ID   GPV_MOUSE               Reviewed;         567 AA.
AC   O08742;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Platelet glycoprotein V;
DE            Short=GPV;
DE   AltName: Full=Glycoprotein 5;
DE   AltName: CD_antigen=CD42d;
DE   Flags: Precursor;
GN   Name=Gp5;
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 [GENOMIC DNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=9129030;
RA   Ravanat C., Morales M., Azorsa D.O., Moog S., Schuhler S., Grunert P.,
RA   Loew D., van Dorsselaer A., Cazenave J.-P., Lanza F.;
RT   "Gene cloning of rat and mouse platelet glycoprotein V: identification of
RT   megakaryocyte-specific promoters and demonstration of functional thrombin
RT   cleavage.";
RL   Blood 89:3253-3262(1997).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and
CC       mediates vWF-dependent platelet adhesion to blood vessels. The adhesion
CC       of platelets to injured vascular surfaces in the arterial circulation
CC       is a critical initiating event in hemostasis (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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; Z69595; CAA93441.1; -; Genomic_DNA.
DR   CCDS; CCDS28100.1; -.
DR   AlphaFoldDB; O08742; -.
DR   SMR; O08742; -.
DR   ComplexPortal; CPX-115; Glycoprotein Ib-IX-V complex.
DR   ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR   STRING; 10090.ENSMUSP00000051895; -.
DR   GlyCosmos; O08742; 7 sites, No reported glycans.
DR   GlyGen; O08742; 7 sites.
DR   PhosphoSitePlus; O08742; -.
DR   CPTAC; non-CPTAC-3306; -.
DR   MaxQB; O08742; -.
DR   PaxDb; 10090-ENSMUSP00000051895; -.
DR   PeptideAtlas; O08742; -.
DR   ProteomicsDB; 271083; -.
DR   AGR; MGI:1096363; -.
DR   MGI; MGI:1096363; Gp5.
DR   eggNOG; KOG0619; Eukaryota.
DR   InParanoid; O08742; -.
DR   PhylomeDB; O08742; -.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
DR   Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
DR   Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
DR   PRO; PR:O08742; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O08742; Protein.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:MGI.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0007596; P:blood coagulation; IDA:ComplexPortal.
DR   GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0035855; P:megakaryocyte development; IMP:ComplexPortal.
DR   GO; GO:0010544; P:negative regulation of platelet activation; IMP:MGI.
DR   GO; GO:0030168; P:platelet activation; IMP:MGI.
DR   GO; GO:0010572; P:positive regulation of platelet activation; ISO:MGI.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR46473:SF10; CHAOPTIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR46473; GH08155P; 1.
DR   Pfam; PF13855; LRR_8; 4.
DR   SMART; SM00369; LRR_TYP; 14.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   PROSITE; PS51450; LRR; 12.
PE   1: Evidence at protein level;
KW   Blood coagulation; Cell adhesion; Glycoprotein; Hemostasis;
KW   Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..567
FT                   /note="Platelet glycoprotein V"
FT                   /id="PRO_0000021362"
FT   TOPO_DOM        17..522
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        544..567
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..50
FT                   /note="LRRNT"
FT   REPEAT          75..96
FT                   /note="LRR 1"
FT   REPEAT          99..120
FT                   /note="LRR 2"
FT   REPEAT          123..144
FT                   /note="LRR 3"
FT   REPEAT          147..168
FT                   /note="LRR 4"
FT   REPEAT          171..193
FT                   /note="LRR 5"
FT   REPEAT          195..216
FT                   /note="LRR 6"
FT   REPEAT          219..240
FT                   /note="LRR 7"
FT   REPEAT          243..264
FT                   /note="LRR 8"
FT   REPEAT          267..288
FT                   /note="LRR 9"
FT   REPEAT          291..312
FT                   /note="LRR 10"
FT   REPEAT          315..337
FT                   /note="LRR 11"
FT   REPEAT          340..361
FT                   /note="LRR 12"
FT   REPEAT          364..385
FT                   /note="LRR 13"
FT   REPEAT          388..409
FT                   /note="LRR 14"
FT   DOMAIN          421..474
FT                   /note="LRRCT"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        298
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   567 AA;  63468 MW;  C48643AA73967A7D CRC64;
     MLRSALLSAV LPLLRAQPFP CPKTCKCVVR DAAQCSGGSV AHIAELGLPT NLTHILLFRM
     DQGILRNHSF SGMTVLQRQM LSDSHISAID PGTFNDLVKL KTLRLTRNKI SRLPRAILDK
     MVLLEQLFLD HNALRDLDQN LFQQLRNLQE LGLNQNQLSF LPANLFSSLR ELKLLDLSRN
     NLTHLPKGLL GAQVKLEKLL LYSNQLTSVD SGLLSNLGAL TELRLERNHL RSVAPGAFDR
     LGNLSSLTLS GNLLESLPPA LFLHVSSVSR LTLFENPLEE LPDVLFGEMA GLRELWLNGT
     HLSTLPAAAF RNLSGLQTLG LTRNPRLSAL PRGVFQGLRE LRVLGLHTNA LAELRDDALR
     GLGHLRQVSL RHNRLRALPR TLFRNLSSLE SVQLEHNQLE TLPGDVFAAL PQLTQVLLGH
     NPWLCDCGLW RFLQWLRHHP DILGRDEPPQ CRGPEPRASL SFWELLQGDP WCPDPRSLPL
     DPPTENALEA PVPSWLPNSW QSQTWAQLVA RGESPNNRLY WGLYILLLVA QAIIAAFIVF
     AMIKIGQLFR TLIREKLLLE AMGKSCN
//