15805RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., 15806RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., 15807RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., 15808RA Waterston R.H., Wilson R.K.; 15809RT "The DNA sequence of human chromosome 7."; 15810RL Nature 424:157-164(2003). 15811RN [4] 15812RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 15813RC TISSUE=Colon; 15814RX PubMed=15489334; DOI=10.1101/gr.2596504; 15815RG The MGC Project Team; 15816RT "The status, quality, and expansion of the NIH full-length cDNA 15817RT project: the Mammalian Gene Collection (MGC)."; 15818RL Genome Res. 14:2121-2127(2004). 15819RN [5] 15820RP ALTERNATIVE SPLICING (ISOFORM 2). 15821RC TISSUE=Insulinoma; 15822RX MEDLINE=21164695; PubMed=11263967; DOI=10.1006/bbrc.2001.4552; 15823RA Miyamoto T., Kakizawa T., Ichikawa K., Nishio S., Kajikawa S., 15824RA Hashizume K.; 15825RT "Expression of dominant negative form of PAX4 in human insulinoma."; 15826RL Biochem. Biophys. Res. Commun. 282:34-40(2001). 15827RN [6] 15828RP VARIANT DIABETES MELLITUS TYPE 2 TRP-129. 15829RX PubMed=11723072; 15830RA Shimajiri Y., Sanke T., Furuta H., Hanabusa T., Nakagawa T., 15831RA Fujitani Y., Kajimoto Y., Takasu N., Nanjo K.; 15832RT "A missense mutation of Pax4 gene (R121W) is associated with type 2 15833RT diabetes in Japanese."; 15834RL Diabetes 50:2864-2869(2001). 15835RN [7] 15836RP VARIANTS TRP-45 AND TRP-141, AND ASSOCIATION WITH SUSCEPTIBILITY TO 15837RP KETOSIS-PRONE DIABETES. 15838RX PubMed=15509590; DOI=10.1093/hmg/ddh341; 15839RA Mauvais-Jarvis F., Smith S.B., Le May C., Leal S.M., Gautier J.-F., 15840RA Molokhia M., Riveline J.-P., Rajan A.S., Kevorkian J.-P., Zhang S., 15841RA Vexiau P., German M.S., Vaisse C.; 15842RT "PAX4 gene variations predispose to ketosis-prone diabetes."; 15843RL Hum. Mol. Genet. 13:3151-3159(2004). 15844RN [8] 15845RP VARIANT PRO-321 (ISOFORM 3), AND ASSOCIATION WITH SUSCEPTIBILITY TO 15846RP IDDM. 15847RX PubMed=15834548; DOI=10.1007/s00125-005-1723-5; 15848RA Biason-Lauber A., Boehm B., Lang-Muritano M., Gauthier B.R., Brun T., 15849RA Wollheim C.B., Schoenle E.J.; 15850RT "Association of childhood type 1 diabetes mellitus with a variant of 15851RT PAX4: possible link to beta cell regenerative capacity."; 15852RL Diabetologia 48:900-905(2005). 15853RN [9] 15854RP VARIANT MODY9 TRP-172, VARIANTS GLN-39; CYS-191; HIS-200 AND SER-200, 15855RP VARIANT PRO-321 (ISOFORM 3), AND CHARACTERIZATION OF VARIANT MODY9 15856RP TRP-172. 15857RX PubMed=17426099; DOI=10.1210/jc.2006-1927; 15858RA Plengvidhya N., Kooptiwut S., Songtawee N., Doi A., Furuta H., 15859RA Nishi M., Nanjo K., Tantibhedhyangkul W., Boonyasrisawat W., 15860RA Yenchitsomanus P.-T., Doria A., Banchuin N.; 15861RT "PAX4 mutations in Thais with maturity onset diabetes of the young."; 15862RL J. Clin. Endocrinol. Metab. 92:2821-2826(2007). 15863CC -!- FUNCTION: Plays an important role in the differentiation and 15864CC development of pancreatic islet beta cells. Transcriptional 15865CC repressor that binds to a common element in the glucagon, insulin 15866CC and somatostatin promoters. Competes with PAX6 for this same 15867CC promoter binding site. Isoform 2 appears to be a dominant negative 15868CC form antagonizing PAX4 transcriptional activity. 15869CC -!- SUBCELLULAR LOCATION: Nucleus. 15870CC -!- ALTERNATIVE PRODUCTS: 15871CC Event=Alternative splicing; Named isoforms=3; 15872CC Name=1; Synonyms=Pax4; 15873CC IsoId=O43316-1; Sequence=Displayed; 15874CC Name=2; Synonyms=Pax4V; 15875CC IsoId=O43316-2; Sequence=VSP_002359, VSP_002360; 15876CC Name=3; 15877CC IsoId=O43316-4; Sequence=VSP_036448, VSP_036449; 15878CC Note=Variant in position: 321:H->P (associated with 15879CC susceptibility to IDDM, dbSNP:rs712701); 15880CC -!- DISEASE: Defects in PAX4 are a cause of noninsulin-dependent 15881CC diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes 15882CC mellitus type 2 or maturity-onset diabetes. NIDDM is characterized 15883CC by an autosomal dominant mode of inheritance, onset during 15884CC adulthood and insulin resistance. 15885CC -!- DISEASE: Genetic variations in PAX4 are associated with 15886CC susceptibility to insulin-dependent diabetes mellitus (IDDM) 15887CC [MIM:222100]. IDDM normally starts in childhood or adolescence and 15888CC is caused by the body's own immune system which destroys the 15889CC insulin-producing beta cells in the pancreas. Classical features 15890CC are polydipsia, polyphagia and polyuria, due to hyperglycemia- 15891CC induced osmotic diuresis. 15892CC -!- DISEASE: Defects in PAX4 are a cause of susceptibility to diabetes 15893CC mellitus ketosis-prone (KPD) [MIM:612227]. KPD is an atypical form 15894CC of diabetes mellitus characterized by an acute initial 15895CC presentation with severe hyperglycemia and ketosis, as seen in 15896CC classic type 1 diabetes, but after initiation of insulin therapy, 15897CC prolonged remission is often possible with cessation of insulin 15898CC therapy and maintenance of appropriate metabolic control. 15899CC Metabolic studies show a markedly blunted insulin secretory 15900CC response to glucose, partially reversible with the improvement of 15901CC blood glucose control. Variable levels of insulin resistance are 15902CC observed, especially in obese patients. Pancreatic beta-cell 15903CC autoimmunity is a rare finding. 15904CC -!- DISEASE: Defects in PAX4 are the cause of maturity-onset diabetes 15905CC of the young type 9 (MODY9) [MIM:612225]. MODY is a form of 15906CC diabetes that is characterized by an autosomal dominant mode of 15907CC inheritance, onset in childhood or early adulthood (usually before 15908CC 25 years of age), a primary defect in insulin secretion and 15909CC frequent insulin-independence at the beginning of the disease. 15910CC -!- SIMILARITY: Belongs to the paired homeobox family. 15911CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. 15912CC -!- SIMILARITY: Contains 1 paired domain. 15913CC -!- SEQUENCE CAUTION: 15914CC Sequence=AC073934; Type=Miscellaneous discrepancy; Note=According to the human genome assembly there is a stop codon in position 349; 15915CC ----------------------------------------------------------------------- 15916CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 15917CC Distributed under the Creative Commons Attribution-NoDerivs License 15918CC ----------------------------------------------------------------------- 15919DR EMBL; AB008913; BAA24506.1; -; mRNA. 15920DR EMBL; AF043978; AAD02289.1; -; mRNA. 15921DR EMBL; AC073934; -; NOT_ANNOTATED_CDS; Genomic_DNA. 15922DR EMBL; BC074761; AAH74761.1; -; mRNA. 15923DR IPI; IPI00011955; -. 15924DR IPI; IPI00218426; -. 15925DR IPI; IPI00844339; -. 15926DR RefSeq; NP_006184.2; NM_006193.2. 15927DR UniGene; Hs.129706; -. 15928DR ProteinModelPortal; O43316; -. 15929DR SMR; O43316; 7-135, 164-233. 15930DR STRING; O43316; -. 15931DR PRIDE; O43316; -. 15932DR DNASU; 5078; -. 15933DR Ensembl; ENST00000338516; ENSP00000344297; ENSG00000106331. 15934DR Ensembl; ENST00000341640; ENSP00000339906; ENSG00000106331. 15935DR Ensembl; ENST00000378740; ENSP00000368014; ENSG00000106331. 15936DR GeneID; 5078; -. 15937DR KEGG; hsa:5078; -. 15938DR UCSC; uc003vmg.1; human. 15939DR UCSC; uc010lld.1; human. 15940DR CTD; 5078; -. 15941DR GeneCards; GC07M127250; -. 15942DR H-InvDB; HIX0033508; -. 15943DR HGNC; HGNC:8618; PAX4. 15944DR HPA; HPA006806; -. 15945DR HPA; HPA007182; -. 15946DR MIM; 125853; phenotype. 15947DR MIM; 167413; gene. 15948DR MIM; 222100; phenotype. 15949DR MIM; 612225; phenotype. 15950DR MIM; 612227; phenotype. 15951DR neXtProt; NX_O43316; -. 15952DR Orphanet; 552; MODY syndrome. 15953DR PharmGKB; PA32958; -. 15954DR eggNOG; NOG309473; -. 15955DR GeneTree; ENSGT00650000093130; -. 15956DR HOGENOM; HOG000230939; -. 15957DR HOVERGEN; HBG009115; -. 15958DR KO; K08032; -. 15959DR Reactome; REACT_111045; Developmental Biology. 15960DR NextBio; 19588; -. 15961DR ArrayExpress; O43316; -. 15962DR Bgee; O43316; -. 15963DR CleanEx; HS_PAX4; -. 15964DR Genevestigator; O43316; -. 15965DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 15966DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. 15967DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro. 15968DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. 15969DR GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome. 15970DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. 15971DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 15972DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. 15973DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 15974DR InterPro; IPR017970; Homeobox_CS. 15975DR InterPro; IPR001356; Homeodomain. 15976DR InterPro; IPR009057; Homeodomain-like. 15977DR InterPro; IPR001523; Paired_box_N. 15978DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 15979DR Pfam; PF00046; Homeobox; 1. 15980DR Pfam; PF00292; PAX; 1. 15981DR PRINTS; PR00027; PAIREDBOX. 15982DR SMART; SM00389; HOX; 1. 15983DR SMART; SM00351; PAX; 1. 15984DR SUPFAM; SSF46689; Homeodomain_like; 2. 15985DR PROSITE; PS00027; HOMEOBOX_1; 1. 15986DR PROSITE; PS50071; HOMEOBOX_2; 1. 15987DR PROSITE; PS00034; PAIRED_1; 1. 15988DR PROSITE; PS51057; PAIRED_2; 1. 15989PE 1: Evidence at protein level; 15990KW Alternative splicing; Complete proteome; Developmental protein; 15991KW Diabetes mellitus; Differentiation; Disease mutation; DNA-binding; 15992KW Homeobox; Nucleus; Paired box; Polymorphism; Reference proteome; 15993KW Repressor; Transcription; Transcription regulation. 15994FT CHAIN 1 350 Paired box protein Pax-4. 15995FT /FTId=PRO_0000050180. 15996FT DOMAIN 5 131 Paired. 15997FT DNA_BIND 170 229 Homeobox. 15998FT REGION 278 350 Transcription repression. 15999FT VAR_SEQ 1 8 Missing (in isoform 3). 16000FT /FTId=VSP_036448. 16001FT VAR_SEQ 239 257 Missing (in isoform 2). 16002FT /FTId=VSP_002359. 16003FT VAR_SEQ 258 350 QSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKA 16004FT CLKPCWDCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAG 16005FT KATPTHFSHWP -> AVPWQCAHSSPACPGTTGSLLLSAVL 16006FT GNSTRKVSE (in isoform 2). 16007FT /FTId=VSP_002360. 16008FT VAR_SEQ 305 350 DCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAGKATPTH 16009FT FSHWP -> GHLPPQPNSLDSGLLCLPCPSSHCHLASLSGS 16010FT QALLWPGCPLLYGLE (in isoform 3). 16011FT /FTId=VSP_036449. 16012FT VARIANT 39 39 R -> Q. 16013FT /FTId=VAR_054879. 16014FT VARIANT 45 45 R -> W (associated with PKD 16015FT susceptbility). 16016FT /FTId=VAR_054880. 16017FT VARIANT 129 129 R -> W (in diabetes mellitus type 2). 16018FT /FTId=VAR_054881. 16019FT VARIANT 141 141 R -> W (confers susceptibility to 16020FT ketosis-prone diabetes mellitus). 16021FT /FTId=VAR_054882. 16022FT VARIANT 172 172 R -> W (in MODY9; the mutant sequence 16023FT represses the activity of the insulin and 16024FT glucagon promoters by only 35% compared 16025FT to 50% and 57% respectively with wild- 16026FT type sequence). 16027FT /FTId=VAR_054883. 16028FT VARIANT 191 191 R -> C. 16029FT /FTId=VAR_054884. 16030FT VARIANT 200 200 R -> H. 16031FT /FTId=VAR_054885. 16032FT VARIANT 200 200 R -> S. 16033FT /FTId=VAR_054886. 16034SQ SEQUENCE 350 AA; 37833 MW; 2C2343AF16AEAAAC CRC64; 16035 MHQDGISSMN QLGGLFVNGR PLPLDTRQQI VRLAVSGMRP CDISRILKVS NGCVSKILGR 16036 YYRTGVLEPK GIGGSKPRLA TPPVVARIAQ LKGECPALFA WEIQRQLCAE GLCTQDKTPS 16037 VSSINRVLRA LQEDQGLPCT RLRSPAVLAP AVLTPHSGSE TPRGTHPGTG HRNRTIFSPS 16038 QAEALEKEFQ RGQYPDSVAR GKLATATSLP EDTVRVWFSN RRAKWRRQEK LKWEMQLPGA 16039 SQGLTVPRVA PGIISAQQSP GSVPTAALPA LEPLGPSCYQ LCWATAPERC LSDTPPKACL 16040 KPCWDCGSFL LPVIAPSCVD VAWPCLDASL AHHLIGGAGK ATPTHFSHWP 16041// 16042ID PAX5_HUMAN Reviewed; 391 AA. 16043AC Q02548; A3QVP6; A3QVP7; A3QVP8; O75933; 16044DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. 16045DT 01-OCT-1993, sequence version 1. 16046DT 13-JUN-2012, entry version 114. 16047DE RecName: Full=Paired box protein Pax-5; 16048DE AltName: Full=B-cell-specific transcription factor; 16049DE Short=BSAP; 16050GN Name=PAX5; 16051OS Homo sapiens (Human). 16052OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 16053OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 16054OC Catarrhini; Hominidae; Homo. 16055OX NCBI_TaxID=9606; 16056RN [1] 16057RP NUCLEOTIDE SEQUENCE [MRNA]. 16058RX MEDLINE=92387536; PubMed=1516825; 16059RA Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P., 16060RA Maurer-Fogy I., Busslinger M.; 16061RT "Pax-5 encodes the transcription factor BSAP and is expressed in B 16062RT lymphocytes, the developing CNS, and adult testis."; 16063RL Genes Dev. 6:1589-1607(1992). 16064RN [2] 16065RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-333, CHROMOSOMAL TRANSLOCATION WITH 16066RP ZNF521, CHROMOSOMAL TRANSLOCATION WITH FOXP1, AND CHROMOSOMAL 16067RP TRANSLOCATION WITH ETV6. 16068RX PubMed=17344859; DOI=10.1038/nature05690; 16069RA Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E., 16070RA Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., 16071RA Pui C.-H., Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.; 16072RT "Genome-wide analysis of genetic alterations in acute lymphoblastic 16073RT leukaemia."; 16074RL Nature 446:758-764(2007). 16075RN [3] 16076RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-197. 16077RX MEDLINE=98416211; PubMed=9742255; DOI=10.1093/nar/26.19.4497; 16078RA Verkoczy L.K., Berinstein N.L.; 16079RT "Isolation of genes negatively or positively co-expressed with human 16080RT recombination activating gene 1 (RAG1) by differential display PCR (DD 16081RT RT-PCR)."; 16082RL Nucleic Acids Res. 26:4497-4507(1998). 16083RN [4] 16084RP INTERACTION WITH TLE4. 16085RX MEDLINE=20271869; PubMed=10811620; DOI=10.1093/emboj/19.10.2292; 16086RA Eberhard D., Jimenez G., Heavey B., Busslinger M.; 16087RT "Transcriptional repression by Pax5 (BSAP) through interaction with 16088RT corepressors of the Groucho family."; 16089RL EMBO J. 19:2292-2303(2000). 16090CC -!- FUNCTION: May play an important role in B-cell differentiation as 16091CC well as neural development and spermatogenesis. Involved in the 16092CC regulation of the CD19 gene, a B-lymphoid-specific target gene. 16093CC -!- SUBUNIT: Interacts with DAXX (By similarity). Binds DNA as a 16094CC monomer. Binds TLE4. 16095CC -!- SUBCELLULAR LOCATION: Nucleus. 16096CC -!- DEVELOPMENTAL STAGE: Expressed at early B-cell differentiation, in 16097CC the developing CNS and in adult testis. 16098CC -!- PTM: O-glycosylated (Probable). 16099CC -!- DISEASE: Note=A chromosomal aberration involving PAX5 is a cause 16100CC of acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2) 16101CC with ZNF521. Translocation t(9;3)(p13;p14.1) with FOXP1. 16102CC Translocation t(9;12)(p13;p13) with ETV6. 16103CC -!- SIMILARITY: Contains 1 paired domain. 16104CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology 16105CC and Haematology; 16106CC URL="http://atlasgeneticsoncology.org/Genes/PAX5ID62.html"; 16107CC ----------------------------------------------------------------------- 16108CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 16109CC Distributed under the Creative Commons Attribution-NoDerivs License 16110CC ----------------------------------------------------------------------- 16111DR EMBL; M96944; AAA58397.1; -; mRNA. 16112DR EMBL; DQ841178; ABI30005.1; ALT_TERM; mRNA. 16113DR EMBL; DQ845345; ABI33104.1; ALT_TERM; mRNA. 16114DR EMBL; DQ845346; ABI33105.1; ALT_TERM; mRNA. 16115DR EMBL; AF080573; AAC35286.1; -; mRNA. 16116DR IPI; IPI00026209; -. 16117DR PIR; A44063; A44063. 16118DR RefSeq; NP_057953.1; NM_016734.1. 16119DR UniGene; Hs.654464; -. 16120DR PDB; 1K78; X-ray; 2.25 A; A/E/I=1-149. 16121DR PDB; 1MDM; X-ray; 2.80 A; A=1-149. 16122DR PDBsum; 1K78; -. 16123DR PDBsum; 1MDM; -. 16124DR ProteinModelPortal; Q02548; -. 16125DR SMR; Q02548; 19-142, 222-281. 16126DR IntAct; Q02548; 2. 16127DR STRING; Q02548; -. 16128DR PhosphoSite; Q02548; -. 16129DR DMDM; 417449; -. 16130DR PRIDE; Q02548; -. 16131DR DNASU; 5079; -. 16132DR Ensembl; ENST00000358127; ENSP00000350844; ENSG00000196092. 16133DR GeneID; 5079; -. 16134DR KEGG; hsa:5079; -. 16135DR UCSC; uc003zzo.1; human. 16136DR CTD; 5079; -. 16137DR GeneCards; GC09M036828; -. 16138DR HGNC; HGNC:8619; PAX5. 16139DR HPA; CAB026269; -. 16140DR HPA; CAB026869; -. 16141DR MIM; 167414; gene. 16142DR neXtProt; NX_Q02548; -. 16143DR PharmGKB; PA32959; -. 16144DR eggNOG; NOG326044; -. 16145DR HOGENOM; HOG000230938; -. 16146DR HOVERGEN; HBG009115; -. 16147DR InParanoid; Q02548; -. 16148DR KO; K09383; -. 16149DR OMA; HSIASTG; -. 16150DR OrthoDB; EOG4DZ1VJ; -. 16151DR EvolutionaryTrace; Q02548; -. 16152DR NextBio; 19592; -. 16153DR ArrayExpress; Q02548; -. 16154DR Bgee; Q02548; -. 16155DR CleanEx; HS_PAX5; -. 16156DR Genevestigator; Q02548; -. 16157DR GermOnline; ENSG00000196092; Homo sapiens. 16158DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 16159DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. 16160DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. 16161DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. 16162DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW. 16163DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. 16164DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. 16165DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 16166DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 16167DR InterPro; IPR009057; Homeodomain-like. 16168DR InterPro; IPR001523; Paired_box_N. 16169DR InterPro; IPR022130; Pax2_C. 16170DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 16171DR Pfam; PF00292; PAX; 1. 16172DR Pfam; PF12403; Pax2_C; 1. 16173DR PRINTS; PR00027; PAIREDBOX. 16174DR SMART; SM00351; PAX; 1. 16175DR SUPFAM; SSF46689; Homeodomain_like; 1. 16176DR PROSITE; PS00034; PAIRED_1; 1. 16177DR PROSITE; PS51057; PAIRED_2; 1. 16178PE 1: Evidence at protein level; 16179KW 3D-structure; Chromosomal rearrangement; Complete proteome; 16180KW Developmental protein; Differentiation; DNA-binding; Glycoprotein; 16181KW Neurogenesis; Nucleus; Paired box; Polymorphism; Proto-oncogene; 16182KW Reference proteome; Spermatogenesis; Transcription; 16183KW Transcription regulation. 16184FT CHAIN 1 391 Paired box protein Pax-5. 16185FT /FTId=PRO_0000050183. 16186FT DOMAIN 16 142 Paired. 16187FT SITE 158 159 Breakpoint for translocation to form 16188FT PAX5-ETV6. 16189FT SITE 260 261 Breakpoint for translocation to form 16190FT PAX5-FOXP1. 16191FT SITE 303 304 Breakpoint for translocation to form 16192FT PAX5-ZNF521. 16193FT VARIANT 322 322 A -> T (in dbSNP:rs34810717). 16194FT /FTId=VAR_034370. 16195FT CONFLICT 99 99 I -> F (in Ref. 3; AAC35286). 16196FT CONFLICT 141 143 TKV -> PKL (in Ref. 3; AAC35286). 16197FT HELIX 35 46 16198FT HELIX 51 58 16199FT HELIX 62 75 16200FT STRAND 89 91 16201FT HELIX 93 105 16202FT HELIX 111 120 16203FT TURN 126 128 16204FT HELIX 132 140 16205SQ SEQUENCE 391 AA; 42149 MW; DB37E6EACD9F993A CRC64; 16206 MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV 16207 SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA 16208 ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS 16209 ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV 16210 FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP 16211 IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF 16212 PNPGLLGSPY YYSAAARGAA PPAAATAYDR H 16213// 16214ID PAX6_HUMAN Reviewed; 422 AA. 16215AC P26367; Q6N006; Q99413; 16216DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. 16217DT 15-JUL-1999, sequence version 2. 16218DT 13-JUN-2012, entry version 151. 16219DE RecName: Full=Paired box protein Pax-6; 16220DE AltName: Full=Aniridia type II protein; 16221DE AltName: Full=Oculorhombin; 16222GN Name=PAX6; Synonyms=AN2; 16223OS Homo sapiens (Human). 16224OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 16225OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 16226OC Catarrhini; Hominidae; Homo. 16227OX NCBI_TaxID=9606; 16228RN [1] 16229RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 16230RC TISSUE=Fetal eye; 16231RX MEDLINE=92103673; PubMed=1684738; DOI=10.1016/0092-8674(91)90284-6; 16232RA Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T., 16233RA van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M., 16234RA Royer-Pokora B., Collins F.S., Swaroop A., Strong L.C., Saunders G.F.; 16235RT "Positional cloning and characterization of a paired box- and 16236RT homeobox-containing gene from the aniridia region."; 16237RL Cell 67:1059-1074(1991). 16238RN [2] 16239RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 16240RX MEDLINE=94258210; PubMed=1345175; DOI=10.1038/ng1192-232; 16241RA Glaser T., Walton D.S., Maas R.L.; 16242RT "Genomic structure, evolutionary conservation and aniridia mutations 16243RT in the human PAX6 gene."; 16244RL Nat. Genet. 2:232-239(1992). 16245RN [3] 16246RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 16247RA Liu J., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.; 16248RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. 16249RN [4] 16250RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A). 16251RC TISSUE=Cerebellum; 16252RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; 16253RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., 16254RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., 16255RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., 16256RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; 16257RT "The full-ORF clone resource of the German cDNA consortium."; 16258RL BMC Genomics 8:399-399(2007). 16259RN [5] 16260RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 16261RX PubMed=16554811; DOI=10.1038/nature04632; 16262RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., 16263RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., 16264RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., 16265RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., 16266RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., 16267RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., 16268RA Sakaki Y.; 16269RT "Human chromosome 11 DNA sequence and analysis including novel gene 16270RT identification."; 16271RL Nature 440:497-500(2006). 16272RN [6] 16273RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 16274RC TISSUE=Lung; 16275RX PubMed=15489334; DOI=10.1101/gr.2596504; 16276RG The MGC Project Team; 16277RT "The status, quality, and expansion of the NIH full-length cDNA 16278RT project: the Mammalian Gene Collection (MGC)."; 16279RL Genome Res. 14:2121-2127(2004). 16280RN [7] 16281RP ALTERNATIVE SPLICING, AND DNA-BINDING. 16282RX MEDLINE=95047352; PubMed=7958875; 16283RA Epstein J.A., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L.; 16284RT "Two independent and interactive DNA-binding subdomains of the Pax6 16285RT paired domain are regulated by alternative splicing."; 16286RL Genes Dev. 8:2022-2034(1994). 16287RN [8] 16288RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-136. 16289RX PubMed=10346815; 16290RA Xu H.E., Rould M.A., Xu W., Epstein J.A., Maas R.L., Pabo C.O.; 16291RT "Crystal structure of the human Pax-6 paired domain-DNA complex 16292RT reveals specific roles for the linker region and carboxyl-terminal 16293RT subdomain in DNA binding."; 16294RL Genes Dev. 13:1263-1275(1999). 16295RN [9] 16296RP REVIEW ON VARIANTS. 16297RX MEDLINE=98141676; PubMed=9482572; 16298RX DOI=10.1002/(SICI)1098-1004(1998)11:2<93::AID-HUMU1>3.3.CO;2-J; 16299RA Prosser J., van Heyningen V.; 16300RT "PAX6 mutations reviewed."; 16301RL Hum. Mutat. 11:93-108(1998). 16302RN [10] 16303RP STRUCTURE BY NMR OF 211-277. 16304RG RIKEN structural genomics initiative (RSGI); 16305RT "Solution structure of the homeobox domain of the human paired box 16306RT protein PAX-6."; 16307RL Submitted (NOV-2005) to the PDB data bank. 16308RN [11] 16309RP VARIANT AN TRP-208. 16310RX MEDLINE=93372853; PubMed=8364574; DOI=10.1093/hmg/2.7.915; 16311RA Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D., 16312RA Fekete G., van Heyningen V.; 16313RT "PAX6 mutations in aniridia."; 16314RL Hum. Mol. Genet. 2:915-920(1993). 16315RN [12] 16316RP VARIANT PAN GLY-26. 16317RX MEDLINE=94214497; PubMed=8162071; DOI=10.1038/ng0294-168; 16318RA Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D., 16319RA Adams R.J., Punnet H.H., van Heyningen V.; 16320RT "Mutations at the PAX6 locus are found in heterogeneous anterior 16321RT segment malformations including Peters' anomaly."; 16322RL Nat. Genet. 6:168-173(1994). 16323RN [13] 16324RP VARIANTS FOVHYP CYS-125 AND CYS-128. 16325RX MEDLINE=96225435; PubMed=8640214; DOI=10.1038/ng0696-141; 16326RA Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.; 16327RT "PAX6 missense mutation in isolated foveal hypoplasia."; 16328RL Nat. Genet. 13:141-142(1996). 16329RN [14] 16330RP VARIANT AN ARG-87, AND VARIANT GLY-26. 16331RX MEDLINE=97227282; PubMed=9147640; DOI=10.1093/hmg/6.3.381; 16332RA Tang H.K., Chao L.-Y., Saunders G.F.; 16333RT "Functional analysis of paired box missense mutations in the PAX6 16334RT gene."; 16335RL Hum. Mol. Genet. 6:381-386(1997). 16336RN [15] 16337RP VARIANT AN 22-PRO--ARG-26 DEL. 16338RX MEDLINE=97428347; PubMed=9281415; DOI=10.1006/mcpr.1997.0117; 16339RA Axton R., Hanson I.M., Love J., Seawright A., Prosser J., 16340RA van Heyningen V.; 16341RT "Combined SSCP/heteroduplex analysis in the screening for PAX6 16342RT mutations."; 16343RL Mol. Cell. Probes 11:287-292(1997). 16344RN [16] 16345RP VARIANT AN TRP-18. 16346RX MEDLINE=99006892; PubMed=9792406; 16347RX DOI=10.1002/(SICI)1098-1004(1998)12:5<304::AID-HUMU3>3.3.CO;2-Y; 16348RA Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V., 16349RA Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.; 16350RT "Ten novel mutations found in Aniridia."; 16351RL Hum. Mutat. 12:304-313(1998). 16352RN [17] 16353RP VARIANT EYE MALFORMATIONS ARG-422. 16354RX MEDLINE=98199717; PubMed=9538891; 16355RA Azuma N., Yamada M.; 16356RT "Missense mutation at the C-terminus of the PAX6 gene in ocular 16357RT anterior segment anomalies."; 16358RL Invest. Ophthalmol. Vis. Sci. 39:828-830(1998). 16359RN [18] 16360RP VARIANTS AN SER-17; VAL-29; GLN-44 AND HIS-178. 16361RX MEDLINE=99072581; PubMed=9856761; 16362RA Azuma N., Hotta Y., Tanaka H., Yamada M.; 16363RT "Missense mutations in the PAX6 gene in aniridia."; 16364RL Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998). 16365RN [19] 16366RP VARIANT PAN ASP-53. 16367RX MEDLINE=99375017; PubMed=10441571; DOI=10.1086/302529; 16368RA Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.; 16369RT "Missense mutation in the alternative splice region of the PAX6 gene 16370RT in eye anomalies."; 16371RL Am. J. Hum. Genet. 65:656-663(1999). 16372RN [20] 16373RP ALTERNATIVE SPLICING, AND VARIANTS AN SER-42; LEU-53; PRO-63; GLU-79 16374RP AND GLN-208. 16375RX MEDLINE=99250762; PubMed=10234503; DOI=10.1038/sj.ejhg.5200308; 16376RA Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.; 16377RT "Mutational analysis of PAX6: 16 novel mutations including 5 missense 16378RT mutations with a mild aniridia phenotype."; 16379RL Eur. J. Hum. Genet. 7:274-286(1999). 16380RN [21] 16381RP VARIANTS AN PRO-33; PRO-43 AND ASP-126, AND VARIANT FOVHYP VAL-64. 16382RX MEDLINE=99135896; PubMed=9931324; DOI=10.1093/hmg/8.2.165; 16383RA Hanson I.M., Churchill A., Love J., Axton R., Moore T., Clarke M., 16384RA Meire F., van Heyningen V.; 16385RT "Missense mutations in the most ancient residues of the PAX6 paired 16386RT domain underlie a spectrum of human congenital eye malformations."; 16387RL Hum. Mol. Genet. 8:165-172(1999). 16388RN [22] 16389RP VARIANTS AN SER-29; ARG-119 AND ALA-353. 16390RA Wildhardt G.; 16391RL Unpublished observations (APR-1999). 16392RN [23] 16393RP VARIANT AN 37-ALA--PRO-39 DEL. 16394RA Saunders G.F.; 16395RL Unpublished observations (AUG-1999). 16396RN [24] 16397RP VARIANT NYSTAGMUS ARG-118. 16398RX MEDLINE=20410622; PubMed=10955655; DOI=10.1007/s004170000124; 16399RA Sonoda S., Isashiki Y., Tabata Y., Kimura K., Kakiuchi T., Ohba N.; 16400RT "A novel PAX6 gene mutation (P118R) in a family with congenital 16401RT nystagmus associated with a variant form of aniridia."; 16402RL Graefes Arch. Clin. Exp. Ophthalmol. 238:552-558(2000). 16403RN [25] 16404RP VARIANT AN 37-ARG--PRO-39 DEL, AND VARIANT ASP-387. 16405RX PubMed=10737978; 16406RX DOI=10.1002/(SICI)1098-1004(200004)15:4<332::AID-HUMU5>3.0.CO;2-1; 16407RA Chao L.-Y., Huff V., Strong L.C., Saunders G.F.; 16408RT "Mutation in the PAX6 gene in twenty patients with aniridia."; 16409RL Hum. Mutat. 15:332-339(2000). 16410RN [26] 16411RP VARIANT AN ARG-119. 16412RX PubMed=11553050; DOI=10.1034/j.1399-0004.2001.600210.x; 16413RA Malandrini A., Mari F., Palmeri S., Gambelli S., Berti G., 16414RA Bruttini M., Bardelli A.M., Williamson K., van Heyningen V., 16415RA Renieri A.; 16416RT "PAX6 mutation in a family with aniridia, congenital ptosis, and 16417RT mental retardation."; 16418RL Clin. Genet. 60:151-154(2001). 16419RN [27] 16420RP VARIANTS AN GLN-375 AND ARG-422. 16421RX MEDLINE=21205761; PubMed=11309364; DOI=10.1093/hmg/10.9.911; 16422RA Singh S., Chao L.-Y., Mishra R., Davies J., Saunders G.F.; 16423RT "Missense mutation at the C-terminus of PAX6 negatively modulates 16424RT homeodomain function."; 16425RL Hum. Mol. Genet. 10:911-918(2001). 16426RN [28] 16427RP VARIANT AN THR-242. 16428RX PubMed=11826019; DOI=10.1136/jmg.39.1.16; 16429RA Morrison D., FitzPatrick D., Hanson I., Williamson K., 16430RA van Heyningen V., Fleck B., Jones I., Chalmers J., Campbell H.; 16431RT "National study of microphthalmia, anophthalmia, and coloboma (MAC) in 16432RT Scotland: investigation of genetic aetiology."; 16433RL J. Med. Genet. 39:16-22(2002). 16434RN [29] 16435RP VARIANT MORNING GLORY DISK ANOMALY SER-68, VARIANT COI SER-258, 16436RP VARIANT PAN PRO-363, AND VARIANTS BONH ILE-292; ARG-378; VAL-381 AND 16437RP ALA-391. 16438RX MEDLINE=22633032; PubMed=12721955; DOI=10.1086/375555; 16439RA Azuma N., Yamaguchi Y., Handa H., Tadokoro K., Asaka A., Kawase E., 16440RA Yamada M.; 16441RT "Mutations of the PAX6 gene detected in patients with a variety of 16442RT optic-nerve malformations."; 16443RL Am. J. Hum. Genet. 72:1565-1570(2003). 16444RN [30] 16445RP VARIANTS AN PRO-19 AND 22-PRO--ARG-26 DEL. 16446RX PubMed=12634864; DOI=10.1038/sj.ejhg.5200940; 16447RA Vincent M.-C., Pujo A.-L., Olivier D., Calvas P.; 16448RT "Screening for PAX6 gene mutations is consistent with 16449RT haploinsufficiency as the main mechanism leading to various ocular 16450RT defects."; 16451RL Eur. J. Hum. Genet. 11:163-169(2003). 16452RN [31] 16453RP VARIANTS AN ARG-46; ARG-52; THR-56; ASP-73 AND LYS-87, VARIANT 16454RP THR-321, CHARACTERIZATION OF VARIANTS AN ARG-46; ARG-52; LEU-53; 16455RP THR-56 AND ASP-73, AND CHARACTERIZATION OF VARIANT THR-321. 16456RX PubMed=12552561; DOI=10.1002/humu.10163; 16457RA Chao L.-Y., Mishra R., Strong L.C., Saunders G.F.; 16458RT "Missense mutations in the DNA-binding region and termination codon in 16459RT PAX6."; 16460RL Hum. Mutat. 21:138-145(2003). 16461RN [32] 16462RP CHARACTERIZATION OF VARIANT AN THR-242. 16463RX PubMed=16493447; DOI=10.1038/sj.ejhg.5201579; 16464RA D'Elia A.V., Puppin C., Pellizzari L., Pianta A., Bregant E., 16465RA Lonigro R., Tell G., Fogolari F., van Heyningen V., Damante G.; 16466RT "Molecular analysis of a human PAX6 homeobox mutant."; 16467RL Eur. J. Hum. Genet. 14:744-751(2006). 16468RN [33] 16469RP INVOLVEMENT IN ACAMD. 16470RX PubMed=17595013; DOI=10.1002/ajmg.a.31808; 16471RA Graziano C., D'Elia A.V., Mazzanti L., Moscano F., Guidelli Guidi S., 16472RA Scarano E., Turchetti D., Franzoni E., Romeo G., Damante G., Seri M.; 16473RT "A de novo nonsense mutation of PAX6 gene in a patient with aniridia, 16474RT ataxia, and mental retardation."; 16475RL Am. J. Med. Genet. A 143:1802-1805(2007). 16476RN [34] 16477RP VARIANT AN ARG-395. 16478RX PubMed=21850189; 16479RA Zhang X., Wang P., Li S., Xiao X., Guo X., Zhang Q.; 16480RT "Mutation spectrum of PAX6 in Chinese patients with aniridia."; 16481RL Mol. Vis. 17:2139-2147(2011). 16482CC -!- FUNCTION: Transcription factor with important functions in the 16483CC development of the eye, nose, central nervous system and pancreas. 16484CC Required for the differentiation of pancreatic islet alpha cells 16485CC (By similarity). Competes with PAX4 in binding to a common element 16486CC in the glucagon, insulin and somatostatin promoters. Regulates 16487CC specification of the ventral neuron subtypes by establishing the 16488CC correct progenitor domains (By similarity). Isoform 5a appears to 16489CC function as a molecular switch that specifies target genes. 16490CC -!- SUBUNIT: Interacts with MAF and MAFB (By similarity). Interacts 16491CC with TRIM11; this interaction leads to ubiquitination and 16492CC proteasomal degradation, as well as inhibition of transactivation, 16493CC possibly in part by preventing PAX6 binding to consensus DNA 16494CC sequences (By similarity). 16495CC -!- INTERACTION: 16496CC P63168:Dynll1 (xeno); NbExp=3; IntAct=EBI-747278, EBI-349121; 16497CC Q9NSC5:HOMER3; NbExp=3; IntAct=EBI-747278, EBI-748420; 16498CC -!- SUBCELLULAR LOCATION: Nucleus. 16499CC -!- ALTERNATIVE PRODUCTS: 16500CC Event=Alternative splicing; Named isoforms=3; 16501CC Name=1; 16502CC IsoId=P26367-1; Sequence=Displayed; 16503CC Name=5a; Synonyms=Pax6-5a; 16504CC IsoId=P26367-2; Sequence=VSP_002366; 16505CC Name=3; Synonyms=Pax6-5A,6*; 16506CC IsoId=P26367-3; Sequence=Not described; 16507CC -!- TISSUE SPECIFICITY: Fetal eye, brain, spinal cord and olfactory 16508CC epithelium. Isoform 5a is less abundant than the PAX6 shorter 16509CC form. 16510CC -!- DEVELOPMENTAL STAGE: Expressed in the developing eye and brain. 16511CC -!- PTM: Ubiquitinated by TRIM11, leading to ubiquitination and 16512CC proteasomal degradation (By similarity). 16513CC -!- DISEASE: Defects in PAX6 are the cause of aniridia (AN) 16514CC [MIM:106210]. A congenital, bilateral, panocular disorder 16515CC characterized by complete absence of the iris or extreme iris 16516CC hypoplasia. Aniridia is not just an isolated defect in iris 16517CC development but it is associated with macular and optic nerve 16518CC hypoplasia, cataract, corneal changes, nystagmus. Visual acuity is 16519CC generally low but is unrelated to the degree of iris hypoplasia. 16520CC Glaucoma is a secondary problem causing additional visual loss 16521CC over time. 16522CC -!- DISEASE: Defects in PAX6 are a cause of Peters anomaly (PAN) 16523CC [MIM:604229]. Peters anomaly consists of a central corneal 16524CC leukoma, absence of the posterior corneal stroma and Descemet 16525CC membrane, and a variable degree of iris and lenticular attachments 16526CC to the central aspect of the posterior cornea. 16527CC -!- DISEASE: Defects in PAX6 are a cause of foveal hypoplasia (FOVHYP) 16528CC [MIM:136520]. Foveal hypoplasia can be isolated or associated with 16529CC presenile cataract. Inheritance is autosomal dominant. 16530CC -!- DISEASE: Defects in PAX6 are a cause of keratitis hereditary 16531CC (KERH) [MIM:148190]. An ocular disorder characterized by corneal 16532CC opacification, recurrent stromal keratitis and vascularization. 16533CC -!- DISEASE: Defects in PAX6 are a cause of coloboma of iris choroid 16534CC and retina (COI) [MIM:120200]; also known as uveoretinal coloboma. 16535CC Ocular colobomas are a set of malformations resulting from 16536CC abnormal morphogenesis of the optic cup and stalk, and the fusion 16537CC of the fetal fissure (optic fissure). Severe colobomatous 16538CC malformations may cause as much as 10% of the childhood blindness. 16539CC The clinical presentation of ocular coloboma is variable. Some 16540CC individuals may present with minimal defects in the anterior iris 16541CC leaf without other ocular defects. More complex malformations 16542CC create a combination of iris, uveoretinal and/or optic nerve 16543CC defects without or with microphthalmia or even anophthalmia. 16544CC -!- DISEASE: Defects in PAX6 are a cause of coloboma of optic nerve 16545CC (COLON) [MIM:120430]. 16546CC -!- DISEASE: Defects in PAX6 are a cause of bilateral optic nerve 16547CC hypoplasia (BONH) [MIM:165550]; also known as bilateral optic 16548CC nerve aplasia. A congenital anomaly in which the optic disc 16549CC appears abnormally small. It may be an isolated finding or part of 16550CC a spectrum of anatomic and functional abnormalities that includes 16551CC partial or complete agenesis of the septum pellucidum, other 16552CC midline brain defects, cerebral anomalies, pituitary dysfunction, 16553CC and structural abnormalities of the pituitary. 16554CC -!- DISEASE: Defects in PAX6 are a cause of aniridia cerebellar ataxia 16555CC and mental deficiency (ACAMD) [MIM:206700]; also known as 16556CC Gillespie syndrome. A rare condition consisting of partial 16557CC rudimentary iris, cerebellar impairment of the ability to perform 16558CC coordinated voluntary movements, and mental retardation. 16559CC -!- SIMILARITY: Belongs to the paired homeobox family. 16560CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. 16561CC -!- SIMILARITY: Contains 1 paired domain. 16562CC -!- WEB RESOURCE: Name=Human PAX6 allelic variant database web site; 16563CC URL="http://pax6.hgu.mrc.ac.uk/"; 16564CC -!- WEB RESOURCE: Name=GeneReviews; 16565CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX6"; 16566CC ----------------------------------------------------------------------- 16567CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 16568CC Distributed under the Creative Commons Attribution-NoDerivs License 16569CC ----------------------------------------------------------------------- 16570DR EMBL; M77844; AAA59962.1; -; mRNA. 16571DR EMBL; M93650; AAA36416.1; -; mRNA. 16572DR EMBL; AY047583; AAK95849.1; -; mRNA. 16573DR EMBL; BX640762; CAE45868.1; -; mRNA. 16574DR EMBL; Z95332; CAG38363.1; -; Genomic_DNA. 16575DR EMBL; Z83307; CAG38363.1; JOINED; Genomic_DNA. 16576DR EMBL; Z83307; CAG38087.1; -; Genomic_DNA. 16577DR EMBL; Z95332; CAG38087.1; JOINED; Genomic_DNA. 16578DR EMBL; BC011953; AAH11953.1; -; mRNA. 16579DR IPI; IPI00218800; -. 16580DR IPI; IPI00449071; -. 16581DR PIR; A56674; A56674. 16582DR RefSeq; NP_000271.1; NM_000280.3. 16583DR RefSeq; NP_001121084.1; NM_001127612.1. 16584DR RefSeq; NP_001595.2; NM_001604.4. 16585DR UniGene; Hs.270303; -. 16586DR UniGene; Hs.611376; -. 16587DR PDB; 2CUE; NMR; -; A=211-277. 16588DR PDB; 6PAX; X-ray; 2.50 A; A=4-136. 16589DR PDBsum; 2CUE; -. 16590DR PDBsum; 6PAX; -. 16591DR ProteinModelPortal; P26367; -. 16592DR SMR; P26367; 4-136, 211-278. 16593DR IntAct; P26367; 5. 16594DR MINT; MINT-1465118; -. 16595DR STRING; P26367; -. 16596DR PhosphoSite; P26367; -. 16597DR DMDM; 6174889; -. 16598DR PRIDE; P26367; -. 16599DR DNASU; 5080; -. 16600DR Ensembl; ENST00000241001; ENSP00000241001; ENSG00000007372. 16601DR Ensembl; ENST00000379107; ENSP00000368401; ENSG00000007372. 16602DR Ensembl; ENST00000379109; ENSP00000368403; ENSG00000007372. 16603DR Ensembl; ENST00000379111; ENSP00000368406; ENSG00000007372. 16604DR Ensembl; ENST00000379115; ENSP00000368410; ENSG00000007372. 16605DR Ensembl; ENST00000379123; ENSP00000368418; ENSG00000007372. 16606DR Ensembl; ENST00000379129; ENSP00000368424; ENSG00000007372. 16607DR Ensembl; ENST00000379132; ENSP00000368427; ENSG00000007372. 16608DR Ensembl; ENST00000419022; ENSP00000404100; ENSG00000007372. 16609DR Ensembl; ENST00000439164; ENSP00000407893; ENSG00000007372. 16610DR GeneID; 5080; -. 16611DR KEGG; hsa:5080; -. 16612DR UCSC; uc001mtd.4; human. 16613DR CTD; 5080; -. 16614DR GeneCards; GC11M031768; -. 16615DR HGNC; HGNC:8620; PAX6. 16616DR HPA; CAB034143; -. 16617DR HPA; HPA030775; -. 16618DR MIM; 106210; phenotype. 16619DR MIM; 120200; phenotype. 16620DR MIM; 120430; phenotype. 16621DR MIM; 136520; phenotype. 16622DR MIM; 148190; phenotype. 16623DR MIM; 165550; phenotype. 16624DR MIM; 206700; phenotype. 16625DR MIM; 604229; phenotype. 16626DR MIM; 607108; gene. 16627DR neXtProt; NX_P26367; -. 16628DR Orphanet; 1065; Aniridia - cerebellar ataxia - intellectual deficit. 16629DR Orphanet; 2253; Foveal hypoplasia - presenile cataract. 16630DR Orphanet; 2334; Hereditary keratitis. 16631DR Orphanet; 250923; Isolated aniridia. 16632DR Orphanet; 137902; Isolated optic nerve hypoplasia. 16633DR Orphanet; 194; Ocular coloboma. 16634DR Orphanet; 708; Peters anomaly. 16635DR Orphanet; 893; WAGR syndrome. 16636DR PharmGKB; PA32960; -. 16637DR eggNOG; NOG326044; -. 16638DR GeneTree; ENSGT00650000093130; -. 16639DR HOVERGEN; HBG009115; -. 16640DR KO; K08031; -. 16641DR OMA; AGENTNS; -. 16642DR OrthoDB; EOG47PX63; -. 16643DR EvolutionaryTrace; P26367; -. 16644DR NextBio; 19596; -. 16645DR ArrayExpress; P26367; -. 16646DR Bgee; P26367; -. 16647DR CleanEx; HS_PAX6; -. 16648DR Genevestigator; P26367; -. 16649DR GermOnline; ENSG00000007372; Homo sapiens. 16650DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. 16651DR GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL. 16652DR GO; GO:0035035; F:histone acetyltransferase binding; ISS:BHF-UCL. 16653DR GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL. 16654DR GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL. 16655DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL. 16656DR GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:BHF-UCL. 16657DR GO; GO:0008134; F:transcription factor binding; ISS:BHF-UCL. 16658DR GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB. 16659DR GO; GO:0001568; P:blood vessel development; IMP:DFLAT. 16660DR GO; GO:0061303; P:cornea development in camera-type eye; IMP:DFLAT. 16661DR GO; GO:0042593; P:glucose homeostasis; IMP:DFLAT. 16662DR GO; GO:0061072; P:iris morphogenesis; IMP:DFLAT. 16663DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB. 16664DR GO; GO:0003322; P:pancreatic A cell development; IMP:BHF-UCL. 16665DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL. 16666DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB. 16667DR GO; GO:0007601; P:visual perception; TAS:ProtInc. 16668DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. 16669DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 16670DR InterPro; IPR017970; Homeobox_CS. 16671DR InterPro; IPR001356; Homeodomain. 16672DR InterPro; IPR009057; Homeodomain-like. 16673DR InterPro; IPR001523; Paired_box_N. 16674DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 16675DR Pfam; PF00046; Homeobox; 1. 16676DR Pfam; PF00292; PAX; 1. 16677DR PRINTS; PR00027; PAIREDBOX. 16678DR SMART; SM00389; HOX; 1. 16679DR SMART; SM00351; PAX; 1. 16680DR SUPFAM; SSF46689; Homeodomain_like; 2. 16681DR PROSITE; PS00027; HOMEOBOX_1; 1. 16682DR PROSITE; PS50071; HOMEOBOX_2; 1. 16683DR PROSITE; PS00034; PAIRED_1; 1. 16684DR PROSITE; PS51057; PAIRED_2; 1. 16685PE 1: Evidence at protein level; 16686KW 3D-structure; Alternative splicing; Complete proteome; 16687KW Developmental protein; Differentiation; Disease mutation; DNA-binding; 16688KW Homeobox; Mental retardation; Nucleus; Paired box; Peters anomaly; 16689KW Reference proteome; Repressor; Transcription; 16690KW Transcription regulation; Ubl conjugation. 16691FT CHAIN 1 422 Paired box protein Pax-6. 16692FT /FTId=PRO_0000050185. 16693FT DOMAIN 4 130 Paired. 16694FT DNA_BIND 210 269 Homeobox. 16695FT COMPBIAS 131 209 Gln/Gly-rich. 16696FT COMPBIAS 279 422 Pro/Ser/Thr-rich. 16697FT VAR_SEQ 47 47 Q -> QTHADAKVQVLDNQN (in isoform 5a). 16698FT /FTId=VSP_002366. 16699FT VARIANT 17 17 N -> S (in AN). 16700FT /FTId=VAR_003808. 16701FT VARIANT 18 18 G -> W (in AN). 16702FT /FTId=VAR_003809. 16703FT VARIANT 19 19 R -> P (in AN). 16704FT /FTId=VAR_047860. 16705FT VARIANT 22 26 Missing (in AN). 16706FT /FTId=VAR_008693. 16707FT VARIANT 26 26 R -> G (in PAN). 16708FT /FTId=VAR_003810. 16709FT VARIANT 29 29 I -> S (in AN). 16710FT /FTId=VAR_008694. 16711FT VARIANT 29 29 I -> V (in AN). 16712FT /FTId=VAR_003811. 16713FT VARIANT 33 33 A -> P (in AN). 16714FT /FTId=VAR_008695. 16715FT VARIANT 37 39 Missing (in AN). 16716FT /FTId=VAR_008696. 16717FT VARIANT 42 42 I -> S (in AN; mild). 16718FT /FTId=VAR_008697. 16719FT VARIANT 43 43 S -> P (in AN). 16720FT /FTId=VAR_008698. 16721FT VARIANT 44 44 R -> Q (in AN). 16722FT /FTId=VAR_003812. 16723FT VARIANT 46 46 L -> R (in AN; shows almost no binding 16724FT efficiency; transcriptional activation 16725FT ability is about 50% lower than that of 16726FT the wild-type protein). 16727FT /FTId=VAR_047861. 16728FT VARIANT 52 52 C -> R (in AN; shows almost no binding 16729FT efficiency; transcriptional activation 16730FT ability is about 50% lower than that of 16731FT the wild-type protein). 16732FT /FTId=VAR_047862. 16733FT VARIANT 53 53 V -> D (in PAN; also found in patients 16734FT with congenital cataract and foveal 16735FT hypoplasia). 16736FT /FTId=VAR_008700. 16737FT VARIANT 53 53 V -> L (in AN; mild; shows 50% lower DNA- 16738FT binding and transactivation ability than 16739FT the wild-type protein). 16740FT /FTId=VAR_008699. 16741FT VARIANT 56 56 I -> T (in AN; shows only one-quarter to 16742FT one-third the binding ability of the 16743FT normal wild-type protein; exhibits normal 16744FT transactivation). 16745FT /FTId=VAR_047863. 16746FT VARIANT 63 63 T -> P (in AN; mild). 16747FT /FTId=VAR_008701. 16748FT VARIANT 64 64 G -> V (in foveal hypoplasia; associated 16749FT with presenile cataract syndrome). 16750FT /FTId=VAR_008702. 16751FT VARIANT 68 68 P -> S (in morning glory disk anomaly; 16752FT significant impairment of transcriptional 16753FT activation ability). 16754FT /FTId=VAR_017540. 16755FT VARIANT 73 73 G -> D (in AN; shows almost no binding 16756FT efficiency; transcriptional activation 16757FT ability is about 80% of that of the wild- 16758FT type protein). 16759FT /FTId=VAR_047864. 16760FT VARIANT 79 79 A -> E (in AN; mild). 16761FT /FTId=VAR_008703. 16762FT VARIANT 87 87 I -> K (in AN). 16763FT /FTId=VAR_047865. 16764FT VARIANT 87 87 I -> R (in AN; loss of activity). 16765FT /FTId=VAR_003813. 16766FT VARIANT 118 118 P -> R (in a family with nystagmus 16767FT associated with a variant form of 16768FT aniridia). 16769FT /FTId=VAR_015065. 16770FT VARIANT 119 119 S -> R (in AN). 16771FT /FTId=VAR_008704. 16772FT VARIANT 125 125 R -> C (in FOVHYP; isolated). 16773FT /FTId=VAR_017541. 16774FT VARIANT 126 126 V -> D (in AN; atypical form). 16775FT /FTId=VAR_008705. 16776FT VARIANT 128 128 R -> C (in FOVHYP; isolated). 16777FT /FTId=VAR_003814. 16778FT VARIANT 178 178 Q -> H (in AN). 16779FT /FTId=VAR_003815. 16780FT VARIANT 208 208 R -> Q (in AN; mild). 16781FT /FTId=VAR_008706. 16782FT VARIANT 208 208 R -> W (in AN). 16783FT /FTId=VAR_003816. 16784FT VARIANT 242 242 R -> T (in AN; the mutant homeodomain 16785FT binds DNA as well as the wild-type 16786FT homeodomain; the mutant does not modify 16787FT the DNA-binding properties of the paired 16788FT domain; the steady-state levels of the 16789FT full length mutant protein are higher 16790FT than those of the wild-type one; a 16791FT responsive promoter is activated to a 16792FT higher extend by the mutant protein than 16793FT by the wild-type protein; the presence of 16794FT the mutation reduces sensitivity to 16795FT trypsin digestion). 16796FT /FTId=VAR_047866. 16797FT VARIANT 258 258 F -> S (in COI; significant impairment of 16798FT transcriptional activation ability). 16799FT /FTId=VAR_017542. 16800FT VARIANT 292 292 S -> I (in BONH; significant impairment 16801FT of ability to activate transcription). 16802FT /FTId=VAR_017543. 16803FT VARIANT 321 321 A -> T (shows about two-fold higher 16804FT binding efficiency than the normal wild- 16805FT type protein; transcriptional activation 16806FT ability is about 89% of that of the wild- 16807FT type protein). 16808FT /FTId=VAR_047867. 16809FT VARIANT 353 353 S -> A (in AN). 16810FT /FTId=VAR_008707. 16811FT VARIANT 363 363 S -> P (in PAN). 16812FT /FTId=VAR_017544. 16813FT VARIANT 375 375 P -> Q (in AN; reduced DNA binding 16814FT ability). 16815FT /FTId=VAR_015066. 16816FT VARIANT 378 378 Q -> R (in optic nerve aplasia). 16817FT /FTId=VAR_017545. 16818FT VARIANT 381 381 M -> V (in BONH). 16819FT /FTId=VAR_017546. 16820FT VARIANT 387 387 G -> D. 16821FT /FTId=VAR_047868. 16822FT VARIANT 391 391 T -> A (in BONH). 16823FT /FTId=VAR_017547. 16824FT VARIANT 395 395 G -> R (in AN). 16825FT /FTId=VAR_067698. 16826FT VARIANT 422 422 Q -> R (in AN and ocular anterior segment 16827FT anomalies; loss of DNA binding ability). 16828FT /FTId=VAR_008708. 16829FT CONFLICT 317 317 R -> L (in Ref. 1; AAA59962). 16830FT CONFLICT 369 369 Y -> C (in Ref. 4; CAE45868). 16831FT STRAND 6 8 16832FT STRAND 14 16 16833FT HELIX 23 34 16834FT HELIX 39 46 16835FT HELIX 50 63 16836FT STRAND 77 79 16837FT HELIX 81 93 16838FT HELIX 99 108 16839FT TURN 114 116 16840FT HELIX 120 133 16841FT HELIX 219 229 16842FT HELIX 237 246 16843FT HELIX 251 275 16844SQ SEQUENCE 422 AA; 46683 MW; C33CDD2C1B13C397 CRC64; 16845 MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY 16846 YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV 16847 SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ 16848 EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR 16849 ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP 16850 QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT 16851 SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR 16852 LQ 16853// 16854ID PAX7_HUMAN Reviewed; 520 AA. 16855AC P23759; Q0VA99; 16856DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. 16857DT 30-MAY-2000, sequence version 3. 16858DT 13-JUN-2012, entry version 132. 16859DE RecName: Full=Paired box protein Pax-7; 16860DE AltName: Full=HuP1; 16861GN Name=PAX7; Synonyms=HUP1; 16862OS Homo sapiens (Human). 16863OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 16864OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 16865OC Catarrhini; Hominidae; Homo. 16866OX NCBI_TaxID=9606; 16867RN [1] 16868RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING. 16869RX MEDLINE=97480728; PubMed=9339373; DOI=10.1006/geno.1997.4915; 16870RA Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B., 16871RA Horst J.; 16872RT "The genomic organization and the full coding region of the human PAX7 16873RT gene."; 16874RL Genomics 45:168-174(1997). 16875RN [2] 16876RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 16877RX PubMed=16710414; DOI=10.1038/nature04727; 16878RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., 16879RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., 16880RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., 16881RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., 16882RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., 16883RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., 16884RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., 16885RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., 16886RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., 16887RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., 16888RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., 16889RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., 16890RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., 16891RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., 16892RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., 16893RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., 16894RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., 16895RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., 16896RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., 16897RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., 16898RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., 16899RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., 16900RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., 16901RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., 16902RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., 16903RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., 16904RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., 16905RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., 16906RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., 16907RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., 16908RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., 16909RA Beck S., Rogers J., Bentley D.R.; 16910RT "The DNA sequence and biological annotation of human chromosome 1."; 16911RL Nature 441:315-321(2006). 16912RN [3] 16913RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 16914RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., 16915RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., 16916RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., 16917RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., 16918RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., 16919RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., 16920RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 16921RA Venter J.C.; 16922RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. 16923RN [4] 16924RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT). 16925RX PubMed=15489334; DOI=10.1101/gr.2596504; 16926RG The MGC Project Team; 16927RT "The status, quality, and expansion of the NIH full-length cDNA 16928RT project: the Mammalian Gene Collection (MGC)."; 16929RL Genome Res. 14:2121-2127(2004). 