GPV_RAT
ID GPV_RAT Reviewed; 567 AA.
AC O08770;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; 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).
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.
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DR EMBL; Z69594; CAA93440.1; -; Genomic_DNA.
DR RefSeq; NP_036927.1; NM_012795.2.
DR AlphaFoldDB; O08770; -.
DR SMR; O08770; -.
DR STRING; 10116.ENSRNOP00000047810; -.
DR GlyGen; O08770; 7 sites.
DR iPTMnet; O08770; -.
DR PhosphoSitePlus; O08770; -.
DR PaxDb; O08770; -.
DR PRIDE; O08770; -.
DR GeneID; 25259; -.
DR KEGG; rno:25259; -.
DR UCSC; RGD:2724; rat.
DR CTD; 2814; -.
DR RGD; 2724; Gp5.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; O08770; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O08770; -.
DR PRO; PR:O08770; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0035855; P:megakaryocyte development; ISO:RGD.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISO:RGD.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:RGD.
DR Gene3D; 3.80.10.10; -; 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 Pfam; PF13855; LRR_8; 4.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 13.
PE 3: Inferred from homology;
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_0000021363"
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 REGION 474..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
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"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 567 AA; 63345 MW; CA10708E0D03707F CRC64;
MLRSVLLSAV LSLVGAQPFP CPKTCKCVVR DAVQCSGGSV AHIAELGLPT NLTHILLFRM
DRGVLQSHSF SGMTVLQRLM LSDSHISAID PGTFNDLVKL KTLRLTRNKI SHLPRAILDK
MVLLEQLFLD HNALRDLDQN LFQKLLNLRD LCLNQNQLSF LPANLFSSLG KLKVLDLSRN
NLTHLPQGLL GAQIKLEKLL LYSNRLMSLD SGLLANLGAL TELRLERNHL RSIAPGAFDS
LGNLSTLTLS GNLLESLPPA LFLHVSWLTR LTLFENPLEE LPEVLFGEMA GLRELWLNGT
HLRTLPAAAF RNLSGLQTLG LTRNPLLSAL PPGMFHGLTE LRVLAVHTNA LEELPEDALR
GLGRLRQVSL RHNRLRALPR TLFRNLSSLV TVQLEHNQLK TLPGDVFAAL PQLTRVLLGH
NPWLCDCGLW PFLQWLRHHL ELLGRDEPPQ CNGPESRASL TFWELLQGDQ WCPSSRGLPP
DPPTENALKA PDPTQRPNSS QSWAWVQLVA RGESPDNRFY WNLYILLLIA QATIAGFIVF
AMIKIGQLFR TLIREELLFE AMGKSSN
