ID DOK1_HUMAN Reviewed; 481 AA. AC Q99704; O43204; Q53TY2; Q9UHG6; DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 29-SEP-2021, entry version 190. DE RecName: Full=Docking protein 1; DE AltName: Full=Downstream of tyrosine kinase 1; DE AltName: Full=p62(dok); DE AltName: Full=pp62; GN Name=DOK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION AT TYROSINE RP RESIDUES. RX PubMed=9008160; DOI=10.1016/s0092-8674(00)81840-1; RA Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R., RA Stillman B., Clarkson B.; RT "p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein RT in chronic myelogenous leukemia progenitor cells."; RL Cell 88:197-204(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10940083; DOI=10.1046/j.1365-2370.2000.00203.x; RA Hubert P., Ferreira V., Debre P., Bismuth G.; RT "Molecular cloning of a truncated p62Dok1 isoform, p22Dokdel."; RL Eur. J. Immunogenet. 27:145-148(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Yu W., Sarginson J., Gibbs R.A.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION AT TYR-362 AND TYR-398, AND MUTAGENESIS OF TYR-362 AND RP TYR-398. RX PubMed=11551902; DOI=10.1074/jbc.m102116200; RA Wick M.J., Dong L.Q., Hu D., Langlais P., Liu F.; RT "Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 RT and 398 plays distinct roles for binding GTPase-activating protein and Nck RT and is essential for inhibiting insulin-stimulated activation of Ras and RT Akt."; RL J. Biol. Chem. 276:42843-42850(2001). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12595900; DOI=10.1038/sj.gene.6363891; RA Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.; RT "DOK4 and DOK5: new Dok-related genes expressed in human T cells."; RL Genes Immun. 4:40-45(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-362; TYR-377; TYR-398 AND RP TYR-409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 3), AND ACETYLATION RP AT MET-1 (ISOFORM 3). RX PubMed=19481542; DOI=10.1016/j.febslet.2009.05.042; RA Kobayashi R., Patenia R., Ashizawa S., Vykoukal J.; RT "Targeted mass spectrometric analysis of N-terminally truncated isoforms RT generated via alternative translation initiation."; RL FEBS Lett. 583:2441-2445(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; TYR-341 AND TYR-362, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRMS. RX PubMed=23822091; DOI=10.1111/febs.12420; RA Goel R.K., Miah S., Black K., Kalra N., Dai C., Lukong K.E.; RT "The unique N-terminal region of SRMS regulates enzymatic activity and RT phosphorylation of its novel substrate Dok1."; RL FEBS J. 280:4539-4559(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-269 AND SER-460, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 152-256, FUNCTION, AND INTERACTION RP WITH ITGB3. RX PubMed=18156175; DOI=10.1074/jbc.m709435200; RA Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D., RA Wegener K.L.; RT "An integrin phosphorylation switch: the effect of beta3 integrin tail RT phosphorylation on Dok1 and talin binding."; RL J. Biol. Chem. 283:5420-5426(2008). CC -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding CC proteins. They provide a docking platform for the assembly of CC multimolecular signaling complexes. DOK1 appears to be a negative CC regulator of the insulin signaling pathway. Modulates integrin CC activation by competing with talin for the same binding site on ITGB3. CC {ECO:0000269|PubMed:18156175}. CC -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with RasGAP and CC INPP5D/SHIP1. Interacts directly with phosphorylated ITGB3. Interacts CC with SRMS (via the SH2 and SH3 domains). {ECO:0000250, CC ECO:0000269|PubMed:18156175, ECO:0000269|PubMed:23822091}. CC -!