16930RN [5] 16931RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-467 (ISOFORM LONG). 16932RX MEDLINE=95075634; PubMed=7527137; DOI=10.1093/nar/22.22.4574; 16933RA Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.; 16934RT "Molecular cloning and characterization of a human PAX-7 cDNA 16935RT expressed in normal and neoplastic myocytes."; 16936RL Nucleic Acids Res. 22:4574-4582(1994). 16937RN [6] 16938RP NUCLEOTIDE SEQUENCE OF 30-195 (ISOFORM SHORT). 16939RX MEDLINE=89305521; PubMed=2501086; 16940RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; 16941RT "Conservation of the paired domain in metazoans and its structure in 16942RT three isolated human genes."; 16943RL EMBO J. 8:1183-1190(1989). 16944CC -!- FUNCTION: Probable transcription factor. May have a role in 16945CC myogenesis. 16946CC -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts 16947CC with DAXX. 16948CC -!- SUBCELLULAR LOCATION: Nucleus. 16949CC -!- ALTERNATIVE PRODUCTS: 16950CC Event=Alternative splicing; Named isoforms=2; 16951CC Name=Long; 16952CC IsoId=P23759-1; Sequence=Displayed; 16953CC Name=Short; 16954CC IsoId=P23759-2; Sequence=VSP_002370; 16955CC -!- DISEASE: Defects in PAX7 are a cause of rhabdomyosarcoma type 2 16956CC (RMS2) [MIM:268220]. It is a form of rhabdomyosarcoma, a highly 16957CC malignant tumor of striated muscle derived from primitive 16958CC mesenchimal cells and exhibiting differentiation along 16959CC rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most 16960CC frequently occurring soft tissue sarcomas and the most common in 16961CC children. It occurs in four forms: alveolar, pleomorphic, 16962CC embryonal and botryoidal rhabdomyosarcomas. Note=A chromosomal 16963CC aberration involving PAX7 is found in rhabdomyosarcoma. 16964CC Translocation t(1;13)(p36;q14) with FOXO1. The resulting protein 16965CC is a transcriptional activator. 16966CC -!- SIMILARITY: Belongs to the paired homeobox family. 16967CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. 16968CC -!- SIMILARITY: Contains 1 paired domain. 16969CC ----------------------------------------------------------------------- 16970CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 16971CC Distributed under the Creative Commons Attribution-NoDerivs License 16972CC ----------------------------------------------------------------------- 16973DR EMBL; X96743; CAA65520.1; -; mRNA. 16974DR EMBL; X96744; CAA65521.1; -; Genomic_DNA. 16975DR EMBL; X15042; CAA65521.1; JOINED; Genomic_DNA. 16976DR EMBL; X15250; CAA65521.1; JOINED; Genomic_DNA. 16977DR EMBL; X15251; CAA65521.1; JOINED; Genomic_DNA. 16978DR EMBL; X96745; CAA65521.1; JOINED; Genomic_DNA. 16979DR EMBL; X96746; CAA65521.1; JOINED; Genomic_DNA. 16980DR EMBL; X96747; CAA65521.1; JOINED; Genomic_DNA. 16981DR EMBL; X96748; CAA65521.1; JOINED; Genomic_DNA. 16982DR EMBL; X96744; CAA65522.1; -; Genomic_DNA. 16983DR EMBL; X15042; CAA65522.1; JOINED; Genomic_DNA. 16984DR EMBL; X15250; CAA65522.1; JOINED; Genomic_DNA. 16985DR EMBL; X15251; CAA65522.1; JOINED; Genomic_DNA. 16986DR EMBL; X96745; CAA65522.1; JOINED; Genomic_DNA. 16987DR EMBL; X96746; CAA65522.1; JOINED; Genomic_DNA. 16988DR EMBL; X96747; CAA65522.1; JOINED; Genomic_DNA. 16989DR EMBL; X96748; CAA65522.1; JOINED; Genomic_DNA. 16990DR EMBL; AL021528; CAA16432.1; -; Genomic_DNA. 16991DR EMBL; CH471134; EAW94853.1; -; Genomic_DNA. 16992DR EMBL; BC121165; AAI21166.1; -; mRNA. 16993DR EMBL; BC121166; AAI21167.1; -; mRNA. 16994DR EMBL; Z35141; CAA84513.1; -; mRNA. 16995DR IPI; IPI00004431; -. 16996DR IPI; IPI00012894; -. 16997DR PIR; S78502; S78502. 16998DR RefSeq; NP_001128726.1; NM_001135254.1. 16999DR RefSeq; NP_002575.1; NM_002584.2. 17000DR RefSeq; NP_039236.1; NM_013945.2. 17001DR UniGene; Hs.113253; -. 17002DR ProteinModelPortal; P23759; -. 17003DR SMR; P23759; 35-160, 217-275. 17004DR IntAct; P23759; 4. 17005DR MINT; MINT-7241806; -. 17006DR STRING; P23759; -. 17007DR DMDM; 8247951; -. 17008DR PRIDE; P23759; -. 17009DR Ensembl; ENST00000375375; ENSP00000364524; ENSG00000009709. 17010DR Ensembl; ENST00000400661; ENSP00000383502; ENSG00000009709. 17011DR GeneID; 5081; -. 17012DR KEGG; hsa:5081; -. 17013DR UCSC; uc001bay.3; human. 17014DR UCSC; uc001baz.3; human. 17015DR CTD; 5081; -. 17016DR GeneCards; GC01P018957; -. 17017DR HGNC; HGNC:8621; PAX7. 17018DR MIM; 167410; gene. 17019DR MIM; 268220; phenotype. 17020DR neXtProt; NX_P23759; -. 17021DR Orphanet; 99756; Alveolar rhabdomyosarcoma. 17022DR PharmGKB; PA32961; -. 17023DR eggNOG; NOG326044; -. 17024DR GeneTree; ENSGT00650000093130; -. 17025DR HOGENOM; HOG000230939; -. 17026DR HOVERGEN; HBG009115; -. 17027DR InParanoid; P23759; -. 17028DR KO; K09381; -. 17029DR OMA; MSILGNP; -. 17030DR OrthoDB; EOG4JM7PH; -. 17031DR PhylomeDB; P23759; -. 17032DR NextBio; 19602; -. 17033DR ArrayExpress; P23759; -. 17034DR Bgee; P23759; -. 17035DR CleanEx; HS_PAX7; -. 17036DR Genevestigator; P23759; -. 17037DR GermOnline; ENSG00000009709; Homo sapiens. 17038DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 17039DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. 17040DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc. 17041DR GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc. 17042DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 17043DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. 17044DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 17045DR InterPro; IPR017970; Homeobox_CS. 17046DR InterPro; IPR001356; Homeodomain. 17047DR InterPro; IPR009057; Homeodomain-like. 17048DR InterPro; IPR001523; Paired_box_N. 17049DR InterPro; IPR022106; Pax7. 17050DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 17051DR Pfam; PF00046; Homeobox; 1. 17052DR Pfam; PF00292; PAX; 1. 17053DR Pfam; PF12360; Pax7; 1. 17054DR PRINTS; PR00027; PAIREDBOX. 17055DR SMART; SM00389; HOX; 1. 17056DR SMART; SM00351; PAX; 1. 17057DR SUPFAM; SSF46689; Homeodomain_like; 2. 17058DR PROSITE; PS00027; HOMEOBOX_1; 1. 17059DR PROSITE; PS50071; HOMEOBOX_2; 1. 17060DR PROSITE; PS00034; PAIRED_1; 1. 17061DR PROSITE; PS51057; PAIRED_2; 1. 17062PE 2: Evidence at transcript level; 17063KW Alternative splicing; Chromosomal rearrangement; Complete proteome; 17064KW Developmental protein; DNA-binding; Homeobox; Nucleus; Paired box; 17065KW Proto-oncogene; Reference proteome; Transcription; 17066KW Transcription regulation. 17067FT CHAIN 1 520 Paired box protein Pax-7. 17068FT /FTId=PRO_0000050194. 17069FT DOMAIN 34 163 Paired. 17070FT DNA_BIND 217 276 Homeobox. 17071FT COMPBIAS 340 346 Poly-Ala. 17072FT VAR_SEQ 151 152 Missing (in isoform Short). 17073FT /FTId=VSP_002370. 17074SQ SEQUENCE 520 AA; 56896 MW; 3B0F8CC99D65699C CRC64; 17075 MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV 17076 EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE 17077 YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG 17078 EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH 17079 YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL 17080 PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS 17081 YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS 17082 ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQSEC LVPWASPVPI 17083 PSPTPRASCL FMESYKVVSG WGMSISQMEK LKSSQMEQFT 17084// 17085ID PAX9_HUMAN Reviewed; 341 AA. 17086AC P55771; Q99582; Q9UQR4; 17087DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 17088DT 30-MAY-2000, sequence version 3. 17089DT 13-JUN-2012, entry version 116. 17090DE RecName: Full=Paired box protein Pax-9; 17091GN Name=PAX9; 17092OS Homo sapiens (Human). 17093OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 17094OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 17095OC Catarrhini; Hominidae; Homo. 17096OX NCBI_TaxID=9606; 17097RN [1] 17098RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 17099RX MEDLINE=20461864; PubMed=10899593; DOI=10.1016/S0167-4781(00)00130-5; 17100RA Hetzer-Egger C., Schorpp M., Boehm T.; 17101RT "Evolutionary conservation of gene structures of the Pax1/9 gene 17102RT family."; 17103RL Biochim. Biophys. Acta 1492:517-521(2000). 17104RN [2] 17105RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 17106RC TISSUE=Lung; 17107RX PubMed=15489334; DOI=10.1101/gr.2596504; 17108RG The MGC Project Team; 17109RT "The status, quality, and expansion of the NIH full-length cDNA 17110RT project: the Mammalian Gene Collection (MGC)."; 17111RL Genome Res. 14:2121-2127(2004). 17112RN [3] 17113RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211. 17114RX MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292; 17115RA Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.; 17116RT "Chromosomal localization of seven PAX genes and cloning of a novel 17117RT family member, PAX-9."; 17118RL Nat. Genet. 3:292-298(1993). 17119RN [4] 17120RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-339. 17121RC TISSUE=Esophagus; 17122RX MEDLINE=97179475; PubMed=9021154; DOI=10.1007/s003359900351; 17123RA Peters H., Schuster G., Neubueser A., Richter T., Hoefler H.; 17124RT "Isolation of the Pax9 cDNA from adult human esophagus."; 17125RL Mamm. Genome 8:62-64(1997). 17126RN [5] 17127RP INTERACTION WITH KDM5B, MUTAGENESIS OF 173-VAL-PRO-174; 17128RP 179-VAL-PRO-180 AND PRO-189, AND FUNCTION. 17129RX PubMed=12657635; DOI=10.1074/jbc.M301994200; 17130RA Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J., 17131RA Freemont P.S.; 17132RT "Human PLU-1 has transcriptional repression properties and interacts 17133RT with the developmental transcription factors BF-1 and PAX9."; 17134RL J. Biol. Chem. 278:20507-20513(2003). 17135RN [6] 17136RP VARIANT STHAG3 SER-51. 17137RX MEDLINE=22671556; PubMed=12786960; 17138RX DOI=10.1034/j.1600-0722.2003.00036.x; 17139RA Mostowska A., Kobielak A., Biedziak B., Trzeciak W.H.; 17140RT "Novel mutation in the paired box sequence of PAX9 gene in a sporadic 17141RT form of oligodontia."; 17142RL Eur. J. Oral Sci. 111:272-276(2003). 17143CC -!- FUNCTION: Transcription factor required for normal development of 17144CC thymus, parathyroid glands, ultimobranchial bodies, teeth, 17145CC skeletal elements of skull and larynx as well as distal limbs (By 17146CC similarity). 17147CC -!- SUBUNIT: Interacts with KDM5B. 17148CC -!- SUBCELLULAR LOCATION: Nucleus. 17149CC -!- DISEASE: Defects in PAX9 are the cause of tooth agenesis selective 17150CC type 3 (STHAG3) [MIM:604625]. A form of selective tooth agenesis, 17151CC a common anomaly characterized by the congenital absence of one or 17152CC more teeth. Selective tooth agenesis without associated systemic 17153CC disorders has sometimes been divided into 2 types: oligodontia, 17154CC defined as agenesis of 6 or more permanent teeth, and hypodontia, 17155CC defined as agenesis of less than 6 teeth. The number in both cases 17156CC does not include absence of third molars (wisdom teeth). 17157CC -!- SIMILARITY: Contains 1 paired domain. 17158CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology 17159CC and Haematology; 17160CC URL="http://atlasgeneticsoncology.org/Genes/PAX9ID41644ch14q12.html"; 17161CC ----------------------------------------------------------------------- 17162CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 17163CC Distributed under the Creative Commons Attribution-NoDerivs License 17164CC ----------------------------------------------------------------------- 17165DR EMBL; AJ238381; CAB41533.1; -; Genomic_DNA. 17166DR EMBL; AJ238382; CAB41533.1; JOINED; Genomic_DNA. 17167DR EMBL; AJ238383; CAB41533.1; JOINED; Genomic_DNA. 17168DR EMBL; BC001159; AAH01159.1; -; mRNA. 17169DR EMBL; L09745; -; NOT_ANNOTATED_CDS; Genomic_DNA. 17170DR EMBL; X92850; CAA63436.1; -; mRNA. 17171DR IPI; IPI00413469; -. 17172DR PIR; S36155; S36155. 17173DR RefSeq; NP_006185.1; NM_006194.3. 17174DR UniGene; Hs.132576; -. 17175DR UniGene; Hs.609574; -. 17176DR ProteinModelPortal; P55771; -. 17177DR SMR; P55771; 8-130. 17178DR STRING; P55771; -. 17179DR DMDM; 8247954; -. 17180DR PRIDE; P55771; -. 17181DR DNASU; 5083; -. 17182DR Ensembl; ENST00000361487; ENSP00000355245; ENSG00000198807. 17183DR Ensembl; ENST00000402703; ENSP00000384817; ENSG00000198807. 17184DR GeneID; 5083; -. 17185DR KEGG; hsa:5083; -. 17186DR UCSC; uc001wty.4; human. 17187DR CTD; 5083; -. 17188DR GeneCards; GC14P037126; -. 17189DR HGNC; HGNC:8623; PAX9. 17190DR HPA; HPA038462; -. 17191DR MIM; 167416; gene. 17192DR MIM; 604625; phenotype. 17193DR neXtProt; NX_P55771; -. 17194DR Orphanet; 2227; Hypodontia. 17195DR PharmGKB; PA32963; -. 17196DR eggNOG; NOG252808; -. 17197DR HOGENOM; HOG000230938; -. 17198DR HOVERGEN; HBG009115; -. 17199DR InParanoid; P55771; -. 17200DR KO; K09382; -. 17201DR OMA; HGWQHAG; -. 17202DR OrthoDB; EOG4RBQJV; -. 17203DR PhylomeDB; P55771; -. 17204DR NextBio; 19612; -. 17205DR ArrayExpress; P55771; -. 17206DR Bgee; P55771; -. 17207DR CleanEx; HS_PAX9; -. 17208DR Genevestigator; P55771; -. 17209DR GermOnline; ENSG00000198807; Homo sapiens. 17210DR GO; GO:0005739; C:mitochondrion; IDA:HPA. 17211DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. 17212DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. 17213DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. 17214DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB. 17215DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 17216DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. 17217DR InterPro; IPR009057; Homeodomain-like. 17218DR InterPro; IPR001523; Paired_box_N. 17219DR InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd. 17220DR Pfam; PF00292; PAX; 1. 17221DR PRINTS; PR00027; PAIREDBOX. 17222DR SMART; SM00351; PAX; 1. 17223DR SUPFAM; SSF46689; Homeodomain_like; 1. 17224DR PROSITE; PS00034; PAIRED_1; 1. 17225DR PROSITE; PS51057; PAIRED_2; 1. 17226PE 1: Evidence at protein level; 17227KW Complete proteome; Developmental protein; Disease mutation; 17228KW DNA-binding; Nucleus; Paired box; Polymorphism; Reference proteome; 17229KW Transcription; Transcription regulation. 17230FT CHAIN 1 341 Paired box protein Pax-9. 17231FT /FTId=PRO_0000050203. 17232FT DOMAIN 4 130 Paired. 17233FT REGION 168 189 Interaction with KDM5B. 17234FT VARIANT 51 51 G -> S (in STHAG3). 17235FT /FTId=VAR_015698. 17236FT VARIANT 240 240 A -> P (in dbSNP:rs4904210). 17237FT /FTId=VAR_034371. 17238FT MUTAGEN 173 174 VP->AA: Abolishes interaction with KDM5B. 17239FT MUTAGEN 179 180 VP->AA: Abolishes interaction with KDM5B. 17240FT MUTAGEN 189 189 P->A: Abolishes interaction with KDM5B. 17241FT CONFLICT 211 211 V -> G (in Ref. 3; L09745). 17242SQ SEQUENCE 341 AA; 36310 MW; F5E6B0BC991E7C1D CRC64; 17243 MEPAFGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY 17244 NETGSILPGA IGGSKPRVTT PTVVKHIRTY KQRDPGIFAW EIRDRLLADG VCDKYNVPSV 17245 SSISRILRNK IGNLAQQGHY DSYKQHQPTP QPALPYNHIY SYPSPITAAA AKVPTPPGVP 17246 AIPGSVAMPR TWPSSHSVTD ILGIRSITDQ VSDSSPYHSP KVEEWSSLGR NNFPAAAPHA 17247 VNGLEKGALE QEAKYGQAPN GLPAVGSFVS ASSMAPYPTP AQVSPYMTYS AAPSGYVAGH 17248 GWQHAGGTSL SPHNCDIPAS LAFKGMQAAR EGSHSVTASA L 17249// 17250ID PAXI_HUMAN Reviewed; 591 AA. 17251AC P49023; B2RAI3; B7ZMB4; O14970; O14971; O60360; Q5HYA4; 17252DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. 17253DT 11-JAN-2011, sequence version 3. 17254DT 13-JUN-2012, entry version 135. 17255DE RecName: Full=Paxillin; 17256GN Name=PXN; 17257OS Homo sapiens (Human). 17258OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 17259OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; 17260OC Catarrhini; Hominidae; Homo. 17261OX NCBI_TaxID=9606; 17262RN [1] 17263RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT GLY-73. 17264RX MEDLINE=95197488; PubMed=7534286; DOI=10.1074/jbc.270.10.5039; 17265RA Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., 17266RA Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., 17267RA Chen L.B., Griffin J.D.; 17268RT "Molecular cloning of human paxillin, a focal adhesion protein 17269RT phosphorylated by P210BCR/ABL."; 17270RL J. Biol. Chem. 270:5039-5047(1995). 17271RN [2] 17272RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-73. 17273RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., 17274RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., 17275RA Lathrop M., Cox R.D., Bell G.I.; 17276RT "Transcription map of the 5cM region surrounding the hepatocyte 17277RT nuclear factor-1a/MODY3 gene on chromosome 12."; 17278RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 17279RN [3] 17280RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), AND VARIANT 17281RP GLY-73. 17282RC TISSUE=Placenta; 17283RX MEDLINE=97207310; PubMed=9054445; DOI=10.1074/jbc.272.11.7437; 17284RA Mazaki Y., Hashimoto S., Sabe H.; 17285RT "Monocyte cells and cancer cells express novel paxillin isoforms with 17286RT different binding properties to focal adhesion proteins."; 17287RL J. Biol. Chem. 272:7437-7444(1997). 17288RN [4] 17289RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT 17290RP GLY-73. 