ID GPVI_HUMAN Reviewed; 339 AA. AC Q9HCN6; Q9HCN7; Q9UIF2; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 4. DT 27-MAR-2024, entry version 184. DE RecName: Full=Platelet glycoprotein VI {ECO:0000305}; DE Short=GPVI {ECO:0000305}; DE AltName: Full=Glycoprotein 6; DE Flags: Precursor; GN Name=GP6 {ECO:0000312|HGNC:HGNC:14388}; 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] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF RP 28-41; 62-79 AND 114-142, AND VARIANTS SER-219; LYS-237; THR-249; GLN-317 RP AND HIS-322. RX PubMed=11027634; DOI=10.1006/bbrc.2000.3624; RA Ezumi Y., Uchiyama T., Takayama H.; RT "Molecular cloning, genomic structure, chromosomal localization, and RT alternative splice forms of the platelet collagen receptor glycoprotein RT VI."; RL Biochem. Biophys. Res. Commun. 277:27-36(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH FC RP RECEPTOR GAMMA CHAIN, AND TISSUE SPECIFICITY. RC TISSUE=Megakaryocyte; RX PubMed=10961879; RA Jandrot-Perrus M., Busfield S., Lagrue A.-H., Xiong X., Debili N., RA Chickering T., Le Couedic J.-P., Goodearl A., Dussault B., Fraser C., RA Vainchenker W., Villeval J.-L.; RT "Cloning, characterization, and functional studies of human and mouse RT glycoprotein VI: a platelet-specific collagen receptor from the RT immunoglobulin superfamily."; RL Blood 96:1798-1807(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-219; LYS-237; RP THR-249; GLN-317 AND HIS-322. RA Miura Y.; RT "Platelet glycoprotein VI."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-219; RP LYS-237; THR-249; GLN-317 AND HIS-322. 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 INTERACTION WITH FC RECEPTOR GAMMA CHAIN. RX PubMed=9295288; DOI=10.1074/jbc.272.38.23528; RA Tsuji M., Ezumi Y., Arai M., Takayama H.; RT "A novel association of Fc receptor gamma-chain with glycoprotein VI and RT their co-expression as a collagen receptor in human platelets."; RL J. Biol. Chem. 272:23528-23531(1997). RN [7] RP GLYCOSYLATION AT ASN-92, AND MUTAGENESIS OF ASN-92; SER-94 AND LEU-95. RX PubMed=16014566; DOI=10.1182/blood-2005-04-1454; RA Kunicki T.J., Cheli Y., Moroi M., Furihata K.; RT "The influence of N-linked glycosylation on the function of platelet RT glycoprotein VI."; RL Blood 106:2744-2749(2005). RN [8] RP MUTAGENESIS OF LYS-61; LYS-79; ARG-80 AND ARG-186. RX PubMed=16405521; DOI=10.1111/j.1538-7836.2005.01764.x; RA O'connor M.N., Smethurst P.A., Farndale R.W., Ouwehand W.H.; RT "Gain- and loss-of-function mutants confirm the importance of apical RT residues to the primary interaction of human glycoprotein VI with RT collagen."; RL J. Thromb. Haemost. 4:869-873(2006). RN [9] RP FUNCTION. RX PubMed=18955485; DOI=10.1074/jbc.m806895200; RA Mori J., Pearce A.C., Spalton J.C., Grygielska B., Eble J.A., RA Tomlinson M.G., Senis Y.A., Watson S.P.; RT "G6b-B inhibits constitutive and agonist-induced signaling by glycoprotein RT VI and CLEC-2."; RL J. Biol. Chem. 283:35419-35427(2008). RN [10] RP INTERACTION WITH TRAF4. RX PubMed=20946164; DOI=10.1111/j.1538-7836.2010.04091.x; RA Arthur J.F., Shen Y., Gardiner E.E., Coleman L., Murphy D., Kenny D., RA Andrews R.K., Berndt M.C.; RT "TNF receptor-associated factor 4 (TRAF4) is a novel binding partner of RT glycoprotein Ib and glycoprotein VI in human platelets."; RL J. Thromb. Haemost. 9:163-172(2011). RN [11] RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SSL5 (MICROBIAL INFECTION). RX PubMed=21552524; DOI=10.1371/journal.pone.0019190; RA Hu H., Armstrong P.C., Khalil E., Chen Y.C., Straub A., Li M., RA Soosairajah J., Hagemeyer C.E., Bassler N., Huang D., Ahrens I., RA Krippner G., Gardiner E., Peter K.; RT "GPVI and GPIbalpha mediate staphylococcal superantigen-like protein 5 RT (SSL5) induced platelet activation and direct toward glycans as potential RT inhibitors."; RL PLoS ONE 6:E19190-E19190(2011). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-203, AND DISULFIDE BONDS. RX PubMed=16861347; DOI=10.1182/blood-2006-01-010215; RA Horii K., Kahn M.L., Herr A.B.; RT "Structural basis for platelet collagen responses by the immune-type RT receptor glycoprotein VI."; RL Blood 108:936-942(2006). RN [13] RP VARIANT BDPLT11 CYS-58, AND CHARACTERIZATION OF VARIANT BDPLT11 CYS-58. RX PubMed=19549989; DOI=10.1182/blood-2009-03-213504; RA Dumont B., Lasne D., Rothschild C., Bouabdelli M., Ollivier V., Oudin C., RA Ajzenberg N., Grandchamp B., Jandrot-Perrus M.; RT "Absence of collagen-induced platelet activation caused by compound RT heterozygous GPVI mutations."; RL Blood 114:1900-1903(2009). RN [14] RP VARIANT BDPLT11 ASN-175, AND CHARACTERIZATION OF VARIANT BDPLT11 ASN-175. RX PubMed=19552682; DOI=10.1111/j.1538-7836.2009.03520.x; RA Hermans C., Wittevrongel C., Thys C., Smethurst P.A., Van Geet C., RA Freson K.; RT "A compound heterozygous mutation in glycoprotein VI in a patient with a RT bleeding disorder."; RL J. Thromb. Haemost. 7:1356-1363(2009). CC -!- FUNCTION: Collagen receptor involved in collagen-induced platelet CC adhesion and activation. Plays a key role in platelet procoagulant CC activity and subsequent thrombin and fibrin formation. This CC procoagulant function may contribute to arterial and venous thrombus CC formation. The signaling pathway involves the FcR gamma-chain, the Src CC kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads CC to the activation of PLCG2. {ECO:0000269|PubMed:10961879, CC ECO:0000269|PubMed:18955485}. CC -!- SUBUNIT: Associated with Fc receptor gamma chain. The GPVI:FcRgamma CC complex is associated with the Src kinase family FYN and LYN CC (PubMed:10961879, PubMed:9295288). Interacts with TRAF4 CC (PubMed:20946164). Interacts with COL1A1, but not with COL4A4 (By CC similarity). {ECO:0000250|UniProtKB:P0C191, CC ECO:0000269|PubMed:10961879, ECO:0000269|PubMed:9295288}. CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus CC protein SSL5. {ECO:0000269|PubMed:21552524}. CC -!- INTERACTION: CC Q9HCN6; P06241: FYN; NbExp=2; IntAct=EBI-515278, EBI-515315; CC Q9HCN6; P07948: LYN; NbExp=5; IntAct=EBI-515278, EBI-79452; CC Q9HCN6-1; P06241: FYN; NbExp=2; IntAct=EBI-15816577, EBI-515315; CC Q9HCN6-1; P07948: LYN; NbExp=2; IntAct=EBI-15816577, EBI-79452; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass membrane CC protein. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=VI-1; CC IsoId=Q9HCN6-1; Sequence=Displayed; CC Name=2; Synonyms=VI-2; CC IsoId=Q9HCN6-2; Sequence=VSP_017879; CC Name=3; Synonyms=VI-3; CC IsoId=Q9HCN6-3; Sequence=VSP_017880; CC -!- TISSUE SPECIFICITY: Megakaryocytes and platelets. CC {ECO:0000269|PubMed:10961879}. CC -!- PTM: N-linked glycosylation at Asn-92 is not required for the cell CC surface expression, but contributes to maximal adhesion to type I CC collagen, collagen-related peptide (CRP), and, to a lesser extent, to CC the snake venom C-type lectin convulxin (CVX). CC {ECO:0000269|PubMed:16014566}. CC -!- DISEASE: Bleeding disorder, platelet-type, 11 (BDPLT11) [MIM:614201]: A CC mild to moderate bleeding disorder caused by defective platelet CC activation and aggregation in response to collagen. CC {ECO:0000269|PubMed:19549989, ECO:0000269|PubMed:19552682}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 3]: Has no transmembrane domain. Does not CC interact with Fc receptor gamma chain. Does not bind to collagen-like CC peptides. {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; AB043819; BAB12245.1; -; mRNA. DR EMBL; AB043820; BAB12246.1; -; mRNA. DR EMBL; AB043821; BAB12247.1; -; mRNA. DR EMBL; AB035073; BAA89353.1; -; mRNA. DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC104832; AAI04833.1; -; mRNA. DR EMBL; BC111963; AAI11964.1; -; mRNA. DR CCDS; CCDS42626.1; -. [Q9HCN6-3] DR CCDS; CCDS46184.1; -. [Q9HCN6-1] DR CCDS; CCDS58678.1; -. [Q9HCN6-2] DR PIR; JC7509; JC7509. DR RefSeq; NP_001077368.2; NM_001083899.2. [Q9HCN6-3] DR RefSeq; NP_001242946.2; NM_001256017.2. [Q9HCN6-2] DR RefSeq; NP_057447.5; NM_016363.5. [Q9HCN6-1] DR PDB; 2GI7; X-ray; 2.40 A; A/B=21-203. DR PDB; 5OU7; X-ray; 1.90 A; A/B/C/D=21-206. DR PDB; 5OU8; X-ray; 2.50 A; A/B=21-206. DR PDB; 5OU9; X-ray; 2.50 A; A/B=21-206. DR PDB; 7NMU; X-ray; 2.50 A; AAA/BBB=22-204. DR PDB; 7R58; X-ray; 1.90 A; A=21-203. DR PDBsum; 2GI7; -. DR PDBsum; 5OU7; -. DR PDBsum; 5OU8; -. DR PDBsum; 5OU9; -. DR PDBsum; 7NMU; -. DR PDBsum; 7R58; -. DR AlphaFoldDB; Q9HCN6; -. DR SMR; Q9HCN6; -. DR BioGRID; 119379; 11. DR DIP; DIP-33875N; -. DR IntAct; Q9HCN6; 9. DR MINT; Q9HCN6; -. DR STRING; 9606.ENSP00000308782; -. DR BindingDB; Q9HCN6; -. DR ChEMBL; CHEMBL3308912; -. DR GlyCosmos; Q9HCN6; 1 site, No reported glycans. DR GlyGen; Q9HCN6; 1 site. DR iPTMnet; Q9HCN6; -. DR PhosphoSitePlus; Q9HCN6; -. DR BioMuta; GP6; -. DR DMDM; 327478600; -. DR jPOST; Q9HCN6; -. DR MassIVE; Q9HCN6; -. DR PaxDb; 9606-ENSP00000308782; -. DR PeptideAtlas; Q9HCN6; -. DR ProteomicsDB; 81778; -. [Q9HCN6-1] DR ProteomicsDB; 81779; -. [Q9HCN6-2] DR ProteomicsDB; 81780; -. [Q9HCN6-3] DR ABCD; Q9HCN6; 42 sequenced antibodies. DR Antibodypedia; 32992; 345 antibodies from 34 providers. DR DNASU; 51206; -. DR Ensembl; ENST00000310373.7; ENSP00000308782.3; ENSG00000088053.11. [Q9HCN6-3] DR