- INTERACTION: CC Q99704; P04626: ERBB2; NbExp=2; IntAct=EBI-1384360, EBI-641062; CC Q99704; Q9H3Y6: SRMS; NbExp=7; IntAct=EBI-1384360, EBI-8541270; CC Q99704; Q9JIY2: Cbll1; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-7644904; CC Q99704; Q9Q2G4: ORF; Xeno; NbExp=2; IntAct=EBI-1384360, EBI-6248094; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, perinuclear region. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=1; Synonyms=p62Dok1; CC IsoId=Q99704-1; Sequence=Displayed; CC Name=2; Synonyms=p22Dokdel; CC IsoId=Q99704-2; Sequence=VSP_003852, VSP_003853; CC Name=3; Synonyms=p44Dok; CC IsoId=Q99704-3; Sequence=VSP_038224; CC -!- TISSUE SPECIFICITY: Expressed in pancreas, heart, leukocyte and spleen. CC Expressed in both resting and activated peripheral blood T-cells. CC Expressed in breast cancer. {ECO:0000269|PubMed:12595900}. CC -!- DOMAIN: The PTB domain mediates receptor interaction. CC -!- PTM: Constitutively tyrosine-phosphorylated. Phosphorylated by TEC (By CC similarity). Phosphorylated by LYN (By similarity). Phosphorylated on CC tyrosine residues by the insulin receptor kinase. Results in the CC negative regulation of the insulin signaling pathway. Phosphorylated on CC tyrosine residues by SRMS. {ECO:0000250, ECO:0000269|PubMed:11551902, CC ECO:0000269|PubMed:23822091, ECO:0000269|PubMed:9008160}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met- CC 140 of isoform 1. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U70987; AAC51127.1; -; mRNA. DR EMBL; AF180527; AAF19167.1; -; mRNA. DR EMBL; AF035299; AAB88182.1; -; mRNA. DR EMBL; AC005033; AAX93224.1; -; Genomic_DNA. DR EMBL; BC114440; AAI14441.1; -; mRNA. DR CCDS; CCDS1954.1; -. [Q99704-1] DR CCDS; CCDS56125.1; -. [Q99704-3] DR CCDS; CCDS82474.1; -. [Q99704-2] DR RefSeq; NP_001184189.1; NM_001197260.1. [Q99704-3] DR RefSeq; NP_001305797.1; NM_001318868.1. [Q99704-2] DR RefSeq; NP_001372.1; NM_001381.4. [Q99704-1] DR PDB; 2V76; X-ray; 1.60 A; A/B/C/D=152-256. DR PDBsum; 2V76; -. DR BMRB; Q99704; -. DR SMR; Q99704; -. DR BioGRID; 108131; 42. DR ELM; Q99704; -. DR IntAct; Q99704; 30. DR MINT; Q99704; -. DR STRING; 9606.ENSP00000233668; -. DR iPTMnet; Q99704; -. DR PhosphoSitePlus; Q99704; -. DR BioMuta; DOK1; -. DR DMDM; 17366642; -. DR EPD; Q99704; -. DR jPOST; Q99704; -. DR MassIVE; Q99704; -. DR MaxQB; Q99704; -. DR PaxDb; Q99704; -. DR PeptideAtlas; Q99704; -. DR PRIDE; Q99704; -. DR ProteomicsDB; 78413; -. [Q99704-1] DR ProteomicsDB; 78414; -. [Q99704-2] DR ProteomicsDB; 78415; -. [Q99704-3] DR Antibodypedia; 3784; 885 antibodies. DR DNASU; 1796; -. DR Ensembl; ENST00000233668; ENSP00000233668; ENSG00000115325. [Q99704-1] DR Ensembl; ENST00000340004; ENSP00000344330; ENSG00000115325. [Q99704-2] DR Ensembl; ENST00000409429; ENSP00000387016; ENSG00000115325. [Q99704-3] DR GeneID; 1796; -. DR KEGG; hsa:1796; -. DR UCSC; uc002smr.4; human. [Q99704-1] DR CTD; 1796; -. DR DisGeNET; 1796; -. DR GeneCards; DOK1; -. DR HGNC; HGNC:2990; DOK1. DR HPA; ENSG00000115325; Low tissue specificity. DR MIM; 602919; gene. DR neXtProt; NX_Q99704; -. DR OpenTargets; ENSG00000115325; -. DR PharmGKB; PA27456; -. DR VEuPathDB; HostDB:ENSG00000115325; -. DR eggNOG; KOG4047; Eukaryota. DR GeneTree; ENSGT00940000155980; -. DR HOGENOM; CLU_056741_0_0_1; -. DR InParanoid; Q99704; -. DR OMA; ALYSQVH; -. DR PhylomeDB; Q99704; -. DR TreeFam; TF324994; -. DR PathwayCommons; Q99704; -. DR Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1. DR Reactome; R-HSA-8853659; RET signaling. DR SignaLink; Q99704; -. DR SIGNOR; Q99704; -. DR BioGRID-ORCS; 1796; 3 hits in 1017 CRISPR screens. DR ChiTaRS; DOK1; human. DR EvolutionaryTrace; Q99704; -. DR GeneWiki; DOK1; -. DR GenomeRNAi; 1796; -. DR Pharos; Q99704; Tbio. DR PRO; PR:Q99704; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q99704; protein. DR Bgee; ENSG00000115325; Expressed in tendon and 244 other tissues. DR ExpressionAtlas; Q99704; baseline and differential. DR Genevisible; Q99704; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc. DR GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IEA:Ensembl. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc. DR CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1. DR Gene3D; 2.30.29.30; -; 2. DR InterPro; IPR037751; Dok1/2/3_PTB. DR InterPro; IPR002404; IRS_PTB. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR Pfam; PF02174; IRS; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00310; PTBI; 1. DR PROSITE; PS51064; IRS_PTB; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..481 FT /note="Docking protein 1" FT /id="PRO_0000187268" FT DOMAIN 4..119 FT /note="PH" FT DOMAIN 151..259 FT /note="IRS-type PTB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389" FT REGION 270..293 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 307..329 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 404..481 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..328 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..430 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 438..460 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 296 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P97465" FT MOD_RES 337 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P97465" FT MOD_RES 341 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 362 FT /note="Phosphotyrosine; by INSR" FT /evidence="ECO:0000269|PubMed:11551902, FT ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332" FT MOD_RES 377 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 398 FT /note="Phosphotyrosine; by INSR" FT /evidence="ECO:0000269|PubMed:11551902, FT ECO:0007744|PubMed:15592455" FT MOD_RES 409 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 416 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P97465" FT MOD_RES 449 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P97465" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..139 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_038224" FT VAR_SEQ 153..177 FT /note="SQFWVTVQRTEAAERCGLHGSYVLR -> HVLFRGRPPLPLRPWNLHLPDGT FT GK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10940083" FT /id="VSP_003852" FT VAR_SEQ 178..481 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10940083" FT /id="VSP_003853" FT MUTAGEN 362 FT /note="Y->F: No association with NCK. No association with FT GAP; when associated with F-398." FT /evidence="ECO:0000269|PubMed:11551902" FT MUTAGEN 398 FT /note="Y->F: No association with GAP; when associated with FT F-362." FT /evidence="ECO:0000269|PubMed:11551902" FT CONFLICT 1..20 FT /note="MDGAVMEGPLFLQSQRFGTK -> RLPAQASATREREPRWSPFQ (in FT Ref. 3; AAB88182)" FT /evidence="ECO:0000305" FT STRAND 153..159 FT /evidence="ECO:0007829|PDB:2V76" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 180..188 FT /evidence="ECO:0007829|PDB:2V76" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 195..202 FT /evidence="ECO:0007829|PDB:2V76" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 206..211 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 213..220 FT /evidence="ECO:0007829|PDB:2V76" FT STRAND 228..234 FT /evidence="ECO:0007829|PDB:2V76" FT HELIX 238..251 FT /evidence="ECO:0007829|PDB:2V76" FT MOD_RES Q99704-3:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:19481542" SQ SEQUENCE 481 AA; 52392 MW; E9D947831244BA6C CRC64; MDGAVMEGPL FLQSQRFGTK RWRKTWAVLY PASPHGVARL EFFDHKGSSS GGGRGSSRRL DCKVIRLAEC VSVAPVTVET PPEPGATAFR LDTAQRSHLL AADAPSSAAW VQTLCRNAFP KGSWTLAPTD NPPKLSALEM LENSLYSPTW EGSQFWVTVQ RTEAAERCGL HGSYVLRVEA ERLTLLTVGA QSQILEPLLS WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND IFQAVETAIH RQKAQGKAGQ GHDVLRADSH EGEVAEGKLP SPPGPQELLD SPPALYAEPL DSLRIAPCPS QDSLYSDPLD STSAQAGEGV QRKKPLYWDL YEHAQQQLLK AKLTDPKEDP IYDEPEGLAP VPPQGLYDLP REPKDAWWCQ ARVKEEGYEL PYNPATDDYA VPPPRSTKPL LAPKPQGPAF PEPGTATGSG IKSHNSALYS QVQKSGASGS WDCGLSRVGT DKTGVKSEGS T //