17291RC TISSUE=Placenta; 17292RX PubMed=14702039; DOI=10.1038/ng1285; 17293RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., 17294RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., 17295RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., 17296RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., 17297RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., 17298RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., 17299RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., 17300RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., 17301RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., 17302RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., 17303RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., 17304RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., 17305RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., 17306RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., 17307RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., 17308RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., 17309RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., 17310RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., 17311RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., 17312RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., 17313RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., 17314RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., 17315RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., 17316RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., 17317RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., 17318RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., 17319RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., 17320RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; 17321RT "Complete sequencing and characterization of 21,243 full-length human 17322RT cDNAs."; 17323RL Nat. Genet. 36:40-45(2004). 17324RN [5] 17325RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). 17326RC TISSUE=Fetal kidney; 17327RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; 17328RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., 17329RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., 17330RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., 17331RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; 17332RT "The full-ORF clone resource of the German cDNA consortium."; 17333RL BMC Genomics 8:399-399(2007). 17334RN [6] 17335RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 17336RX PubMed=16541075; DOI=10.1038/nature04569; 17337RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., 17338RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., 17339RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., 17340RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., 17341RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., 17342RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., 17343RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., 17344RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., 17345RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., 17346RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., 17347RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., 17348RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., 17349RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., 17350RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., 17351RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., 17352RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., 17353RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., 17354RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., 17355RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., 17356RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., 17357RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., 17358RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., 17359RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., 17360RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., 17361RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., 17362RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., 17363RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., 17364RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., 17365RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., 17366RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., 17367RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., 17368RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., 17369RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., 17370RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., 17371RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., 17372RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., 17373RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., 17374RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., 17375RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., 17376RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., 17377RA Kucherlapati R., Weinstock G., Gibbs R.A.; 17378RT "The finished DNA sequence of human chromosome 12."; 17379RL Nature 440:346-351(2006). 17380RN [7] 17381RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT 17382RP GLY-73. 17383RC TISSUE=Brain, and Testis; 17384RX PubMed=15489334; DOI=10.1101/gr.2596504; 17385RG The MGC Project Team; 17386RT "The status, quality, and expansion of the NIH full-length cDNA 17387RT project: the Mammalian Gene Collection (MGC)."; 17388RL Genome Res. 14:2121-2127(2004). 17389RN [8] 17390RP INTERACTION WITH ITGA4. 17391RX PubMed=10604475; DOI=10.1038/45264; 17392RA Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., 17393RA Ginsberg M.H.; 17394RT "Binding of paxillin to alpha4 integrins modifies integrin-dependent 17395RT biological responses."; 17396RL Nature 402:676-681(1999). 17397RN [9] 17398RP INTERACTION WITH GIT1. 17399RX PubMed=10938112; DOI=10.1128/MCB.20.17.6354-6363.2000; 17400RA Zhao Z.-S., Manser E., Loo T.-H., Lim L.; 17401RT "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes 17402RT focal complex disassembly."; 17403RL Mol. Cell. Biol. 20:6354-6363(2000). 17404RN [10] 17405RP INTERACTION WITH ASAP2. 17406RX MEDLINE=20214823; PubMed=10749932; 17407RA Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.; 17408RT "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an 17409RT ADP-ribosylation factor GTPase-activating protein activity, is 17410RT involved in paxillin recruitment to focal adhesions and cell 17411RT migration."; 17412RL Mol. Biol. Cell 11:1315-1327(2000). 17413RN [11] 17414RP PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181. 17415RX MEDLINE=21634701; PubMed=11774284; DOI=10.1002/ijc.1609; 17416RA Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., 17417RA Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E., 17418RA Akedo H.; 17419RT "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in 17420RT MM1 cancer cell migration."; 17421RL Int. J. Cancer 97:330-335(2002). 17422RN [12] 17423RP INTERACTION WITH RNF5. 17424RX PubMed=12861019; DOI=10.1128/MCB.23.15.5331-5345.2003; 17425RA Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., 17426RA Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., 17427RA Ronai Z.; 17428RT "RNF5, a RING finger protein that regulates cell motility by targeting 17429RT paxillin ubiquitination and altered localization."; 17430RL Mol. Cell. Biol. 23:5331-5345(2003). 17431RN [13] 17432RP PHOSPHORYLATION AT TYR-31 AND TYR-118, AND INTERACTION WITH PTK6. 17433RX PubMed=15572663; DOI=10.1128/MCB.24.24.10558-10572.2004; 17434RA Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.; 17435RT "Brk activates rac1 and promotes cell migration and invasion by 17436RT phosphorylating paxillin."; 17437RL Mol. Cell. Biol. 24:10558-10572(2004). 17438RN [14] 17439RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS 17440RP SPECTROMETRY. 17441RC TISSUE=Cervix carcinoma; 17442RX PubMed=16212419; DOI=10.1021/pr050134h; 17443RA Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; 17444RT "Phosphoproteome analysis of HeLa cells using stable isotope labeling 17445RT with amino acids in cell culture (SILAC)."; 17446RL J. Proteome Res. 4:1661-1671(2005). 17447RN [15] 17448RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS 17449RP SPECTROMETRY. 17450RC TISSUE=Mammary epithelium; 17451RX PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200; 17452RA Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., 17453RA Lauffenburger D.A., White F.M.; 17454RT "Time-resolved mass spectrometry of tyrosine phosphorylation sites in 17455RT the epidermal growth factor receptor signaling network reveals dynamic 17456RT modules."; 17457RL Mol. Cell. Proteomics 4:1240-1250(2005). 17458RN [16] 17459RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS 17460RP SPECTROMETRY. 17461RX PubMed=15592455; DOI=10.1038/nbt1046; 17462RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., 17463RA Zha X.-M., Polakiewicz R.D., Comb M.J.; 17464RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer 17465RT cells."; 17466RL Nat. Biotechnol. 23:94-101(2005). 17467RN [17] 17468RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS 17469RP SPECTROMETRY. 17470RC TISSUE=Leukemic T-cell; 17471RX PubMed=16094384; DOI=10.1038/nmeth776; 17472RA Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., 17473RA Bodenmiller B., Watts J.D., Hood L., Aebersold R.; 17474RT "Quantitative phosphoproteome analysis using a dendrimer conjugation 17475RT chemistry and tandem mass spectrometry."; 17476RL Nat. Methods 2:591-598(2005). 17477RN [18] 17478RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, AND 17479RP MASS SPECTROMETRY. 17480RC TISSUE=Cervix carcinoma; 17481RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; 17482RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., 17483RA Mann M.; 17484RT "Global, in vivo, and site-specific phosphorylation dynamics in 17485RT signaling networks."; 17486RL Cell 127:635-648(2006). 17487RN [19] 17488RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS 17489RP SPECTROMETRY. 17490RC TISSUE=Cervix carcinoma; 17491RX PubMed=16964243; DOI=10.1038/nbt1240; 17492RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; 17493RT "A probability-based approach for high-throughput protein 17494RT phosphorylation analysis and site localization."; 17495RL Nat. Biotechnol. 24:1285-1292(2006). 17496RN [20] 17497RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS 17498RP SPECTROMETRY. 17499RC TISSUE=Lung carcinoma; 17500RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; 17501RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., 17502RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., 17503RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., 17504RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., 17505RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; 17506RT "Global survey of phosphotyrosine signaling identifies oncogenic 17507RT kinases in lung cancer."; 17508RL Cell 131:1190-1203(2007). 17509RN [21] 17510RP PHOSPHORYLATION AT SER-244. 17511RX PubMed=18042622; DOI=10.1242/jcs.018218; 17512RA Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y., 17513RA Hisanaga S., Tanoue A.; 17514RT "Cdk5 regulates differentiation of oligodendrocyte precursor cells 17515RT through the direct phosphorylation of paxillin."; 17516RL J. Cell Sci. 120:4355-4366(2007). 17517RN [22] 17518RP INTERACTION WITH NEK3. 17519RX PubMed=17297458; DOI=10.1038/sj.onc.1210264; 17520RA Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E., 17521RA Clevenger C.V.; 17522RT "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization 17523RT and motility of breast cancer cells."; 17524RL Oncogene 26:4668-4678(2007). 17525RN [23] 17526RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; TYR-88 AND TYR-118, 17527RP AND MASS SPECTROMETRY. 17528RC TISSUE=Mammary epithelium; 17529RX PubMed=17389395; DOI=10.1073/pnas.0608638104; 17530RA Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; 17531RT "Multiple reaction monitoring for robust quantitative proteomic 17532RT analysis of cellular signaling networks."; 17533RL Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). 17534RN [24] 17535RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS 17536RP SPECTROMETRY. 17537RC TISSUE=Cervix carcinoma; 17538RX PubMed=18220336; DOI=10.1021/pr0705441; 17539RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., 17540RA Yates J.R. III; 17541RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for 17542RT efficient phosphoproteomic analysis."; 17543RL J. Proteome Res. 7:1346-1351(2008). 17544RN [25] 17545RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS 17546RP SPECTROMETRY. 17547RC TISSUE=Cervix carcinoma; 17548RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; 17549RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., 17550RA Greff Z., Keri G., Stemmann O., Mann M.; 17551RT "Kinase-selective enrichment enables quantitative phosphoproteomics of 17552RT the kinome across the cell cycle."; 17553RL Mol. Cell 31:438-448(2008). 17554RN [26] 17555RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126; 17556RP SER-130 AND SER-137, AND MASS SPECTROMETRY. 17557RC TISSUE=Cervix carcinoma; 17558RX PubMed=18669648; DOI=10.1073/pnas.0805139105; 17559RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., 17560RA Elledge S.J., Gygi S.P.; 17561RT "A quantitative atlas of mitotic phosphorylation."; 17562RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). 17563RN [27] 17564RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE 17565RP SCALE ANALYSIS] AT SER-106, AND MASS SPECTROMETRY. 17566RC TISSUE=Embryonic kidney; 17567RX PubMed=19413330; DOI=10.1021/ac9004309; 17568RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., 17569RA Mohammed S.; 17570RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in 17571RT a refined SCX-based approach."; 17572RL Anal. Chem. 81:4493-4501(2009). 17573RN [28] 17574RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31; TYR-88 AND TYR-118, 17575RP AND MASS SPECTROMETRY. 17576RC TISSUE=Mammary epithelium; 17577RX PubMed=19534553; DOI=10.1021/pr900044c; 17578RA Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., 17579RA Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., 17580RA Wiley H.S., Qian W.-J.; 17581RT "An extensive survey of tyrosine phosphorylation revealing new sites 17582RT in human mammary epithelial cells."; 17583RL J. Proteome Res. 8:3852-3861(2009). 17584RN [29] 17585RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND THR-318, 17586RP AND MASS SPECTROMETRY. 17587RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; 17588RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., 17589RA Mann M., Daub H.; 17590RT "Large-scale proteomics analysis of the human kinome."; 17591RL Mol. Cell. Proteomics 8:1751-1764(2009). 17592RN [30] 17593RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, AND MASS 17594RP SPECTROMETRY. 17595RC TISSUE=Leukemic T-cell; 17596RX PubMed=19690332; DOI=10.1126/scisignal.2000007; 17597RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., 17598RA Rodionov V., Han D.K.; 17599RT "Quantitative phosphoproteomic analysis of T cell receptor signaling 17600RT reveals system-wide modulation of protein-protein interactions."; 17601RL Sci. Signal. 2:RA46-RA46(2009). 17602RN [31] 17603RP INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 17604RP 7-LEU-LEU-8. 17605RX PubMed=20489202; DOI=10.1074/jbc.M110.128470; 17606RA Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.; 17607RT "Crystal structure of CCM3, a cerebral cavernous malformation protein 17608RT critical for vascular integrity."; 17609RL J. Biol. Chem. 285:24099-24107(2010). 17610RN [32] 17611RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 17612RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; 17613RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., 17614RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; 17615RT "Initial characterization of the human central proteome."; 17616RL BMC Syst. Biol. 5:17-17(2011). 17617RN [33] 17618RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH 17619RP PTK2/FAK1, AND INTERACTION WITH PTK2/FAK1. 17620RX PubMed=14527389; DOI=10.1016/j.str.2003.08.010; 17621RA Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M., 17622RA Arold S.T.; 17623RT "Molecular recognition of paxillin LD motifs by the focal adhesion 17624RT targeting domain."; 17625RL Structure 11:1207-1217(2003). 17626RN [34] 17627RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH 17628RP PTK2B/PYK2, AND INTERACTION WITH PTK2B/PYK2. 17629RX PubMed=19358827; DOI=10.1016/j.bbrc.2009.04.011; 17630RA Lulo J., Yuzawa S., Schlessinger J.; 17631RT "Crystal structures of free and ligand-bound focal adhesion targeting 17632RT domain of Pyk2."; 17633RL Biochem. Biophys. Res. Commun. 383:347-352(2009). 17634CC -!- FUNCTION: Cytoskeletal protein involved in actin-membrane 17635CC attachment at sites of cell adhesion to the extracellular matrix 17636CC (focal adhesion). 17637CC -!- SUBUNIT: Binds in vitro to vinculin as well as to the SH3 domain 17638CC of SRC and, when tyrosine phosphorylated, to the SH2 domain of V- 17639CC CRK. Isoform beta binds to PTK2/FAK1 but weakly to vinculin. 17640CC Isoform gamma binds to vinculin but only weakly to PTK2/FAK1. 17641CC Interacts with GIT1, NUDT16L1/SDOS, PARVA and TGFB1I1. Component 17642CC of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and 17643CC PAK1 (By similarity). Interacts with PTK2/FAK1 and PTK2B/PYK2. 17644CC Binds ASAP2. Interacts with unphosphorylated ITGA4. Interacts with 17645CC RNF5 and PDCD10. Interacts with NEK3 and this interaction is 17646CC prolactin-dependent. Interacts with PTK6. 17647CC -!- INTERACTION: 17648CC Q05397:PTK2; NbExp=7; IntAct=EBI-702209, EBI-702142; 17649CC Q09463:rnf-5 (xeno); NbExp=2; IntAct=EBI-702209, EBI-963421; 17650CC Q99942:RNF5; NbExp=6; IntAct=EBI-702209, EBI-348482; 17651CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, 17652CC focal adhesion. Cytoplasm, cell cortex (By similarity). 17653CC Note=Colocalizes with integrins at the cell periphery (By 17654CC similarity). 17655CC -!- ALTERNATIVE PRODUCTS: 17656CC Event=Alternative splicing; Named isoforms=4; 17657CC Name=Beta; 17658CC IsoId=P49023-1; Sequence=Displayed; 17659CC Name=Alpha; 17660CC IsoId=P49023-2; Sequence=VSP_003114; 17661CC Name=Gamma; 17662CC IsoId=P49023-3; Sequence=VSP_003115; 17663CC Name=4; 17664CC IsoId=P49023-4; Sequence=VSP_040483, VSP_003114; 17665CC -!