ID GPIX_MOUSE Reviewed; 177 AA.
AC O88186;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Platelet glycoprotein IX;
DE Short=GP-IX;
DE Short=GPIX;
DE AltName: Full=Glycoprotein 9;
DE AltName: CD_antigen=CD42a;
DE Flags: Precursor;
GN Name=Gp9;
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].
RX PubMed=9690810; DOI=10.1097/00001721-199806000-00011;
RA Kitaguchi T., Murata M., Ambo H., Ikeda Y.;
RT "Characterization of cDNA encoding full-length mouse platelet glycoprotein
RT IX.";
RL Blood Coagul. Fibrinolysis 9:381-385(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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. GP-IX may provide for
CC membrane insertion and orientation of GP-Ib (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX
CC is complexed with the GP-Ib heterodimer via a non covalent linkage (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AB007464; BAA31694.1; -; mRNA.
DR EMBL; CH466523; EDK99218.1; -; Genomic_DNA.
DR EMBL; BC111106; AAI11107.1; -; mRNA.
DR CCDS; CCDS20328.1; -.
DR RefSeq; NP_061232.1; NM_018762.1.
DR AlphaFoldDB; O88186; -.
DR SMR; O88186; -.
DR ComplexPortal; CPX-115; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR STRING; 10090.ENSMUSP00000032133; -.
DR GlyCosmos; O88186; 1 site, No reported glycans.
DR GlyGen; O88186; 1 site.
DR PhosphoSitePlus; O88186; -.
DR MaxQB; O88186; -.
DR PaxDb; 10090-ENSMUSP00000032133; -.
DR ProteomicsDB; 267761; -.
DR Antibodypedia; 17356; 538 antibodies from 38 providers.
DR DNASU; 54368; -.
DR Ensembl; ENSMUST00000032133.5; ENSMUSP00000032133.4; ENSMUSG00000030054.5.
DR GeneID; 54368; -.
DR KEGG; mmu:54368; -.
DR UCSC; uc009ctv.1; mouse.
DR AGR; MGI:1860137; -.
DR CTD; 2815; -.
DR MGI; MGI:1860137; Gp9.
DR VEuPathDB; HostDB:ENSMUSG00000030054; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00530000064244; -.
DR HOGENOM; CLU_094615_1_1_1; -.
DR InParanoid; O88186; -.
DR OMA; GYELGSC; -.
DR OrthoDB; 5356136at2759; -.
DR PhylomeDB; O88186; -.
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 BioGRID-ORCS; 54368; 1 hit in 77 CRISPR screens.
DR PRO; PR:O88186; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O88186; Protein.
DR Bgee; ENSMUSG00000030054; Expressed in skin of snout and 49 other cell types or tissues.
DR Genevisible; O88186; MM.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IDA:ComplexPortal.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035855; P:megakaryocyte development; IMP:ComplexPortal.
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; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR22650; GLYCOPROTEIN IB BETA; 1.
DR PANTHER; PTHR22650:SF6; PLATELET GLYCOPROTEIN IX; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Disulfide bond; Glycoprotein; Hemostasis;
KW Leucine-rich repeat; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000250"
FT CHAIN 17..177
FT /note="Platelet glycoprotein IX"
FT /id="PRO_0000378456"
FT TOPO_DOM 17..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..51
FT /note="LRRNT"
FT REPEAT 60..83
FT /note="LRR"
FT DOMAIN 85..137
FT /note="LRRCT"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 177 AA; 19664 MW; EB82B952BD3DD7C4 CRC64;
MTTWGLLFLL WPATTDTQAC PRPCTCQSLE TMGLKVNCEG QGLTALPVIP AHTRQLLLAN
NSLRSVPPGA FDHLPQLWDL DVTHNPWHCD CSLTYLRLWL EDHMPEALMH VYCASPDLAT
RRPLGQLTGY ELGSCGWKLP PSWAYPGVWW DVSLVAVAVL GLILLAGLLN TFTESRN
//
