GPV_HUMAN
ID GPV_HUMAN Reviewed; 560 AA.
AC P40197; D1MER9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
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 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].
RC TISSUE=Lung;
RX PubMed=7690959; DOI=10.1073/pnas.90.18.8327;
RA Hickey M.J., Hagen F.S., Yagi M., Roth G.J.;
RT "Human platelet glycoprotein V: characterization of the polypeptide and the
RT related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8327-8331(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Platelet;
RX PubMed=8407908; DOI=10.1016/s0021-9258(19)36855-3;
RA Lanza F., Morales M., de la Salle C., Cazenave J.-P., Clemetson K.J.,
RA Shimomura T., Phillips D.R.;
RT "Cloning and characterization of the gene encoding the human platelet
RT glycoprotein V. A member of the leucine-rich glycoprotein family cleaved
RT during thrombin-induced platelet activation.";
RL J. Biol. Chem. 268:20801-20807(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Xu L., Liu L., Zhang D., Sun G., Wang P., Sun N., Hu Q., Li X., Cao F.,
RA Peng B., Yu S.;
RT "Single novel mutation in transmembrane region of glycoprotein IX affects
RT platelet surface expressions of glycoprotein GP-Ib-IX complex and causes
RT Bernard Soulier syndrome.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Platelet;
RX PubMed=2350580;
RA Shimomura T., Fujimura K., Maehama S., Takemoto M., Oda K., Fujimoto T.,
RA Oyama R., Suzuki M., Icihara-Tanaka K., Titani K., Kuramoto A.;
RT "Rapid purification and characterization of human platelet glycoprotein V:
RT the amino acid sequence contains leucine-rich repetitive modules as in
RT glycoprotein Ib.";
RL Blood 75:2349-2356(1990).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Platelet;
RX PubMed=2372284; DOI=10.1016/0006-291x(90)91253-o;
RA Roth G.J., Church T.A., McMullen B.A., Williams S.A.;
RT "Human platelet glycoprotein V: a surface leucine-rich glycoprotein related
RT to adhesion.";
RL Biochem. Biophys. Res. Commun. 170:153-161(1990).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [8]
RP GLYCOSYLATION AT ASN-181 AND ASN-243.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
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.
CC -!- INTERACTION:
CC P40197; P14770: GP9; NbExp=2; IntAct=EBI-10891395, EBI-1754109;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Platelets and megakaryocytes.
CC -!- PTM: The N-terminus is blocked.
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DR EMBL; L11238; AAA03069.1; -; mRNA.
DR EMBL; Z23091; CAA80637.1; -; Genomic_DNA.
DR EMBL; GU138099; ACZ44929.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78053.1; -; Genomic_DNA.
DR CCDS; CCDS3307.1; -.
DR PIR; A48030; A60164.
DR RefSeq; NP_004479.1; NM_004488.2.
DR AlphaFoldDB; P40197; -.
DR SMR; P40197; -.
DR BioGRID; 109076; 73.
DR ComplexPortal; CPX-114; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-117; Glycoprotein Ib-IX-V-Filamin-A complex.
DR IntAct; P40197; 1.
DR STRING; 9606.ENSP00000383931; -.
DR GlyConnect; 1968; 6 N-Linked glycans (2 sites).
DR GlyGen; P40197; 8 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; P40197; -.
DR PhosphoSitePlus; P40197; -.
DR BioMuta; GP5; -.
DR DMDM; 729616; -.
DR jPOST; P40197; -.
DR MassIVE; P40197; -.
DR PaxDb; P40197; -.
DR PeptideAtlas; P40197; -.
DR PRIDE; P40197; -.
DR ProteomicsDB; 55341; -.
DR Antibodypedia; 56829; 154 antibodies from 19 providers.
DR DNASU; 2814; -.
DR Ensembl; ENST00000401815.1; ENSP00000383931.1; ENSG00000178732.6.
