GPVI_MOUSE
ID GPVI_MOUSE Reviewed; 313 AA.
AC P0C191; E9QPN2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Platelet glycoprotein VI {ECO:0000305};
DE Short=GPVI {ECO:0000305};
DE AltName: Full=Glycoprotein 5;
DE Flags: Precursor;
GN Name=Gp6 {ECO:0000312|MGI:MGI:1889810};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH
RP FC RECEPTOR GAMMA CHAIN, AND DEVELOPMENTAL STAGE.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION.
RX PubMed=16254207; DOI=10.1161/01.atv.0000193568.71980.4a;
RA Munnix I.C., Strehl A., Kuijpers M.J., Auger J.M., van der Meijden P.E.,
RA van Zandvoort M.A., oude Egbrink M.G., Nieswandt B., Heemskerk J.W.;
RT "The glycoprotein VI-phospholipase Cgamma2 signaling pathway controls
RT thrombus formation induced by collagen and tissue factor in vitro and in
RT vivo.";
RL Arterioscler. Thromb. Vasc. Biol. 25:2673-2678(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16139873; DOI=10.1016/j.thromres.2005.08.001;
RA Lockyer S., Okuyama K., Begum S., Le S., Sun B., Watanabe T., Matsumoto Y.,
RA Yoshitake M., Kambayashi J., Tandon N.N.;
RT "GPVI-deficient mice lack collagen responses and are protected against
RT experimentally induced pulmonary thromboembolism.";
RL Thromb. Res. 118:371-380(2006).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH
RP COL1A1, AND LACK OF INTERACTION WITH COL4A4.
RX PubMed=24368846; DOI=10.1073/pnas.1307597111;
RA Pokidysheva E., Boudko S., Vranka J., Zientek K., Maddox K., Moser M.,
RA Faessler R., Ware J., Baechinger H.P.;
RT "Biological role of prolyl 3-hydroxylation in type IV collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:161-166(2014).
CC -!- FUNCTION: Collagen receptor involved in collagen-induced platelet
CC adhesion and activation (PubMed:16139873, PubMed:24368846). Plays a key
CC role in platelet procoagulant activity and subsequent thrombin and
CC fibrin formation. This procoagulant function may contribute to arterial
CC and venous thrombus formation. The signaling pathway involves the FcR
CC gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter
CC protein LAT and leads to the activation of PLCG2.
CC {ECO:0000269|PubMed:10961879, ECO:0000269|PubMed:16139873,
CC ECO:0000269|PubMed:16254207, ECO:0000269|PubMed:24368846}.
CC -!- SUBUNIT: Associated with Fc receptor gamma chain. The GPVI:FcRgamma
CC complex is associated with the Src kinase family FYN and LYN. Interacts
CC with TRAF4 (By similarity). Interacts with COL1A1, but not with COL4A4
CC (PubMed:24368846). {ECO:0000250|UniProtKB:Q9HCN6,
CC ECO:0000269|PubMed:24368846}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:24368846};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Megakaryocytes and platelets.
CC {ECO:0000269|PubMed:10961879}.
CC -!- DEVELOPMENTAL STAGE: Expressed at embryonic day 13.5, 14.5 and 16.5.
CC Expression decreases in intensity at day 18.5 and in 1.5 day-old
CC newborn. {ECO:0000269|PubMed:10961879}.
CC -!- DISRUPTION PHENOTYPE: Mice deficient in Gp6 show a complete protection
CC against arterial thrombosis and induced pulmonary thromboembolism,
CC without significant prolongation of bleeding time (PubMed:16139873).
CC Mutant mice deficient in Gp6 and P3h2 are born at the expected
CC Mendelian rate and have no visible phenotype (PubMed:24368846).
CC {ECO:0000269|PubMed:16139873, ECO:0000269|PubMed:24368846}.
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DR EMBL; AC137969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51972.1; -.
DR RefSeq; NP_001156486.1; NM_001163014.1.
DR AlphaFoldDB; P0C191; -.
DR SMR; P0C191; -.
DR STRING; 10090.ENSMUSP00000104231; -.
DR GlyGen; P0C191; 2 sites.
DR PhosphoSitePlus; P0C191; -.
DR MaxQB; P0C191; -.
DR PaxDb; P0C191; -.
DR PRIDE; P0C191; -.
DR ProteomicsDB; 271082; -.
DR ABCD; P0C191; 1 sequenced antibody.
DR Antibodypedia; 32992; 279 antibodies from 33 providers.
DR DNASU; 243816; -.
DR Ensembl; ENSMUST00000206928; ENSMUSP00000145740; ENSMUSG00000078810.
DR GeneID; 243816; -.
DR KEGG; mmu:243816; -.
DR UCSC; uc009exk.2; mouse.
DR CTD; 51206; -.
DR MGI; MGI:1889810; Gp6.
DR VEuPathDB; HostDB:ENSMUSG00000078810; -.
DR eggNOG; ENOG502SWRJ; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_1_0_1; -.
DR InParanoid; P0C191; -.
DR OMA; ELMVTEF; -.
DR OrthoDB; 1327293at2759; -.
DR PhylomeDB; P0C191; -.
DR TreeFam; TF336644; -.
DR Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR BioGRID-ORCS; 243816; 1 hit in 73 CRISPR screens.
DR PRO; PR:P0C191; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P0C191; protein.
DR Bgee; ENSMUSG00000078810; Expressed in blood and 21 other tissues.
DR ExpressionAtlas; P0C191; baseline and differential.
DR Genevisible; P0C191; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0038064; F:collagen receptor activity; IMP:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0038065; P:collagen-activated signaling pathway; IMP:MGI.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IMP:MGI.
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 Blood coagulation; Cell membrane; Disulfide bond; Glycoprotein; Hemostasis;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..313
FT /note="Platelet glycoprotein VI"
FT /id="PRO_0000232384"
FT TOPO_DOM 22..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 115..197
FT /note="Ig-like C2-type 2"
FT REGION 213..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCN6"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..89
FT /evidence="ECO:0000250|UniProtKB:Q9HCN6"
FT DISULFID 135..181
FT /evidence="ECO:0000250|UniProtKB:Q9HCN6"
FT CONFLICT 256
FT /note="F -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 34595 MW; 34D810EAE120C535 CRC64;
MSPASPTFFC IGLCVLQVIQ TQSGPLPKPS LQAQPSSLVP LGQSVILRCQ GPPDVDLYRL
EKLKPEKYED QDFLFIPTME RSNAGRYRCS YQNGSHWSLP SDQLELIATG VYAKPSLSAH
PSSAVPQGRD VTLKCQSPYS FDEFVLYKEG DTGSYKRPEK WYRANFPIIT VTAAHSGTYR
CYSFSSSSPY LWSAPSDPLV LVVTGLSATP SQVPTEESFP VTESSRRPSI LPTNKISTTE
KPMNITASPE GLSPPFGFAH QHYAKGNLVR ICLGATIIII LLGLLAEDWH SRKKCLQHRM
RALQRPLPPL PLA