Ensembl; ENST00000333884.2; ENSP00000334552.2; ENSG00000088053.11. [Q9HCN6-2] DR Ensembl; ENST00000417454.5; ENSP00000394922.1; ENSG00000088053.11. [Q9HCN6-1] DR Ensembl; ENST00000610596.1; ENSP00000480178.1; ENSG00000275633.4. [Q9HCN6-2] DR Ensembl; ENST00000610746.4; ENSP00000479975.1; ENSG00000276211.4. [Q9HCN6-3] DR Ensembl; ENST00000611436.4; ENSP00000482601.1; ENSG00000275931.4. [Q9HCN6-3] DR Ensembl; ENST00000612096.1; ENSP00000481583.1; ENSG00000276065.4. [Q9HCN6-2] DR Ensembl; ENST00000612184.4; ENSP00000479873.1; ENSG00000277439.4. [Q9HCN6-2] DR Ensembl; ENST00000612862.1; ENSP00000483612.1; ENSG00000274050.4. [Q9HCN6-2] DR Ensembl; ENST00000613649.4; ENSP00000479668.1; ENSG00000274566.4. [Q9HCN6-3] DR Ensembl; ENST00000613801.1; ENSP00000478918.1; ENSG00000278670.4. [Q9HCN6-2] DR Ensembl; ENST00000614662.4; ENSP00000478025.1; ENSG00000276065.4. [Q9HCN6-3] DR Ensembl; ENST00000614889.1; ENSP00000478674.1; ENSG00000274566.4. [Q9HCN6-2] DR Ensembl; ENST00000615407.4; ENSP00000481524.1; ENSG00000278670.4. [Q9HCN6-3] DR Ensembl; ENST00000616319.1; ENSP00000481125.1; ENSG00000278316.4. [Q9HCN6-2] DR Ensembl; ENST00000616456.1; ENSP00000483314.1; ENSG00000277439.4. [Q9HCN6-1] DR Ensembl; ENST00000617954.4; ENSP00000480243.1; ENSG00000275633.4. [Q9HCN6-3] DR Ensembl; ENST00000619136.4; ENSP00000479034.1; ENSG00000278316.4. [Q9HCN6-3] DR Ensembl; ENST00000621278.1; ENSP00000479513.1; ENSG00000276211.4. [Q9HCN6-2] DR Ensembl; ENST00000622279.4; ENSP00000484029.1; ENSG00000277439.4. [Q9HCN6-3] DR Ensembl; ENST00000622589.4; ENSP00000481075.1; ENSG00000274050.4. [Q9HCN6-3] DR Ensembl; ENST00000622653.1; ENSP00000478709.1; ENSG00000275931.4. [Q9HCN6-2] DR GeneID; 51206; -. DR KEGG; hsa:51206; -. DR MANE-Select; ENST00000417454.5; ENSP00000394922.1; NM_016363.5; NP_057447.5. DR UCSC; uc002qik.4; human. [Q9HCN6-1] DR AGR; HGNC:14388; -. DR CTD; 51206; -. DR DisGeNET; 51206; -. DR GeneCards; GP6; -. DR HGNC; HGNC:14388; GP6. DR HPA; ENSG00000088053; Tissue enhanced (brain, testis). DR MalaCards; GP6; -. DR MIM; 605546; gene. DR MIM; 614201; phenotype. DR neXtProt; NX_Q9HCN6; -. DR OpenTargets; ENSG00000088053; -. DR Orphanet; 98885; Bleeding diathesis due to glycoprotein VI deficiency. DR PharmGKB; PA28824; -. DR VEuPathDB; HostDB:ENSG00000088053; -. DR eggNOG; ENOG502RWXV; Eukaryota. DR GeneTree; ENSGT01100000263478; -. DR HOGENOM; CLU_532728_0_0_1; -. DR InParanoid; Q9HCN6; -. DR OMA; LKDWRVW; -. DR OrthoDB; 4596687at2759; -. DR PhylomeDB; Q9HCN6; -. DR TreeFam; TF336644; -. DR PathwayCommons; Q9HCN6; -. DR Reactome; R-HSA-114604; GPVI-mediated activation cascade. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen. DR SignaLink; Q9HCN6; -. DR SIGNOR; Q9HCN6; -. DR BioGRID-ORCS; 51206; 11 hits in 1157 CRISPR screens. DR EvolutionaryTrace; Q9HCN6; -. DR GeneWiki; GPVI; -. DR GenomeRNAi; 51206; -. DR Pharos; Q9HCN6; Tchem. DR PRO; PR:Q9HCN6; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9HCN6; Protein. DR Bgee; ENSG00000088053; Expressed in monocyte and 93 other cell types or tissues. DR ExpressionAtlas; Q9HCN6; baseline and differential. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB. DR GO; GO:0005518; F:collagen binding; TAS:UniProtKB. DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL. DR GO; GO:0038023; F:signaling receptor activity; TAS:UniProtKB. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0038065; P:collagen-activated signaling pathway; TAS:ARUK-UCL. DR GO; GO:0007167; P:enzyme-linked receptor protein signaling pathway; TAS:ProtInc. DR GO; GO:0030168; P:platelet activation; NAS:UniProtKB. DR GO; GO:1901731; P:positive regulation of platelet aggregation; TAS:ARUK-UCL. DR CDD; cd05751; IgC2_D1_LILR_KIR_like; 1. DR CDD; cd05711; IgC2_D2_LILR_KIR_like; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1. DR PANTHER; PTHR11738:SF159; PLATELET GLYCOPROTEIN VI; 1. DR Pfam; PF13895; Ig_2; 1. DR Pfam; PF13927; Ig_3; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR Genevisible; Q9HCN6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood coagulation; Cell membrane; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; KW Hemostasis; Immunoglobulin domain; Membrane; Receptor; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..339 FT /note="Platelet glycoprotein VI" FT /id="PRO_0000232383" FT TOPO_DOM 21..267 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 268..288 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 289..339 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 26..104 FT /note="Ig-like C2-type 1" FT DOMAIN 114..196 FT /note="Ig-like C2-type 2" FT REGION 299..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16014566" FT DISULFID 48..88 FT /evidence="ECO:0000269|PubMed:16861347" FT DISULFID 134..180 FT /evidence="ECO:0000269|PubMed:16861347" FT VAR_SEQ 204..221 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11027634" FT /id="VSP_017879" FT VAR_SEQ 260..339 FT /note="PARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPP FT LPPLPLTRKSNGGQDGGRQDVHSRGLCS -> ESCPPVLHQGQPGPDMPRGCDPNNPGG FT VSGRGLAQPEEAPAAQGQGCAEAASAPPAPPADPEIKRGSGWRPTGCSQPRVMFMTAEP FT QARSYPREGSWHGRRLKDWRVWSVEAGGQRLQLWKRGHAASSWCSIREPFGQCLSVCLP FT LCLRAPSIWDGRNLWRPHPPPCTLWMTWYPGWTTYWPLSSTSLIWAPDGSLRFPALRVD FT SVPSSVQNPPVLPFGPLCSCLVFPRNSHPHSISHCGLTNLLSSLRTGLAGSLGMSFIFL FT SVKLARCPLPFTLENKISLCNMVKPHLYQQNKKTQKLARCGGASLYSQQLRGLRWENGL FT SLGGRGCSELRSHHCTLARVTKPDFVSKNTGMNMSITLI (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11027634" FT /id="VSP_017880" FT VARIANT 58 FT /note="R -> C (in BDPLT11; results in abnormal protein FT migration and a loss of collagen binding; FT dbSNP:rs199588110)" FT /evidence="ECO:0000269|PubMed:19549989" FT /id="VAR_066590" FT VARIANT 175 FT /note="S -> N (in BDPLT11; shows strongly reduced membrane FT expression and decreased interaction with the snake toxin FT convulxin; dbSNP:rs387906919)" FT /evidence="ECO:0000269|PubMed:19552682" FT /id="VAR_066591" FT VARIANT 219 FT /note="P -> S (in dbSNP:rs1613662)" FT /evidence="ECO:0000269|PubMed:11027634, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_060352" FT VARIANT 237 FT /note="E -> K (in dbSNP:rs1654416)" FT /evidence="ECO:0000269|PubMed:11027634, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_060353" FT VARIANT 249 FT /note="A -> T (in dbSNP:rs2304167)" FT /evidence="ECO:0000269|PubMed:11027634, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_060354" FT VARIANT 317 FT /note="L -> Q (in dbSNP:rs1654413)" FT /evidence="ECO:0000269|PubMed:11027634, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_059389" FT VARIANT 322 FT /note="N -> H (in dbSNP:rs1671152)" FT /evidence="ECO:0000269|PubMed:11027634, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_059390" FT VARIANT 335 FT /note="R -> G (in dbSNP:rs1654412)" FT /id="VAR_060355" FT MUTAGEN 61 FT /note="K->A: Increases collagen binding." FT /evidence="ECO:0000269|PubMed:16405521" FT MUTAGEN 79 FT /note="K->E: Dramatically reduces collagen binding." FT /evidence="ECO:0000269|PubMed:16405521" FT MUTAGEN 80 FT /note="R->A: Reduces collagen binding." FT /evidence="ECO:0000269|PubMed:16405521" FT MUTAGEN 92 FT /note="N->A: Reduces collagen binding (65 to 70%)." FT /evidence="ECO:0000269|PubMed:16014566" FT MUTAGEN 94 FT /note="S->A: Reduces collagen binding (65 to 70%)." FT /evidence="ECO:0000269|PubMed:16014566" FT MUTAGEN 95 FT /note="L->H: No effect on collagen binding." FT /evidence="ECO:0000269|PubMed:16014566" FT MUTAGEN 186 FT /note="R->A: Reduces collagen binding." FT /evidence="ECO:0000269|PubMed:16405521" FT STRAND 29..34 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:5OU7" FT TURN 62..65 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 66..77 FT /evidence="ECO:0007829|PDB:5OU7" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 84..92 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 103..111 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 115..120 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 122..125 FT /evidence="ECO:0007829|PDB:7R58" FT TURN 126..128 FT /evidence="ECO:0007829|PDB:5OU9" FT STRAND 130..135 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 159..170 FT /evidence="ECO:0007829|PDB:5OU7" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:7R58" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 187..192 FT /evidence="ECO:0007829|PDB:5OU7" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:5OU7" FT CONFLICT Q9HCN6-3:314 FT /note="P -> A (in Ref. 1; BAB12247)" FT /evidence="ECO:0000305" FT CONFLICT Q9HCN6-3:323 FT /note="K -> T (in Ref. 1; BAB12247)" FT /evidence="ECO:0000305" FT CONFLICT Q9HCN6-3:573 FT /note="R -> G (in Ref. 1; BAB12247)" FT /evidence="ECO:0000305" FT CONFLICT Q9HCN6-3:606 FT /note="F -> L (in Ref. 1; BAB12247)" FT /evidence="ECO:0000305" SQ SEQUENCE 339 AA; 36866 MW; 3EFE2DD0E1676BA8 CRC64; MSPSPTALFC LGLCLGRVPA QSGPLPKPSL QALPSSLVPL EKPVTLRCQG PPGVDLYRLE KLSSSRYQDQ AVLFIPAMKR SLAGRYRCSY QNGSLWSLPS DQLELVATGV FAKPSLSAQP GPAVSSGGDV TLQCQTRYGF DQFALYKEGD PAPYKNPERW YRASFPIITV TAAHSGTYRC YSFSSRDPYL WSAPSDPLEL VVTGTSVTPS RLPTEPPSPV AEFSEATAEL TVSFTNEVFT TETSRSITAS PKESDSPAGP ARQYYTKGNL VRICLGAVIL IILAGFLAED WHSRRKRLRH RGRAVQRPLP PLPPLPLTRK SNGGQDGGRQ DVHSRGLCS //