- PTM: Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated 17666CC on tyrosine residues during integrin-mediated cell adhesion, 17667CC embryonic development, fibroblast transformation and following 17668CC stimulation of cells by mitogens. Phosphorylation at Ser-244 by 17669CC CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal 17670CC adhesions (MCFA) during oligodendrocytes (OLs) differentiation. 17671CC Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the 17672CC activation of RAC1 via CRK/CrKII, thereby promoting migration and 17673CC invasion. 17674CC -!- SIMILARITY: Belongs to the paxillin family. 17675CC -!- SIMILARITY: Contains 4 LIM zinc-binding domains. 17676CC ----------------------------------------------------------------------- 17677CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 17678CC Distributed under the Creative Commons Attribution-NoDerivs License 17679CC ----------------------------------------------------------------------- 17680DR EMBL; U14588; AAC50104.1; -; mRNA. 17681DR EMBL; U87946; AAD00648.1; -; Genomic_DNA. 17682DR EMBL; U87941; AAD00648.1; JOINED; Genomic_DNA. 17683DR EMBL; U87942; AAD00648.1; JOINED; Genomic_DNA. 17684DR EMBL; U87943; AAD00648.1; JOINED; Genomic_DNA. 17685DR EMBL; U87944; AAD00648.1; JOINED; Genomic_DNA. 17686DR EMBL; U87945; AAD00648.1; JOINED; Genomic_DNA. 17687DR EMBL; D86862; BAA18997.1; -; mRNA. 17688DR EMBL; D86863; BAA18998.1; -; mRNA. 17689DR EMBL; AK314204; BAG36880.1; -; mRNA. 17690DR EMBL; BX648777; CAI46024.1; -; mRNA. 17691DR EMBL; AC004263; AAC05175.1; -; Genomic_DNA. 17692DR EMBL; BC136787; AAI36788.1; -; mRNA. 17693DR EMBL; BC136794; AAI36795.1; -; mRNA. 17694DR EMBL; BC144410; AAI44411.1; -; mRNA. 17695DR IPI; IPI00220030; -. 17696DR IPI; IPI00220031; -. 17697DR IPI; IPI00335634; -. 17698DR IPI; IPI00890738; -. 17699DR PIR; A55933; A55933. 17700DR RefSeq; NP_001074324.1; NM_001080855.2. 17701DR RefSeq; NP_001230685.1; NM_001243756.1. 17702DR RefSeq; NP_002850.2; NM_002859.3. 17703DR RefSeq; NP_079433.3; NM_025157.4. 17704DR UniGene; Hs.446336; -. 17705DR PDB; 1KKY; Model; -; A=142-157. 17706DR PDB; 1KL0; Model; -; B=142-157. 17707DR PDB; 1OW6; X-ray; 2.35 A; D/F=262-274. 17708DR PDB; 1OW7; X-ray; 2.60 A; D/E/F=262-274. 17709DR PDB; 1OW8; X-ray; 2.85 A; D/F=141-153. 17710DR PDB; 2O9V; X-ray; 1.63 A; B=45-54. 17711DR PDB; 2VZD; X-ray; 2.10 A; C/D=1-20. 17712DR PDB; 2VZG; X-ray; 1.80 A; A=141-160. 17713DR PDB; 2VZI; X-ray; 2.20 A; A=262-315. 17714DR PDB; 3GM1; X-ray; 2.95 A; C/D/E/F=262-274. 17715DR PDB; 3PY7; X-ray; 2.29 A; A=1-10. 17716DR PDB; 3RQE; X-ray; 2.80 A; E=2-15. 17717DR PDB; 3RQF; X-ray; 2.70 A; E=141-153. 17718DR PDB; 3RQG; X-ray; 2.50 A; E=262-274. 17719DR PDBsum; 1KKY; -. 17720DR PDBsum; 1KL0; -. 17721DR PDBsum; 1OW6; -. 17722DR PDBsum; 1OW7; -. 17723DR PDBsum; 1OW8; -. 17724DR PDBsum; 2O9V; -. 17725DR PDBsum; 2VZD; -. 17726DR PDBsum; 2VZG; -. 17727DR PDBsum; 2VZI; -. 17728DR PDBsum; 3GM1; -. 17729DR PDBsum; 3PY7; -. 17730DR PDBsum; 3RQE; -. 17731DR PDBsum; 3RQF; -. 17732DR PDBsum; 3RQG; -. 17733DR ProteinModelPortal; P49023; -. 17734DR SMR; P49023; 357-590. 17735DR DIP; DIP-33851N; -. 17736DR IntAct; P49023; 20. 17737DR MINT; MINT-92615; -. 17738DR STRING; P49023; -. 17739DR DMDM; 27735219; -. 17740DR PRIDE; P49023; -. 17741DR Ensembl; ENST00000228307; ENSP00000228307; ENSG00000089159. 17742DR Ensembl; ENST00000267257; ENSP00000267257; ENSG00000089159. 17743DR Ensembl; ENST00000424649; ENSP00000391283; ENSG00000089159. 17744DR Ensembl; ENST00000458477; ENSP00000395536; ENSG00000089159. 17745DR GeneID; 5829; -. 17746DR KEGG; hsa:5829; -. 17747DR UCSC; uc001txt.3; human. 17748DR UCSC; uc001txv.3; human. 17749DR UCSC; uc001txx.3; human. 17750DR UCSC; uc001txy.3; human. 17751DR CTD; 5829; -. 17752DR GeneCards; GC12M120648; -. 17753DR HGNC; HGNC:9718; PXN. 17754DR HPA; CAB003841; -. 17755DR MIM; 602505; gene. 17756DR neXtProt; NX_P49023; -. 17757DR PharmGKB; PA34062; -. 17758DR eggNOG; NOG267887; -. 17759DR GeneTree; ENSGT00640000091240; -. 17760DR HOVERGEN; HBG001512; -. 17761DR KO; K05760; -. 17762DR Pathway_Interaction_DB; angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling. 17763DR Pathway_Interaction_DB; arf6cyclingpathway; Arf6 signaling events. 17764DR Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling. 17765DR Pathway_Interaction_DB; fcer1pathway; Fc-epsilon receptor I signaling in mast cells. 17766DR Pathway_Interaction_DB; igf1_pathway; IGF1 pathway. 17767DR Pathway_Interaction_DB; avb3_integrin_pathway; Integrins in angiogenesis. 17768DR Pathway_Interaction_DB; lysophospholipid_pathway; LPA receptor mediated events. 17769DR Pathway_Interaction_DB; a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1. 17770DR Pathway_Interaction_DB; a4b1_paxindep_pathway; Paxillin-independent events mediated by a4b1 and a4b7. 17771DR Pathway_Interaction_DB; met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met). 17772DR Pathway_Interaction_DB; vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2. 17773DR Pathway_Interaction_DB; ret_pathway; Signaling events regulated by Ret tyrosine kinase. 17774DR Reactome; REACT_111102; Signal Transduction. 17775DR Reactome; REACT_111155; Cell-Cell communication. 17776DR Reactome; REACT_116125; Disease. 17777DR Reactome; REACT_17044; Muscle contraction. 17778DR EvolutionaryTrace; P49023; -. 17779DR NextBio; 22710; -. 17780DR PMAP-CutDB; P49023; -. 17781DR ArrayExpress; P49023; -. 17782DR Bgee; P49023; -. 17783DR CleanEx; HS_PXN; -. 17784DR Genevestigator; P49023; -. 17785DR GermOnline; ENSG00000089159; Homo sapiens. 17786DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. 17787DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL. 17788DR GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL. 17789DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc. 17790DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB. 17791DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB. 17792DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. 17793DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL. 17794DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. 17795DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL. 17796DR GO; GO:0006936; P:muscle contraction; TAS:Reactome. 17797DR GO; GO:0007172; P:signal complex assembly; TAS:ProtInc. 17798DR Gene3D; G3DSA:2.10.110.10; Znf_LIM; 4. 17799DR InterPro; IPR001904; Paxillin. 17800DR InterPro; IPR001781; Znf_LIM. 17801DR Pfam; PF00412; LIM; 4. 17802DR PRINTS; PR00832; PAXILLIN. 17803DR SMART; SM00132; LIM; 4. 17804DR PROSITE; PS00478; LIM_DOMAIN_1; 4. 17805DR PROSITE; PS50023; LIM_DOMAIN_2; 4. 17806PE 1: Evidence at protein level; 17807KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion; 17808KW Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; LIM domain; 17809KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; 17810KW Repeat; Zinc. 17811FT CHAIN 1 591 Paxillin. 17812FT /FTId=PRO_0000075853. 17813FT DOMAIN 356 415 LIM zinc-binding 1. 17814FT DOMAIN 416 473 LIM zinc-binding 2. 17815FT DOMAIN 474 533 LIM zinc-binding 3. 17816FT DOMAIN 534 591 LIM zinc-binding 4. 17817FT MOTIF 3 15 LD motif 1. 17818FT MOTIF 144 156 LD motif 2. 17819FT MOTIF 216 228 LD motif 3. 17820FT MOTIF 265 276 LD motif 4. 17821FT MOTIF 333 345 LD motif 5. 17822FT COMPBIAS 46 53 Pro-rich. 17823FT MOD_RES 1 1 N-acetylmethionine. 17824FT MOD_RES 31 31 Phosphotyrosine; by PTK6. 17825FT MOD_RES 83 83 Phosphoserine. 17826FT MOD_RES 84 84 Phosphoserine. 17827FT MOD_RES 85 85 Phosphoserine. 17828FT MOD_RES 88 88 Phosphotyrosine. 17829FT MOD_RES 106 106 Phosphoserine. 17830FT MOD_RES 109 109 Phosphoserine (By similarity). 17831FT MOD_RES 118 118 Phosphotyrosine; by PTK6. 17832FT MOD_RES 126 126 Phosphoserine. 17833FT MOD_RES 130 130 Phosphoserine. 17834FT MOD_RES 137 137 Phosphoserine. 17835FT MOD_RES 181 181 Phosphotyrosine. 17836FT MOD_RES 244 244 Phosphoserine; by CDK5. 17837FT MOD_RES 303 303 Phosphoserine. 17838FT MOD_RES 318 318 Phosphothreonine. 17839FT VAR_SEQ 1 133 Missing (in isoform 4). 17840FT /FTId=VSP_040483. 17841FT VAR_SEQ 278 311 Missing (in isoform Alpha and isoform 4). 17842FT /FTId=VSP_003114. 17843FT VAR_SEQ 278 311 IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSW 17844FT PLEEVVLLVSISSSVQEGEKYPHPCAARHRTPSLRSPDQPP 17845FT PCPQ (in isoform Gamma). 17846FT /FTId=VSP_003115. 17847FT VARIANT 73 73 S -> G (in dbSNP:rs4767884). 17848FT /FTId=VAR_065099. 17849FT MUTAGEN 7 8 LL->RR: Loss of interaction with PDCD10. 17850FT CONFLICT 280 280 G -> D (in Ref. 3; BAA18997). 17851FT CONFLICT 327 327 P -> L (in Ref. 5; CAI46024). 17852FT CONFLICT 413 413 F -> S (in Ref. 5; CAI46024). 17853FT HELIX 143 155 17854SQ SEQUENCE 591 AA; 64505 MW; ABF6C0BE5939623F CRC64; 17855 MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG 17856 TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF 17857 PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL 17858 YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG 17859 EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG 17860 RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA 17861 CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC 17862 NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA 17863 RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK 17864 PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C 17865// 17866ID RS24_TAKRU Reviewed; 132 AA. 17867AC O42387; 17868DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. 17869DT 01-JAN-1998, sequence version 1. 17870DT 16-MAY-2012, entry version 54. 17871DE RecName: Full=40S ribosomal protein S24; 17872GN Name=rps24; 17873OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 17874OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 17875OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 17876OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 17877OC Tetradontoidea; Tetraodontidae; Takifugu. 17878OX NCBI_TaxID=31033; 17879RN [1] 17880RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 17881RA Crosio C., Cecconi F., Giorgi M., Amaldi F., Mariottini P.; 17882RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. 17883CC -!- SIMILARITY: Belongs to the ribosomal protein S24e family. 17884CC ----------------------------------------------------------------------- 17885CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 17886CC Distributed under the Creative Commons Attribution-NoDerivs License 17887CC ----------------------------------------------------------------------- 17888DR EMBL; AJ001398; CAA04728.1; -; Genomic_DNA. 17889DR ProteinModelPortal; O42387; -. 17890DR STRING; O42387; -. 17891DR PRIDE; O42387; -. 17892DR eggNOG; COG2004; -. 17893DR InParanoid; O42387; -. 17894DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. 17895DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. 17896DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. 17897DR GO; GO:0006412; P:translation; IEA:InterPro. 17898DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1. 17899DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. 17900DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. 17901DR InterPro; IPR001976; Ribosomal_S24e. 17902DR InterPro; IPR018098; Ribosomal_S24e_CS. 17903DR PANTHER; PTHR10496; Ribosomal_S24E; 1. 17904DR Pfam; PF01282; Ribosomal_S24e; 1. 17905DR ProDom; PD006052; Ribosomal_S24e; 1. 17906DR SUPFAM; SSF54189; L23_L15e_core; 1. 17907DR PROSITE; PS00529; RIBOSOMAL_S24E; 1. 17908PE 3: Inferred from homology; 17909KW Complete proteome; Reference proteome; Ribonucleoprotein; 17910KW Ribosomal protein. 17911FT CHAIN 1 132 40S ribosomal protein S24. 17912FT /FTId=PRO_0000137627. 17913SQ SEQUENCE 132 AA; 15305 MW; DC437F60F20C14F5 CRC64; 17914 MNDTVTVRTR KFMTNRLLQR KQMVVDVLHP GKATVPKTEI REKLAKMYKT TPDVVFVFGF 17915 RTQFGGGKTT GFAMVYDSLD YAKKNEPKHR LARHGLFEKK KTSRKQRKER KNRMKKVRGT 17916 KKASVGASKK KD 17917// 17918ID RS7_TAKRU Reviewed; 194 AA. 17919AC P50894; P53548; 17920DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 17921DT 01-OCT-1996, sequence version 1. 17922DT 16-MAY-2012, entry version 53. 17923DE RecName: Full=40S ribosomal protein S7; 17924GN Name=rps7; 17925OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 17926OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 17927OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 17928OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 17929OC Tetradontoidea; Tetraodontidae; Takifugu. 17930OX NCBI_TaxID=31033; 17931RN [1] 17932RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 17933RX MEDLINE=96371061; PubMed=8774896; DOI=10.1093/nar/24.16.3167; 17934RA Cecconi F., Crosio C., Mariottini P., Cesareni G., Giorgi M., 17935RA Brenner S., Amaldi F.; 17936RT "A functional role for some Fugu introns larger than the typical short 17937RT ones: the example of the gene coding for ribosomal protein S7 and 17938RT snoRNA U17."; 17939RL Nucleic Acids Res. 24:3167-3172(1996). 17940CC -!- SIMILARITY: Belongs to the ribosomal protein S7e family. 17941CC ----------------------------------------------------------------------- 17942CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 17943CC Distributed under the Creative Commons Attribution-NoDerivs License 17944CC ----------------------------------------------------------------------- 17945DR EMBL; X94942; CAA64412.1; -; Genomic_DNA. 17946DR STRING; P50894; -. 17947DR PRIDE; P50894; -. 17948DR Ensembl; ENSTRUT00000040395; ENSTRUP00000040253; ENSTRUG00000015750. 17949DR eggNOG; NOG280542; -. 17950DR GeneTree; ENSGT00390000014122; -. 17951DR InParanoid; P50894; -. 17952DR OMA; KFSDRHV; -. 17953DR OrthoDB; EOG4GQQ61; -. 17954DR GO; GO:0030686; C:90S preribosome; ISS:RefGenome. 17955DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:RefGenome. 17956DR GO; GO:0032040; C:small-subunit processome; ISS:RefGenome. 17957DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. 17958DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:RefGenome. 17959DR GO; GO:0006364; P:rRNA processing; ISS:RefGenome. 17960DR GO; GO:0006412; P:translation; IEA:InterPro. 17961DR InterPro; IPR000554; Ribosomal_S7e. 17962DR PANTHER; PTHR11278; Ribosomal_S7E; 1. 17963DR Pfam; PF01251; Ribosomal_S7e; 1. 17964DR PROSITE; PS00948; RIBOSOMAL_S7E; 1. 17965PE 3: Inferred from homology; 17966KW Complete proteome; Reference proteome; Ribonucleoprotein; 17967KW Ribosomal protein. 17968FT CHAIN 1 194 40S ribosomal protein S7. 17969FT /FTId=PRO_0000174194. 17970FT COMPBIAS 98 120 Arg/Lys-rich (basic). 17971SQ SEQUENCE 194 AA; 22206 MW; D202501948D47E86 CRC64; 17972 MFSTSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGSRKAI 17973 IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRS KNKQKRPRSR 17974 TLTSVHDAIL EDLVFPSEIV GKRIRVKMDS SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL 17975 TGKDVVFEFP EFQL 17976// 17977ID SSRL_TAKRU Reviewed; 289 AA. 17978AC O42179; 17979DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. 17980DT 01-JAN-1998, sequence version 1. 17981DT 16-MAY-2012, entry version 60. 17982DE RecName: Full=Somatostatin-like receptor F_48D10.1; 17983GN ORFNames=F_48D10.1; 17984OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 17985OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 17986OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 17987OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 17988OC Tetradontoidea; Tetraodontidae; Takifugu. 17989OX NCBI_TaxID=31033; 17990RN [1] 17991RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 17992RA Hawkins J., Gillam B.; 17993RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. 17994CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein 17995CC (By similarity). 17996CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 17997CC -!- CAUTION: Seems to lack the C-terminal part (TM6 and TM7). 17998CC ----------------------------------------------------------------------- 17999CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18000CC Distributed under the Creative Commons Attribution-NoDerivs License 18001CC ----------------------------------------------------------------------- 18002DR EMBL; AF013613; AAB86684.1; -; Genomic_DNA. 18003DR ProteinModelPortal; O42179; -. 18004DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. 18005DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 18006DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW. 18007DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. 18008DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. 18009DR Pfam; PF00001; 7tm_1; 1. 18010DR PRINTS; PR00237; GPCRRHODOPSN. 18011DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. 18012DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. 18013PE 3: Inferred from homology; 18014KW Cell membrane; Complete proteome; Disulfide bond; 18015KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; 18016KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. 18017FT CHAIN 1 289 Somatostatin-like receptor F_48D10.1. 18018FT /FTId=PRO_0000070133. 18019FT TOPO_DOM 1 57 Extracellular (Potential). 18020FT TRANSMEM 58 79 Helical; Name=1; (Potential). 18021FT TOPO_DOM 80 89 Cytoplasmic (Potential). 18022FT TRANSMEM 90 110 Helical; Name=2; (Potential). 18023FT TOPO_DOM 111 126 Extracellular (Potential). 18024FT TRANSMEM 127 148 Helical; Name=3; (Potential). 18025FT TOPO_DOM 149 170 Cytoplasmic (Potential). 18026FT TRANSMEM 171 191 Helical; Name=4; (Potential). 18027FT TOPO_DOM 192 240 Extracellular (Potential). 18028FT TRANSMEM 241 261 Helical; Name=5; (Potential). 18029FT TOPO_DOM 262 289 Cytoplasmic (Potential). 18030FT CARBOHYD 40 40 N-linked (GlcNAc...) (Potential). 18031FT DISULFID 125 221 By similarity. 