GPVI_HUMAN
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 03-AUG-2022, entry version 175.
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 PDBsum; 2GI7; -.
DR PDBsum; 5OU7; -.
DR PDBsum; 5OU8; -.
DR PDBsum; 5OU9; -.
DR PDBsum; 7NMU; -.
DR AlphaFoldDB; Q9HCN6; -.
DR SMR; Q9HCN6; -.
DR BioGRID; 119379; 10.
DR DIP; DIP-33875N; -.
DR IntAct; Q9HCN6; 9.
DR MINT; Q9HCN6; -.
DR STRING; 9606.ENSP00000308782; -.
DR BindingDB; Q9HCN6; -.
DR ChEMBL; CHEMBL3308912; -.
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; Q9HCN6; -.
DR PeptideAtlas; Q9HCN6; -.
DR PRIDE; 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; 279 antibodies from 33 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; ENST00000612184.4; ENSP00000479873.1; ENSG00000277439.4. [Q9HCN6-2]
DR Ensembl; ENST00000616456.1; ENSP00000483314.1; ENSG00000277439.4. [Q9HCN6-1]
DR Ensembl; ENST00000622279.4; ENSP00000484029.1; ENSG00000277439.4. [Q9HCN6-3]
DR GeneID; 51206; -.
DR KEGG; hsa:51206; -.
DR MANE-Select; ENST00000310373.7; ENSP00000308782.3; NM_001083899.2; NP_001077368.2. [Q9HCN6-3]
DR UCSC; uc002qik.4; human. [Q9HCN6-1]
DR CTD; 51206; -.
DR DisGeNET; 51206; -.
DR GeneCards; GP6; -.
DR HGNC; HGNC:14388; GP6.
DR HPA; ENSG00000088053; Tissue enhanced (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; ENSGT01000000214458; -.
DR HOGENOM; CLU_532728_0_0_1; -.
DR InParanoid; Q9HCN6; -.
DR OMA; HAASSWC; -.
DR OrthoDB; 1000446at2759; -.
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 1079 CRISPR screens.
DR EvolutionaryTrace; Q9HCN6; -.
DR GeneWiki; GPVI; -.
DR GenomeRNAi; 51206; -.
DR Pharos; Q9HCN6; Tbio.
DR PRO; PR:Q9HCN6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HCN6; protein.
DR Bgee; ENSG00000088053; Expressed in monocyte and 91 other tissues.
DR ExpressionAtlas; Q9HCN6; baseline and differential.
DR Genevisible; Q9HCN6; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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 Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
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 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 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
