GP1BB_RAT
ID GP1BB_RAT Reviewed; 206 AA.
AC Q9JJM7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 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 [MRNA].
RC STRAIN=Wistar; TISSUE=Brain cortex;
RX PubMed=10873671; DOI=10.1006/bbrc.2000.3003;
RA Tada S., Kajii Y., Sato M., Nishikawa T.;
RT "Reciprocal expression of infant- and adult preferring transcripts of
RT CDCrel-1 septin in the rat neocortex.";
RL Biochem. Biophys. Res. Commun. 273:723-728(2000).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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.
CC {ECO:0000250}.
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DR EMBL; AB027146; BAA98053.1; -; mRNA.
DR RefSeq; NP_446382.1; NM_053930.4.
DR AlphaFoldDB; Q9JJM7; -.
DR SMR; Q9JJM7; -.
DR BioGRID; 250594; 1.
DR STRING; 10116.ENSRNOP00000043041; -.
DR iPTMnet; Q9JJM7; -.
DR PhosphoSitePlus; Q9JJM7; -.
DR PaxDb; Q9JJM7; -.
DR PRIDE; Q9JJM7; -.
DR Ensembl; ENSRNOT00000040954; ENSRNOP00000043041; ENSRNOG00000046981.
DR GeneID; 116727; -.
DR KEGG; rno:116727; -.
DR CTD; 2812; -.
DR RGD; 621050; Gp1bb.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00530000064244; -.
DR HOGENOM; CLU_094615_0_0_1; -.
DR InParanoid; Q9JJM7; -.
DR OMA; HLQGRII; -.
DR OrthoDB; 1229279at2759; -.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
DR Reactome; R-RNO-76009; Platelet Aggregation (Plug Formation).
DR PRO; PR:Q9JJM7; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000046981; Expressed in spleen and 4 other tissues.
DR Genevisible; Q9JJM7; RN.
DR GO; GO:1990779; C:glycoprotein Ib-IX-V complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035855; P:megakaryocyte development; 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; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Cell adhesion; Disulfide bond; 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_0000326528"
FT TOPO_DOM 27..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..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:0000250|UniProtKB:P56400"
FT MOD_RES 191
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P13224"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13224"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56400"
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; 22175 MW; 38ECE6E99DEF22B8 CRC64;
MGSRPRGALS LLLLLLAPPS RPASGCPAPC RCSETRVDCG RRGLTWASLP AAFPPDTTEL
VLTDNNLTAL PPGLLDTLPA LRRVHLGANP WRCDCRLLPL RAWLAGRPER EFYRDLRCVA
PLALRGRLLP YVAEDELRAA CAPGLLCWGA LVAQLALLVL GLLHALLLAL LLSRLRRLRA
QARARSTREF SLTAPLVAES AGGGAS
