GP1BB_MOUSE
ID GP1BB_MOUSE Reviewed; 206 AA.
AC P56400;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Platelet glycoprotein Ib beta chain;
DE Short=GP-Ib beta;
DE Short=GPIb-beta;
DE Short=GPIbB;
DE AltName: CD_antigen=CD42c;
DE Flags: Precursor;
GN Name=Gp1bb;
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].
RX PubMed=9259114; DOI=10.1016/s0049-3848(97)00123-0;
RA Kitaguchi T., Murata M., Anbo H., Moriki T., Ikeda Y.;
RT "Characterization of the gene encoding mouse platelet glycoprotein Ib
RT beta.";
RL Thromb. Res. 87:235-244(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-191; THR-193 AND
RP SER-200, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC 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: Gp-Ib, a surface membrane protein of platelets, participates
CC in the formation of platelet plugs by binding to von Willebrand factor,
CC which is already bound to the subendothelium. {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.
CC Interacts with TRAF4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- MISCELLANEOUS: Platelet activation apparently involves disruption of
CC the macromolecular complex of GP-Ib with the platelet glycoprotein IX
CC (GP-IX) and dissociation of GP-Ib from the actin-binding protein.
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DR EMBL; AB001419; BAA22424.1; -; Genomic_DNA.
DR CCDS; CCDS49787.1; -.
DR RefSeq; NP_034457.1; NM_010327.2.
DR AlphaFoldDB; P56400; -.
DR SMR; P56400; -.
DR BioGRID; 200004; 1.
DR ComplexPortal; CPX-115; Glycoprotein Ib-IX-V complex.
DR ComplexPortal; CPX-118; Glycoprotein Ib-IX-V-Filamin-A complex.
DR STRING; 10090.ENSMUSP00000059270; -.
DR GlyGen; P56400; 1 site.
DR iPTMnet; P56400; -.
DR PhosphoSitePlus; P56400; -.
DR MaxQB; P56400; -.
DR PaxDb; P56400; -.
DR PRIDE; P56400; -.
DR ProteomicsDB; 271259; -.
DR Antibodypedia; 44871; 148 antibodies from 28 providers.
DR Ensembl; ENSMUST00000167388; ENSMUSP00000126292; ENSMUSG00000050761.
DR GeneID; 14724; -.
DR KEGG; mmu:14724; -.
DR UCSC; uc007yoi.1; mouse.
DR CTD; 2812; -.
DR MGI; MGI:107852; Gp1bb.
DR VEuPathDB; HostDB:ENSMUSG00000050761; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00530000064244; -.
DR HOGENOM; CLU_094615_0_0_1; -.
DR InParanoid; P56400; -.
DR PhylomeDB; P56400; -.
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; 14724; 5 hits in 74 CRISPR screens.
DR PRO; PR:P56400; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P56400; protein.
DR Bgee; ENSMUSG00000050761; Expressed in ileum and 58 other tissues.
DR ExpressionAtlas; P56400; baseline.
DR Genevisible; P56400; MM.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0042802; F:identical protein binding; 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; ISS:MGI.
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; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Disulfide bond; Glycoprotein; Hemostasis;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..206
FT /note="Platelet glycoprotein Ib beta chain"
FT /id="PRO_0000021346"
FT TOPO_DOM 27..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..55
FT /note="LRRNT"
FT REPEAT 60..83
FT /note="LRR"
FT DOMAIN 89..143
FT /note="LRRCT"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..32
FT /evidence="ECO:0000250"
FT DISULFID 30..39
FT /evidence="ECO:0000250"
FT DISULFID 93..118
FT /evidence="ECO:0000250"
FT DISULFID 95..141
FT /evidence="ECO:0000250"
FT DISULFID 147
FT /note="Interchain (with C-608 or C-609 in GP1BA)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 21763 MW; AC4BCB4DFA226F1D CRC64;
MGSRPRGALS LLLLLLALLS RPASGCPAPC SCAGTLVDCG RRGLTWASLP AAFPPDTTEL
VLTGNNLTAL PPGLLDALPA LRAAHLGANP WRCDCRLLPL RAWLAGRPER APYRDLRCVA
PPALRGRLLP YVAEDELRAA CAPGLLCWGA LVAQLALLVL GLLHALLLAL LLGRLRRLRA
RARARSIQEF SLTAPLVAES ARGGAS