18032SQ SEQUENCE 289 AA; 32172 MW; 4F5A1776911D0ADA CRC64; 18033 MEPLDQTPGF PLSPEPNYWY ETTPSLLLVS YPHLLDISSN QSTQSVPFQG SSALLTAVIY 18034 ITVFVVGLTG NTLAIYVVLR YAGMKTVTNI YILNLAVADE LYIVGLPFLA TQNVLSYWPF 18035 GSFLCRVVMT ADSMNQFTSI FCLTVMSIDR YLAVVHPIRS TKWRHPRVAK VVSAAVWAVS 18036 FVVVLPVVIF SDVQVRPSRP LQVGTSSKCL VKRVQETFNS CNMIWPEPKN VWSTAFILYT 18037 AMVGFFGPLL IICLCYLLIV IKVRHRMSAA QVGAVVSTCP LNICCLSRR 18038// 18039ID SYHC_TAKRU Reviewed; 519 AA. 18040AC P70076; 18041DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 18042DT 01-FEB-1997, sequence version 1. 18043DT 16-MAY-2012, entry version 76. 18044DE RecName: Full=Histidine--tRNA ligase, cytoplasmic; 18045DE EC=6.1.1.21; 18046DE AltName: Full=Histidyl-tRNA synthetase; 18047DE Short=HisRS; 18048GN Name=hars; Synonyms=hiss; 18049OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 18050OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 18051OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 18052OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 18053OC Tetradontoidea; Tetraodontidae; Takifugu. 18054OX NCBI_TaxID=31033; 18055RN [1] 18056RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 18057RC TISSUE=Testis; 18058RX MEDLINE=96323249; PubMed=8710896; DOI=10.1073/pnas.93.16.8485; 18059RA Brenner S., Corrochano L.M.; 18060RT "Translocation events in the evolution of aminoacyl-tRNA 18061RT synthetases."; 18062RL Proc. Natl. Acad. Sci. U.S.A. 93:8485-8489(1996). 18063CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + 18064CC diphosphate + L-histidyl-tRNA(His). 18065CC -!- SUBCELLULAR LOCATION: Cytoplasm. 18066CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase 18067CC family. 18068CC ----------------------------------------------------------------------- 18069CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18070CC Distributed under the Creative Commons Attribution-NoDerivs License 18071CC ----------------------------------------------------------------------- 18072DR EMBL; Z54243; CAA91012.1; -; Genomic_DNA. 18073DR ProteinModelPortal; P70076; -. 18074DR SMR; P70076; 32-66. 18075DR STRING; P70076; -. 18076DR Ensembl; ENSTRUT00000023098; ENSTRUP00000023002; ENSTRUG00000009144. 18077DR eggNOG; COG0124; -. 18078DR GeneTree; ENSGT00390000005922; -. 18079DR OMA; LVSELWD; -. 18080DR BRENDA; 6.1.1.21; 7222. 18081DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 18082DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 18083DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:EC. 18084DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro. 18085DR Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1. 18086DR InterPro; IPR006195; aa-tRNA-synth_II. 18087DR InterPro; IPR004154; Anticodon-bd. 18088DR InterPro; IPR015807; His-tRNA-synth_IIa_subgr. 18089DR InterPro; IPR004516; His-tRNA_synth_IIA. 18090DR PANTHER; PTHR11476; His-tRNA_synth; 1. 18091DR Pfam; PF03129; HGTP_anticodon; 1. 18092DR PIRSF; PIRSF001549; His-tRNA_synth; 1. 18093DR SUPFAM; SSF52954; Anticodon_bd; 1. 18094DR TIGRFAMs; TIGR00442; HisS; 1. 18095DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. 18096PE 3: Inferred from homology; 18097KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; 18098KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 18099FT CHAIN 1 519 Histidine--tRNA ligase, cytoplasmic. 18100FT /FTId=PRO_0000136337. 18101SQ SEQUENCE 519 AA; 57913 MW; A1CBF5752070759E CRC64; 18102 MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV 18103 LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY 18104 DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD 18105 FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC 18106 STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA 18107 CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE 18108 APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR 18109 TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI 18110 LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA 18111// 18112ID SYVC_TAKRU Reviewed; 1217 AA. 18113AC P49696; 18114DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. 18115DT 01-FEB-1996, sequence version 1. 18116DT 16-MAY-2012, entry version 77. 18117DE RecName: Full=Valine--tRNA ligase; 18118DE EC=6.1.1.9; 18119DE AltName: Full=Valyl-tRNA synthetase; 18120DE Short=ValRS; 18121GN Name=vars; Synonyms=vars1; 18122OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 18123OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 18124OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 18125OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 18126OC Tetradontoidea; Tetraodontidae; Takifugu. 18127OX NCBI_TaxID=31033; 18128RN [1] 18129RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 18130RX MEDLINE=97396021; PubMed=9254008; 18131RA Lim E.H., Corrochano L.M., Elgar G., Brenner S.; 18132RT "Genomic structure and sequence analysis of the valyl-tRNA synthetase 18133RT gene of the Japanese pufferfish, Fugu rubripes."; 18134RL DNA Seq. 7:141-151(1997). 18135CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate 18136CC + L-valyl-tRNA(Val). 18137CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase 18138CC family. 18139CC -!- SIMILARITY: Contains 1 GST C-terminal domain. 18140CC ----------------------------------------------------------------------- 18141CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18142CC Distributed under the Creative Commons Attribution-NoDerivs License 18143CC ----------------------------------------------------------------------- 18144DR EMBL; X91856; CAA62967.1; -; Genomic_DNA. 18145DR ProteinModelPortal; P49696; -. 18146DR STRING; P49696; -. 18147DR PRIDE; P49696; -. 18148DR eggNOG; COG0525; -. 18149DR OrthoDB; EOG4QZ7K3; -. 18150DR BRENDA; 6.1.1.9; 7222. 18151DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. 18152DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 18153DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:EC. 18154DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro. 18155DR Gene3D; G3DSA:3.90.740.10; G3DSA:3.90.740.10; 1. 18156DR Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1. 18157DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 3. 18158DR InterPro; IPR001412; aa-tRNA-synth_I_CS. 18159DR InterPro; IPR002300; aa-tRNA-synth_Ia. 18160DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. 18161DR InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C. 18162DR InterPro; IPR004046; GST_C. 18163DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. 18164DR InterPro; IPR010978; tRNA-bd_arm. 18165DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. 18166DR InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd. 18167DR InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd. 18168DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. 18169DR InterPro; IPR002303; Valyl-tRNA_synthetase. 18170DR PANTHER; PTHR11946:SF5; tRNA-synt_val; 1. 18171DR Pfam; PF08264; Anticodon_1; 1. 18172DR Pfam; PF00043; GST_C; 1. 18173DR Pfam; PF00133; tRNA-synt_1; 1. 18174DR Pfam; PF10458; Val_tRNA-synt_C; 1. 18175DR PRINTS; PR00986; TRNASYNTHVAL. 18176DR SUPFAM; SSF47616; GST_C_like; 1. 18177DR SUPFAM; SSF46589; tRNA_binding_arm; 1. 18178DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 1. 18179DR SUPFAM; SSF50677; ValRS_IleRS_edit; 1. 18180DR TIGRFAMs; TIGR00422; ValS; 1. 18181DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. 18182DR PROSITE; PS50405; GST_CTER; 1. 18183PE 3: Inferred from homology; 18184KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; 18185KW Nucleotide-binding; Protein biosynthesis; Reference proteome. 18186FT CHAIN 1 1217 Valine--tRNA ligase. 18187FT /FTId=PRO_0000106256. 18188FT DOMAIN 27 155 GST C-terminal. 18189FT MOTIF 293 303 "HIGH" region. 18190FT MOTIF 809 813 "KMSKS" region. 18191FT BINDING 812 812 ATP (By similarity). 18192SQ SEQUENCE 1217 AA; 138218 MW; 5E08AF24B5C8A7A1 CRC64; 18193 MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT 18194 GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR 18195 NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT 18196 EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD 18197 VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH 18198 LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK 18199 FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS 18200 KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV 18201 ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT 18202 PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI 18203 KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM 18204 DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV 18205 SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM 18206 VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN 18207 LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL 18208 WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA 18209 IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT 18210 EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL 18211 TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV 18212 NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ 18213 TELEKVKEAM DNFQKMM 18214// 18215ID TCPD_TAKRU Reviewed; 536 AA. 18216AC P53451; 18217DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. 18218DT 01-OCT-1996, sequence version 1. 18219DT 16-MAY-2012, entry version 76. 18220DE RecName: Full=T-complex protein 1 subunit delta; 18221DE Short=TCP-1-delta; 18222DE AltName: Full=CCT-delta; 18223GN Name=cct4; Synonyms=cctd; 18224OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). 18225OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 18226OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; 18227OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; 18228OC Tetradontoidea; Tetraodontidae; Takifugu. 18229OX NCBI_TaxID=31033; 18230RN [1] 18231RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. 18232RC TISSUE=Testis; 18233RX MEDLINE=96125198; PubMed=8543170; DOI=10.1016/0378-1119(95)00604-4; 18234RA Yoda T., Morita T., Kawatsu K., Sueki K., Shibata T., Hamano Y.; 18235RT "Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu 18236RT rubripes rubripes."; 18237RL Gene 166:249-253(1995). 18238CC -!- FUNCTION: Molecular chaperone; assists the folding of proteins 18239CC upon ATP hydrolysis. As part of the BBS/CCT complex may play a 18240CC role in the assembly of BBSome, a complex involved in ciliogenesis 18241CC regulating transports vesicles to the cilia. Known to play a role, 18242CC in vitro, in the folding of actin and tubulin (By similarity). 18243CC -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that 18244CC forms two stacked rings, 12 to 16 nm in diameter. Component of the 18245CC BBS/CCT complex (By similarity). 18246CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). 18247CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. 18248CC ----------------------------------------------------------------------- 18249CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18250CC Distributed under the Creative Commons Attribution-NoDerivs License 18251CC ----------------------------------------------------------------------- 18252DR EMBL; D49483; BAA08447.1; -; mRNA. 18253DR EMBL; D49484; BAA18913.1; -; Genomic_DNA. 18254DR PIR; JC4521; JC4521. 18255DR RefSeq; NP_001027851.1; NM_001032679.1. 18256DR UniGene; Tru.1843; -. 18257DR ProteinModelPortal; P53451; -. 18258DR STRING; P53451; -. 18259DR Ensembl; ENSTRUT00000004220; ENSTRUP00000004197; ENSTRUG00000001819. 18260DR GeneID; 446052; -. 18261DR CTD; 10575; -. 18262DR eggNOG; COG0459; -. 18263DR GeneTree; ENSGT00550000074956; -. 18264DR InParanoid; P53451; -. 18265DR OMA; CNVLLVQ; -. 18266DR OrthoDB; EOG4RJG1B; -. 18267DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 18268DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 18269DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. 18270DR GO; GO:0006457; P:protein folding; IEA:InterPro. 18271DR InterPro; IPR012717; Chap_CCT_delta. 18272DR InterPro; IPR017998; Chaperone_TCP-1. 18273DR InterPro; IPR002194; Chaperonin_TCP-1_CS. 18274DR InterPro; IPR002423; Cpn60/TCP-1. 18275DR PANTHER; PTHR11353:SF26; Chap_CCT_delta; 1. 18276DR PANTHER; PTHR11353; Cpn60/TCP-1; 1. 18277DR Pfam; PF00118; Cpn60_TCP1; 1. 18278DR PRINTS; PR00304; TCOMPLEXTCP1. 18279DR SUPFAM; SSF48592; GroEL-ATPase; 1. 18280DR TIGRFAMs; TIGR02342; Chap_CCT_delta; 1. 18281DR PROSITE; PS00750; TCP1_1; 1. 18282DR PROSITE; PS00751; TCP1_2; 1. 18283DR PROSITE; PS00995; TCP1_3; 1. 18284PE 2: Evidence at transcript level; 18285KW ATP-binding; Chaperone; Complete proteome; Cytoplasm; 18286KW Nucleotide-binding; Reference proteome. 18287FT CHAIN 1 536 T-complex protein 1 subunit delta. 18288FT /FTId=PRO_0000128336. 18289SQ SEQUENCE 536 AA; 57716 MW; B3ED3285FAC18D07 CRC64; 18290 MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD 18291 EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL 18292 LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL 18293 APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK 18294 AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS 18295 ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE 18296 EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA 18297 GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR 18298 HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR 18299// 18300ID THGA_ECOLI Reviewed; 203 AA. 18301AC P07464; P77862; Q2MC82; 18302DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. 18303DT 01-APR-1988, sequence version 1. 18304DT 16-MAY-2012, entry version 112. 18305DE RecName: Full=Galactoside O-acetyltransferase; 18306DE Short=GAT; 18307DE EC=2.3.1.18; 18308DE AltName: Full=Thiogalactoside acetyltransferase; 18309GN Name=lacA; OrderedLocusNames=b0342, JW0333; 18310OS Escherichia coli (strain K12). 18311OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; 18312OC Enterobacteriaceae; Escherichia. 18313OX NCBI_TaxID=83333; 18314RN [1] 18315RP PROTEIN SEQUENCE. 18316RX MEDLINE=85200082; PubMed=3922433; DOI=10.1016/S0300-9084(85)80235-2; 18317RA Fowler A.V., Hediger M.A., Musso R.E., Zabin I.; 18318RT "The amino acid sequence of thiogalactoside transacetylase of 18319RT Escherichia coli."; 18320RL Biochimie 67:101-108(1985). 18321RN [2] 18322RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 18323RX MEDLINE=86016712; PubMed=3901000; DOI=10.1073/pnas.82.19.6414; 18324RA Hediger M.A., Johnson D.F., Nierlich D.P., Zabin I.; 18325RT "DNA sequence of the lactose operon: the lacA gene and the 18326RT transcriptional termination region."; 18327RL Proc. Natl. Acad. Sci. U.S.A. 82:6414-6418(1985). 18328RN [3] 18329RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 18330RC STRAIN=K12 / MG1655 / ATCC 47076; 18331RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., 18332RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., 18333RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; 18334RT "Sequence of minutes 4-25 of Escherichia coli."; 18335RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 18336RN [4] 18337RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 18338RC STRAIN=K12 / MG1655 / ATCC 47076; 18339RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; 18340RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., 18341RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., 18342RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., 18343RA Mau B., Shao Y.; 18344RT "The complete genome sequence of Escherichia coli K-12."; 18345RL Science 277:1453-1474(1997). 18346RN [5] 18347RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 18348RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; 18349RX PubMed=16738553; DOI=10.1038/msb4100049; 18350RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., 18351RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; 18352RT "Highly accurate genome sequences of Escherichia coli K-12 strains 18353RT MG1655 and W3110."; 18354RL Mol. Syst. Biol. 2:E1-E5(2006). 18355RN [6] 18356RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. 18357RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; 18358RA Buechel D.E., Gronenborn B., Mueller-Hill B.; 18359RT "Sequence of the lactose permease gene."; 18360RL Nature 283:541-545(1980). 18361RN [7] 18362RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). 18363RX MEDLINE=21936195; PubMed=11937062; DOI=10.1016/S0969-2126(02)00741-4; 18364RA Wang X.G., Olsen L.R., Roderick S.L.; 18365RT "Structure of the lac operon galactoside acetyltransferase."; 18366RL Structure 10:581-588(2002). 18367CC -!- FUNCTION: May assist cellular detoxification by acetylating non- 18368CC metabolizable pyranosides, thereby preventing their reentry into 18369CC the cell. 18370CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + a beta-D-galactoside = CoA + a 6- 18371CC acetyl-beta-D-galactoside. 18372CC -!- SUBUNIT: Homodimer. 18373CC -!- SUBCELLULAR LOCATION: Cytoplasm. 18374CC -!- PTM: The N-terminus of this protein is heterogeneous because the 18375CC initiator methionine is only partially cleaved. 18376CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. 18377CC ----------------------------------------------------------------------- 18378CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18379CC Distributed under the Creative Commons Attribution-NoDerivs License 18380CC ----------------------------------------------------------------------- 18381DR EMBL; J01636; AAA24055.1; -; Genomic_DNA. 18382DR EMBL; X51872; CAA36162.1; -; Genomic_DNA. 18383DR EMBL; U73857; AAB18066.1; -; Genomic_DNA. 18384DR EMBL; U00096; AAC73445.1; -; Genomic_DNA. 18385DR EMBL; AP009048; BAE76124.1; -; Genomic_DNA. 18386DR EMBL; V00295; CAA23572.1; -; Genomic_DNA. 18387DR PIR; A94061; XXECTG. 18388DR RefSeq; NP_414876.1; NC_000913.2. 