DR Ensembl; ENST00000692618.1; ENSP00000509337.1; ENSG00000178732.6.
DR GeneID; 2814; -.
DR KEGG; hsa:2814; -.
DR MANE-Select; ENST00000692618.1; ENSP00000509337.1; NM_004488.2; NP_004479.1.
DR UCSC; uc062rou.1; human.
DR CTD; 2814; -.
DR DisGeNET; 2814; -.
DR GeneCards; GP5; -.
DR HGNC; HGNC:4443; GP5.
DR HPA; ENSG00000178732; Tissue enhanced (lymphoid).
DR MIM; 173511; gene.
DR neXtProt; NX_P40197; -.
DR OpenTargets; ENSG00000178732; -.
DR PharmGKB; PA28823; -.
DR VEuPathDB; HostDB:ENSG00000178732; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162953; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; P40197; -.
DR OMA; FAMIKIG; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P40197; -.
DR TreeFam; TF351124; -.
DR PathwayCommons; P40197; -.
DR Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-HSA-9673221; Defective F9 activation.
DR SignaLink; P40197; -.
DR SIGNOR; P40197; -.
DR BioGRID-ORCS; 2814; 9 hits in 1067 CRISPR screens.
DR GeneWiki; GP5; -.
DR GenomeRNAi; 2814; -.
DR Pharos; P40197; Tbio.
DR PRO; PR:P40197; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P40197; protein.
DR Bgee; ENSG00000178732; Expressed in monocyte and 31 other tissues.
DR Genevisible; P40197; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IPI:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0035855; P:megakaryocyte development; IC:ComplexPortal.
DR GO; GO:0010572; P:positive regulation of platelet activation; IDA:ComplexPortal.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:ComplexPortal.
DR Gene3D; 3.80.10.10; -; 2.
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 Pfam; PF13855; LRR_8; 5.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Direct protein sequencing; Glycoprotein;
KW Hemostasis; Leucine-rich repeat; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..560
FT /note="Platelet glycoprotein V"
FT /id="PRO_0000021361"
FT TOPO_DOM 17..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..560
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 340..361
FT /note="LRR 11"
FT REPEAT 364..385
FT /note="LRR 12"
FT REPEAT 388..409
FT /note="LRR 13"
FT DOMAIN 421..474
FT /note="LRRCT"
FT REGION 469..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 130
FT /note="D -> W (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..138
FT /note="GID -> PGG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="N -> H (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 60959 MW; B1CDB04AF8AF7115 CRC64;
MLRGTLLCAV LGLLRAQPFP CPPACKCVFR DAAQCSGGDV ARISALGLPT NLTHILLFGM
GRGVLQSQSF SGMTVLQRLM ISDSHISAVA PGTFSDLIKL KTLRLSRNKI THLPGALLDK
MVLLEQLFLD HNALRGIDQN MFQKLVNLQE LALNQNQLDF LPASLFTNLE NLKLLDLSGN
NLTHLPKGLL GAQAKLERLL LHSNRLVSLD SGLLNSLGAL TELQFHRNHI RSIAPGAFDR
LPNLSSLTLS RNHLAFLPSA LFLHSHNLTL LTLFENPLAE LPGVLFGEMG GLQELWLNRT
QLRTLPAAAF RNLSRLRYLG VTLSPRLSAL PQGAFQGLGE LQVLALHSNG LTALPDGLLR
GLGKLRQVSL RRNRLRALPR ALFRNLSSLE SVQLDHNQLE TLPGDVFGAL PRLTEVLLGH
NSWRCDCGLG PFLGWLRQHL GLVGGEEPPR CAGPGAHAGL PLWALPGGDA ECPGPRGPPP
RPAADSSSEA PVHPALAPNS SEPWVWAQPV TTGKGQDHSP FWGFYFLLLA VQAMITVIIV
FAMIKIGQLF RKLIRERALG
