GenomeNet

Database: UniProt
Entry: Q9HCN6
LinkDB: Q9HCN6
Original site: Q9HCN6 
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   07-OCT-2020, entry version 167.
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 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   [11]
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   [12]
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   [13]
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 COL1A1, but not with
CC       COL4A4 (By 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 mutations 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}.
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   PDBsum; 2GI7; -.
DR   PDBsum; 5OU7; -.
DR   PDBsum; 5OU8; -.
DR   PDBsum; 5OU9; -.
DR   SMR; Q9HCN6; -.
DR   BioGRID; 119379; 9.
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   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; 281 antibodies.
DR   Ensembl; ENST00000310373; ENSP00000308782; ENSG00000088053. [Q9HCN6-3]
DR   Ensembl; ENST00000333884; ENSP00000334552; ENSG00000088053. [Q9HCN6-2]
DR   Ensembl; ENST00000417454; ENSP00000394922; ENSG00000088053. [Q9HCN6-1]
DR   Ensembl; ENST00000612184; ENSP00000479873; ENSG00000277439. [Q9HCN6-2]
DR   Ensembl; ENST00000616456; ENSP00000483314; ENSG00000277439. [Q9HCN6-1]
DR   Ensembl; ENST00000622279; ENSP00000484029; ENSG00000277439. [Q9HCN6-3]
DR   GeneID; 51206; -.
DR   KEGG; hsa:51206; -.
DR   UCSC; uc002qik.4; human. [Q9HCN6-1]
DR   CTD; 51206; -.
DR   DisGeNET; 51206; -.
DR   EuPathDB; HostDB:ENSG00000088053.11; -.
DR   GeneCards; GP6; -.
DR   HGNC; HGNC:14388; GP6.
DR   HPA; ENSG00000088053; Tissue enhanced (lymphoid).
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   eggNOG; ENOG502RWXV; Eukaryota.
DR   GeneTree; ENSGT00980000198504; -.
DR   HOGENOM; CLU_532728_0_0_1; -.
DR   InParanoid; Q9HCN6; -.
DR   KO; K06264; -.
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   SIGNOR; Q9HCN6; -.
DR   BioGRID-ORCS; 51206; 3 hits in 872 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 143 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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; TAS:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; TAS:ProtInc.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
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 mutation; Disulfide bond; Glycoprotein;
KW   Hemostasis; Immunoglobulin domain; Membrane; Polymorphism; Receptor;
KW   Reference proteome; 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   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:0000244|PDB:5OU7"
FT   STRAND          36..39
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          44..49
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          55..61
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   TURN            62..65
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          66..77
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   HELIX           80..82
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          84..92
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          95..97
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          103..111
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          115..120
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   TURN            126..128
FT                   /evidence="ECO:0000244|PDB:5OU9"
FT   STRAND          130..135
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          142..147
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          149..151
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          159..170
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          175..184
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          187..192
FT                   /evidence="ECO:0000244|PDB:5OU7"
FT   STRAND          198..201
FT                   /evidence="ECO:0000244|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
//
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