18389DR PDB; 1KQA; X-ray; 3.20 A; A/B/C=1-203. 18390DR PDB; 1KRR; X-ray; 2.50 A; A/B/C=1-203. 18391DR PDB; 1KRU; X-ray; 2.80 A; A/B/C=1-203. 18392DR PDB; 1KRV; X-ray; 2.80 A; A/B/C=1-203. 18393DR PDBsum; 1KQA; -. 18394DR PDBsum; 1KRR; -. 18395DR PDBsum; 1KRU; -. 18396DR PDBsum; 1KRV; -. 18397DR ProteinModelPortal; P07464; -. 18398DR SMR; P07464; 2-202. 18399DR DIP; DIP-10078N; -. 18400DR IntAct; P07464; 4. 18401DR EnsemblBacteria; EBESCT00000004023; EBESCP00000004023; EBESCG00000003288. 18402DR EnsemblBacteria; EBESCT00000004024; EBESCP00000004024; EBESCG00000003288. 18403DR EnsemblBacteria; EBESCT00000004025; EBESCP00000004025; EBESCG00000003288. 18404DR EnsemblBacteria; EBESCT00000004026; EBESCP00000004026; EBESCG00000003288. 18405DR EnsemblBacteria; EBESCT00000017191; EBESCP00000016482; EBESCG00000016250. 18406DR GeneID; 945674; -. 18407DR GenomeReviews; AP009048_GR; JW0333. 18408DR GenomeReviews; U00096_GR; b0342. 18409DR KEGG; eco:b0342; -. 18410DR PATRIC; 32115817; VBIEscCol129921_0350. 18411DR EchoBASE; EB0519; -. 18412DR EcoGene; EG10524; lacA. 18413DR eggNOG; COG0110; -. 18414DR HOGENOM; HOG000049435; -. 18415DR KO; K00633; -. 18416DR OMA; PMTERIK; -. 18417DR ProtClustDB; PRK09527; -. 18418DR BioCyc; EcoCyc:GALACTOACETYLTRAN-MONOMER; -. 18419DR BioCyc; MetaCyc:GALACTOACETYLTRAN-MONOMER; -. 18420DR EvolutionaryTrace; P07464; -. 18421DR Genevestigator; P07464; -. 18422DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 18423DR GO; GO:0008870; F:galactoside O-acetyltransferase activity; IEA:EC. 18424DR GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW. 18425DR InterPro; IPR001451; Hexapep_transf. 18426DR InterPro; IPR018357; Hexapep_transf_CS. 18427DR InterPro; IPR024688; Maltose/galactoside_AcTrfase. 18428DR InterPro; IPR011004; Trimer_LpxA-like. 18429DR Pfam; PF00132; Hexapep; 1. 18430DR Pfam; PF12464; Mac; 1. 18431DR SUPFAM; SSF51161; Trimer_LpxA_like; 1. 18432DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. 18433PE 1: Evidence at protein level; 18434KW 3D-structure; Acyltransferase; Complete proteome; Cytoplasm; 18435KW Direct protein sequencing; Lactose biosynthesis; Reference proteome; 18436KW Repeat; Transferase. 18437FT CHAIN 1 203 Galactoside O-acetyltransferase. 18438FT /FTId=PRO_0000068696. 18439FT HELIX 5 11 18440FT HELIX 22 37 18441FT HELIX 44 54 18442FT STRAND 55 57 18443FT STRAND 68 71 18444FT STRAND 76 78 18445FT STRAND 88 91 18446FT STRAND 96 98 18447FT STRAND 109 114 18448FT TURN 119 121 18449FT STRAND 127 129 18450FT STRAND 132 134 18451FT STRAND 172 175 18452FT TURN 176 179 18453FT STRAND 180 184 18454FT HELIX 187 189 18455SQ SEQUENCE 203 AA; 22799 MW; 31C7FEA0B0150D70 CRC64; 18456 MNMPMTERIR AGKLFTDMCE GLPEKRLRGK TLMYEFNHSH PSEVEKRESL IKEMFATVGE 18457 NAWVEPPVYF SYGSNIHIGR NFYANFNLTI VDDYTVTIGD NVLIAPNVTL SVTGHPVHHE 18458 LRKNGEMYSF PITIGNNVWI GSHVVINPGV TIGDNSVIGA GSIVTKDIPP NVVAAGVPCR 18459 VIREINDRDK HYYFKDYKVE SSV 18460// 18461ID UBR5_RAT Reviewed; 2788 AA. 18462AC Q62671; F1LRS0; 18463DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. 18464DT 22-FEB-2012, sequence version 3. 18465DT 16-MAY-2012, entry version 90. 18466DE RecName: Full=E3 ubiquitin-protein ligase UBR5; 18467DE EC=6.3.2.-; 18468DE AltName: Full=100 kDa protein; 18469DE AltName: Full=E3 ubiquitin-protein ligase, HECT domain-containing 1; 18470DE AltName: Full=Hyperplastic discs protein homolog; 18471GN Name=Ubr5; Synonyms=Dd5, Edd, Edd1, Hyd; 18472OS Rattus norvegicus (Rat). 18473OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 18474OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; 18475OC Muroidea; Muridae; Murinae; Rattus. 18476OX NCBI_TaxID=10116; 18477RN [1] 18478RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 18479RC STRAIN=Brown Norway; 18480RX PubMed=15057822; DOI=10.1038/nature02426; 18481RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., 18482RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., 18483RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., 18484RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., 18485RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., 18486RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., 18487RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., 18488RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., 18489RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., 18490RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., 18491RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., 18492RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., 18493RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., 18494RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., 18495RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., 18496RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., 18497RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., 18498RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., 18499RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., 18500RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., 18501RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., 18502RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., 18503RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., 18504RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., 18505RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., 18506RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., 18507RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., 18508RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., 18509RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., 18510RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., 18511RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., 18512RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., 18513RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., 18514RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., 18515RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., 18516RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., 18517RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., 18518RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., 18519RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., 18520RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., 18521RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., 18522RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., 18523RA Collins F.S.; 18524RT "Genome sequence of the Brown Norway rat yields insights into 18525RT mammalian evolution."; 18526RL Nature 428:493-521(2004). 18527RN [2] 18528RP NUCLEOTIDE SEQUENCE [MRNA] OF 1868-2788. 18529RC STRAIN=Wistar; TISSUE=Testis; 18530RX MEDLINE=92253337; PubMed=1533713; DOI=10.1093/nar/20.7.1471; 18531RA Mueller D., Rehbein M., Baumeister H., Richter D.; 18532RT "Molecular characterization of a novel rat protein structurally 18533RT related to poly(A) binding proteins and the 70K protein of the U1 18534RT small nuclear ribonucleoprotein particle (snRNP)."; 18535RL Nucleic Acids Res. 20:1471-1475(1992). 18536RN [3] 18537RP ERRATUM. 18538RA Mueller D., Rehbein M., Baumeister H., Richter D.; 18539RL Nucleic Acids Res. 20:2624-2624(1992). 18540RN [4] 18541RP IDENTIFICATION OF PROBABLE FRAMESHIFT. 18542RX MEDLINE=99153743; PubMed=10030672; DOI=10.1038/sj.onc.1202249; 18543RA Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R., 18544RA Sutherland R.L., Watts C.K.W.; 18545RT "Identification of a human HECT family protein with homology to the 18546RT Drosophila tumor suppressor gene hyperplastic discs."; 18547RL Oncogene 17:3479-3491(1998). 18548RN [5] 18549RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. 18550RX PubMed=12239083; DOI=10.1210/en.2002-220262; 18551RA Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J., 18552RA Rajapurohitam V., Wing S.S.; 18553RT "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase 18554RT induced in germ cells of the rat testis and similar to the Drosophila 18555RT hyperplastic discs gene."; 18556RL Endocrinology 143:3740-3747(2002). 18557CC -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the 18558CC N-end rule pathway. Recognizes and binds to proteins bearing 18559CC specific N-terminal residues that are destabilizing according to 18560CC the N-end rule, leading to their ubiquitination and subsequent 18561CC degradation (By similarity). Involved in maturation and/or 18562CC transcriptional regulation of mRNA by activating CDK9 by 18563CC polyubiquitination. May play a role in control of cell cycle 18564CC progression. May have tumor suppressor function. Regulates DNA 18565CC topoisomerase II binding protein (TopBP1) for the DNA damage 18566CC response. Plays an essential role in extraembryonic development 18567CC (By similarity). 18568CC -!- PATHWAY: Protein modification; protein ubiquitination. 18569CC -!- SUBUNIT: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and 18570CC forms a transcription regulatory complex made of CDK9, RNAP II, 18571CC UBR5 and TFIIS/TCEA1 that can stimulates target gene transcription 18572CC by recruiting their promoters (By similarity). 18573CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). 18574CC -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present 18575CC in liver, kidney, lung and brain. 18576CC -!- DEVELOPMENTAL STAGE: In early postnatal life, expression in the 18577CC testis increases to reach a maximum around day 28. 18578CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By 18579CC similarity). 18580CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin- 18581CC thioester formation. 18582CC -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein 18583CC ligase) domain. 18584CC -!- SIMILARITY: Contains 1 PABC domain. 18585CC -!- SIMILARITY: Contains 1 UBR-type zinc finger. 18586CC -!- SEQUENCE CAUTION: 18587CC Sequence=CAA45756.1; Type=Frameshift; Positions=30; 18588CC ----------------------------------------------------------------------- 18589CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms 18590CC Distributed under the Creative Commons Attribution-NoDerivs License 18591CC ----------------------------------------------------------------------- 18592DR EMBL; X64411; CAA45756.1; ALT_FRAME; mRNA. 18593DR IPI; IPI00768617; -. 18594DR PIR; S22659; S22659. 18595DR UniGene; Rn.54812; -. 18596DR PDB; 3NTW; X-ray; 2.60 A; A/C=2383-2442. 18597DR PDBsum; 3NTW; -. 18598DR STRING; Q62671; -. 18599DR PhosphoSite; Q62671; -. 18600DR PRIDE; Q62671; -. 18601DR UCSC; X64411; rat. 18602DR RGD; 621236; Ubr5. 18603DR eggNOG; COG5021; -. 18604DR HOGENOM; HOG000046848; -. 18605DR InParanoid; Q62671; -. 18606DR OrthoDB; EOG4QVCB2; -. 18607DR ArrayExpress; Q62671; -. 18608DR Genevestigator; Q62671; -. 18609DR GermOnline; ENSRNOG00000006816; Rattus norvegicus. 18610DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 18611DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 18612DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro. 18613DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. 18614DR GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome. 18615DR Gene3D; G3DSA:1.10.1900.10; PABP_HYD; 1. 18616DR Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 3. 18617DR InterPro; IPR024725; E3_UbLigase_EDD_UBA. 18618DR InterPro; IPR000569; HECT. 18619DR InterPro; IPR002004; PABP_HYD. 18620DR InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh. 18621DR InterPro; IPR003126; Znf_N-recognin. 18622DR InterPro; IPR013993; Znf_N-recognin_met. 18623DR Pfam; PF11547; E3_UbLigase_EDD; 1. 18624DR Pfam; PF00632; HECT; 1. 18625DR Pfam; PF00658; PABP; 1. 18626DR Pfam; PF02207; zf-UBR; 1. 18627DR SMART; SM00119; HECTc; 1. 18628DR SMART; SM00517; PolyA; 1. 18629DR SMART; SM00396; ZnF_UBR1; 1. 18630DR SUPFAM; SSF56204; HECT; 1. 18631DR SUPFAM; SSF63570; PABP_HYD; 1. 18632DR SUPFAM; SSF50985; RCC1/BLIP-II; 1. 18633DR PROSITE; PS50237; HECT; 1. 18634DR PROSITE; PS51309; PABC; 1. 18635DR PROSITE; PS51157; ZF_UBR; 1. 18636PE 1: Evidence at protein level; 18637KW 3D-structure; Complete proteome; Ligase; Metal-binding; Nucleus; 18638KW Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; 18639KW Zinc-finger. 18640FT CHAIN 1 2788 E3 ubiquitin-protein ligase UBR5. 18641FT /FTId=PRO_0000086933. 18642FT DOMAIN 2367 2444 PABC. 18643FT DOMAIN 2451 2788 HECT. 18644FT ZN_FING 1166 1234 UBR-type. 18645FT COMPBIAS 1613 1670 Ser-rich. 18646FT COMPBIAS 2319 2366 Arg-rich. 18647FT ACT_SITE 2757 2757 Glycyl thioester intermediate (By 18648FT similarity). 18649FT MOD_RES 100 100 Phosphoserine (By similarity). 18650FT MOD_RES 342 342 Phosphoserine (By similarity). 18651FT MOD_RES 567 567 Phosphoserine (By similarity). 18652FT MOD_RES 601 601 Phosphoserine (By similarity). 18653FT MOD_RES 626 626 Phosphothreonine (By similarity). 18654FT MOD_RES 797 797 Phosphoserine (By similarity). 18655FT MOD_RES 917 917 Phosphoserine (By similarity). 18656FT MOD_RES 1007 1007 Phosphoserine (By similarity). 18657FT MOD_RES 1104 1104 Phosphothreonine (By similarity). 18658FT MOD_RES 1124 1124 Phosphothreonine (By similarity). 18659FT MOD_RES 1216 1216 Phosphoserine (By similarity). 18660FT MOD_RES 1344 1344 Phosphoserine (By similarity). 18661FT MOD_RES 1364 1364 Phosphoserine (By similarity). 18662FT MOD_RES 1470 1470 Phosphoserine (By similarity). 18663FT MOD_RES 1725 1725 Phosphothreonine (By similarity). 18664FT MOD_RES 1730 1730 Phosphoserine (By similarity). 18665FT MOD_RES 1769 1769 Phosphoserine (By similarity). 18666FT MOD_RES 1959 1959 Phosphothreonine (By similarity). 18667FT MOD_RES 2016 2016 Phosphoserine (By similarity). 18668FT MOD_RES 2018 2018 Phosphoserine (By similarity). 18669FT MOD_RES 2020 2020 Phosphothreonine (By similarity). 18670FT MOD_RES 2061 2061 Phosphoserine (By similarity). 18671FT MOD_RES 2066 2066 Phosphoserine (By similarity). 18672FT MOD_RES 2203 2203 Phosphothreonine (By similarity). 18673FT MOD_RES 2279 2279 Phosphoserine (By similarity). 18674FT MOD_RES 2473 2473 Phosphoserine (By similarity). 18675FT MOD_RES 2475 2475 Phosphoserine (By similarity). 18676FT CONFLICT 1890 1890 Missing (in Ref. 2; CAA45756). 18677FT HELIX 2383 2386 18678FT HELIX 2392 2396 18679FT HELIX 2400 2402 18680FT HELIX 2403 2406 18681FT HELIX 2410 2412 18682FT HELIX 2415 2423 18683FT HELIX 2425 2439 18684SQ SEQUENCE 2788 AA; 308027 MW; C2EA68B962627231 CRC64; 18685 MNKQAVKRLH MLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF LLEDGRICRI 18686 GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL GRLAGNTLGS 18687 RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI 18688 SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS 18689 LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE 18690 RESVLRLRER RWLDGASFDN ERGSTSKEGE PNPDKKNTPV QSPVSLGEDL QWWPDKDGTK 18691 FTCIGALYSE LVAVSSKGEL YQWKWTESEP YRNAQNPSLH HPRATFLGLT NEKIVLLSAN 18692 SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENN 18693 LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GVQSLNVRGG RQVCLRNNPL YHAGAVAFSI 18694 SAGIPKVGVL MESVWNMNDS CRFQLRSPES LKSMEKASKT IETKPESKQE PVKTEMGPPP 18695 SPASTCSDAS SIASSASMPY KRRRSTPAPK EEEKVNEEQW SLREVVFVED VKNVPVGKVL 18696 KVDGAYVAVK FPGTSSNTNC QNSSGPDADP SSLLQDCRLL RIDELQVVKT GGTPKVPDCF 18697 QRTPKKLCIP EKTEILAVNV DSKGVHAVLK TGNWVRYCIF DLATGKAEQE NNFPTSSVAF 18698 LGQNERSVAI FTAGQESPII LRDGNGTIYP MAKDCMGGIR DPDWLDLPPI SSLGMGVHSL 18699 INLPANSTIK KKAAIIIMAV EKQTLMQHIL RCDYEACRQY LVNLEQAVVL EQNLQMLQTF 18700 ISHRCDGNRN ILHACVSVCF PTSNKETKEE EEAERSERNT FAERLSAVEA IANAISVVSS 18701 NGPGNRAGSS SSRSLRLREM MRRSLRAAGL GRHEAGASSS DHQDPVSPPI APPSWVPDPP 18702 SMDPDGDIDF ILAPAVGSLT TAATGGGQGP STSTIPGPST EPSVVESKDR KANAHFILKL 18703 LCDSAVLQPY LRELLSAKDA RGMTPFMSAV SGRAYPAAIT ILETAQKIAK AEVSGSEKEE 18704 DVFMGMVCPS GTNPDDSPLY VLCCNDTCSF TWTGAEHINQ DIFECRTCGL LESLCCCTEC 18705 ARVCHKGHDC KLKRTSPTAY CDCWEKCKCK TLIAGQKSAR LDLLYRLLTA TNLVTLPNSR 18706 GEHLLLFLVQ TVARQTVEHC QYRPPRIRED RNRKTASPDD SDMPDHDLEP PRFAQLALER 18707 VLQDWNALRS MIMFGSQENK DPLSASSRIG HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC 18708 TADILLLDTL LGTLVKELQN KYTPGRREEA IAVTMRFLRS VARVFVILSV EMASSKKKNN 18709 FIPQPIGKCK RVFQALLPYA VEELCNVAES LIVPVRMGIA RPTAPFTLAS TSIDAMQGSE 18710 ELFSVEPLPP RPSSDQSSSS SQSQSSYIIR NPQQRRISQS QPVRGREEEQ DDIVSADVEE 18711 VEVVEGVAGE EDHHDEQEEH GEENAEAEGH HDEHDEDGSD MELDLLAAAE TESDSESNHS 18712 NQDNASGRRS VVTAATAGSE AGASSVPAFF SEDDSQSNDS SDSDSSSSQS DDIEQETFML 18713 DEPLERTTNS SHANGAAQAP RSMQWAVRNT QHQRAASTAP SSTSTPAASS AGLIYIDPSN 18714 LRRSGTISTS AAAAAAALEA SNASSYLTSA SSLARAYSIV IRQISDLMGL IPKYNHLVYS 18715 QIPAAVKLTY QDAVNLQNYV EEKLIPTWNW MVSIMDSTEA QLRYGSALAS AGDPGHPNHP 18716 LHASQNSARR ERMTAREEAS LRTLEGRRRR ATLLSARQGM MSARGDFLNY ALSLMRSHND 18717 EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS 18718 EHENDDDTSQ SATLNDKDDE SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL 18719 ADQPHLLQPN ARKEDLFGRP SQGLYSSSAG SGKCLVEVTM DRNCLEVLPT KMSYAANLKN 18720 VMNMQNRQKK AGEDQSMLAE EADSSKPGPS AHDVAAQLKS SLLAEIGLTE SEGPPLTSFR 18721 PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV KESKFRREME 18722 KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG 18723 VARSFYTAIA QAFLSNEKLP NLDCIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS 18724 GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER LYPRVQAMQP 18725 AFASKITGML LELSPAQLLL LLASEDSLRA RVEEAMELIV AHGRENGADS ILDLGLLDSS 18726 EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR GFYTPRPGKN TEARLNCFRN 18727 IGRILGLCLL QNELCPITLN RHVIKVLLGR KVNWHDFAFF DPVMYESLRQ LILASQSSDA 18728 DAVFSAMDLA FAVDLCKEEG GGQVELIPNG VNIPVTPQNV YEYVRKYAEH RMLVVAEQPL 18729 HAMRKGLLDV LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG ENAEKLLQFK 18730 RWFWSIVERM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH LPTANTCISR 18731 LYVPLYSSKQ ILKQKLLLAI KTKNFGFV 18732// 18733