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Protein

Platelet glycoprotein Ib beta chain

Gene

Gp1bb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.By similarity

Miscellaneous

Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-binding protein.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processBlood coagulation, Cell adhesion, Hemostasis

Enzyme and pathway databases

ReactomeiR-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-RNO-430116. GP1b-IX-V activation signalling.
R-RNO-75892. Platelet Adhesion to exposed collagen.
R-RNO-76009. Platelet Aggregation (Plug Formation).

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet glycoprotein Ib beta chain
Short name:
GP-Ib beta
Short name:
GPIb-beta
Short name:
GPIbB
Alternative name(s):
CD_antigen: CD42c
Gene namesi
Name:Gp1bb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi621050. Gp1bb.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 150ExtracellularSequence analysisAdd BLAST124
Transmembranei151 – 171HelicalSequence analysisAdd BLAST21
Topological domaini172 – 206CytoplasmicSequence analysisAdd BLAST35

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26By similarityAdd BLAST26
ChainiPRO_000032652827 – 206Platelet glycoprotein Ib beta chainAdd BLAST180

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 32By similarity
Disulfide bondi30 ↔ 39By similarity
Disulfide bondi93 ↔ 118By similarity
Disulfide bondi95 ↔ 141By similarity
Disulfide bondi147Interchain (with C-608 or C-609 in GP1BA)By similarity
Modified residuei186PhosphoserineBy similarity1
Modified residuei191Phosphoserine; by PKABy similarity1
Modified residuei193PhosphothreonineBy similarity1
Modified residuei200PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9JJM7.
PRIDEiQ9JJM7.

PTM databases

iPTMnetiQ9JJM7.
PhosphoSitePlusiQ9JJM7.

Expressioni

Gene expression databases

BgeeiENSRNOG00000046981.
GenevisibleiQ9JJM7. RN.

Interactioni

Subunit structurei

Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250594. 1 interactor.
STRINGi10116.ENSRNOP00000043041.

Structurei

3D structure databases

ProteinModelPortaliQ9JJM7.
SMRiQ9JJM7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 55LRRNTAdd BLAST29
Repeati60 – 83LRRAdd BLAST24
Domaini89 – 143LRRCTAdd BLAST55

Keywords - Domaini

Leucine-rich repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00530000064244.
HOGENOMiHOG000060136.
HOVERGENiHBG051791.
InParanoidiQ9JJM7.
KOiK06262.
OMAiYRDLRCA.
OrthoDBiEOG091G0XGH.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiView protein in InterPro
IPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR000372. LRRNT.
PfamiView protein in Pfam
PF01462. LRRNT. 1 hit.
SMARTiView protein in SMART
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SUPFAMiSSF52058. SSF52058. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JJM7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSRPRGALS LLLLLLAPPS RPASGCPAPC RCSETRVDCG RRGLTWASLP
60 70 80 90 100
AAFPPDTTEL VLTDNNLTAL PPGLLDTLPA LRRVHLGANP WRCDCRLLPL
110 120 130 140 150
RAWLAGRPER EFYRDLRCVA PLALRGRLLP YVAEDELRAA CAPGLLCWGA
160 170 180 190 200
LVAQLALLVL GLLHALLLAL LLSRLRRLRA QARARSTREF SLTAPLVAES

AGGGAS
Length:206
Mass (Da):22,175
Last modified:October 1, 2000 - v1
Checksum:i38ECE6E99DEF22B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027146 mRNA. Translation: BAA98053.1.
RefSeqiNP_446382.1. NM_053930.4.
UniGeneiRn.96497.

Genome annotation databases

EnsembliENSRNOT00000040954; ENSRNOP00000043041; ENSRNOG00000046981.
GeneIDi116727.
KEGGirno:116727.

Similar proteinsi

Entry informationi

Entry nameiGP1BB_RAT
AccessioniPrimary (citable) accession number: Q9JJM7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: October 1, 2000
Last modified: August 30, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome