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Protein

Platelet glycoprotein Ib alpha chain

Gene

Gp1ba

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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 the A1 domain of vWF, which is already bound to the subendothelium.By similarity

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: MGI
  • cell adhesion Source: MGI
  • cell morphogenesis Source: MGI
  • cytokine-mediated signaling pathway Source: GO_Central
  • fibrinolysis Source: MGI
  • hemostasis Source: MGI
  • negative regulation of JAK-STAT cascade Source: GO_Central
  • negative regulation of protein kinase activity Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Cell adhesion, Hemostasis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet glycoprotein Ib alpha chain
Short name:
GP-Ib alpha
Short name:
GPIb-alpha
Short name:
GPIbA
Short name:
Glycoprotein Ibalpha
Alternative name(s):
CD_antigen: CD42b
Gene namesi
Name:Gp1ba
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1333744. Gp1ba.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 612596ExtracellularSequence analysisAdd
BLAST
Transmembranei613 – 63321HelicalSequence analysisAdd
BLAST
Topological domaini634 – 734101CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Add
BLAST
Chaini17 – 734718Platelet glycoprotein Ib alpha chainPRO_0000271749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi20 ↔ 33By similarity
Disulfide bondi225 ↔ 264By similarity
Disulfide bondi227 ↔ 280By similarity
Modified residuei292 – 2921SulfotyrosineBy similarity
Disulfide bondi608 – 608Interchain (with C-147 in GP1BB)By similarity
Disulfide bondi609 – 609Interchain (with C-147 in GP1BB)By similarity
Modified residuei711 – 7111PhosphoserineBy similarity
Modified residuei714 – 7141PhosphoserineBy similarity

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiO35930.
PaxDbiO35930.
PRIDEiO35930.

PTM databases

iPTMnetiO35930.
PhosphoSiteiO35930.

Miscellaneous databases

PMAP-CutDBO35930.

Expressioni

Gene expression databases

BgeeiENSMUSG00000050675.
CleanExiMM_GP1BA.
ExpressionAtlasiO35930. baseline and differential.
GenevisibleiO35930. MM.

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. Interacts with FLNB. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057563.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K15model-A52-216[»]
ProteinModelPortaliO35930.
SMRiO35930. Positions 20-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 4731LRRNTAdd
BLAST
Repeati48 – 6922LRR 1Add
BLAST
Repeati72 – 9322LRR 2Add
BLAST
Repeati94 – 11522LRR 3Add
BLAST
Repeati117 – 14024LRR 4Add
BLAST
Repeati141 – 16222LRR 5Add
BLAST
Repeati165 – 18824LRR 6Add
BLAST
Repeati189 – 21022LRR 7Add
BLAST
Domaini221 – 28262LRRCTAdd
BLAST

Sequence similaritiesi

Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129945.
HOGENOMiHOG000234361.
HOVERGENiHBG051790.
InParanoidiO35930.
KOiK06261.
OMAiVHSPPVS.
OrthoDBiEOG091G08IS.
PhylomeDBiO35930.
TreeFamiTF351114.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 6 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O35930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLILLFLL PSPLHSQHTC SISKVTSLLE VNCENKKLTA LPADLPADTG
60 70 80 90 100
ILHLGENQLG TFSTASLVHF THLTYLYLDR CELTSLQTNG KLIKLENLDL
110 120 130 140 150
SHNNLKSLPS LGWALPALTT LDVSFNKLGS LSPGVLDGLS QLQELYLQNN
160 170 180 190 200
DLKSLPPGLL LPTTKLKKLN LANNKLRELP SGLLDGLEDL DTLYLQRNWL
210 220 230 240 250
RTIPKGFFGT LLLPFVFLHA NSWYCDCEIL YFRHWLQENA NNVYLWKQGV
260 270 280 290 300
DVKDTTPNVA SVRCANLDNA PVYSYPGKGC PTSSGDTDYD DYDDIPDVPA
310 320 330 340 350
TRTEVKFSTN TKVHTTHWSL LAAAPSTSQD SQMISLPPTH KPTKKQSTFI
360 370 380 390 400
HTQSPGFTTL PETMESNPTF YSLKLNTVLI PSPTTLEPTS TQATPEPNIQ
410 420 430 440 450
PMLTTSTLTT PEHSTTPVPT TTILTTPEHS TIPVPTTAIL TTPKPSTIPV
460 470 480 490 500
PTTATLTTLE PSTTPVPTTA TLTTPEPSTT LVPTTATLTT PEHSTTPVPT
510 520 530 540 550
TATLTTPEHS TTPVPTTATL TTPEPSTTLT NLVSTISPVL TTTLTTPEST
560 570 580 590 600
PIETILEQFF TTELTLLPTL ESTTTIIPEQ NSFLNLPEVA LVSSDTSESS
610 620 630 640 650
PFLNSDFCCF LPLGFYVLGL LWLLFASVVL ILLLTWTWHV TPHSLDMEQS
660 670 680 690 700
AALATSTHTT SLEVQRARQV TMPRAWLLFL QGSLPTFRSS LFLWVRPNGR
710 720 730
VGPLVAGRRP SALSQGRGQD LLGTVGIRYS GHSL
Length:734
Mass (Da):80,055
Last modified:January 9, 2007 - v2
Checksum:iFA42553EC2ED4D0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti532 – 5321L → V in AAC53320 (PubMed:9410473).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91967 Genomic DNA. Translation: AAC53320.1.
AL596117 Genomic DNA. Translation: CAI25162.1.
CCDSiCCDS24957.1.
RefSeqiNP_034456.2. NM_010326.2.
XP_006532295.1. XM_006532232.2.
XP_006537194.1. XM_006537131.2.
UniGeneiMm.377085.

Genome annotation databases

EnsembliENSMUST00000055184; ENSMUSP00000057563; ENSMUSG00000050675.
ENSMUST00000108551; ENSMUSP00000104191; ENSMUSG00000050675.
GeneIDi14723.
KEGGimmu:14723.
UCSCiuc007jvq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91967 Genomic DNA. Translation: AAC53320.1.
AL596117 Genomic DNA. Translation: CAI25162.1.
CCDSiCCDS24957.1.
RefSeqiNP_034456.2. NM_010326.2.
XP_006532295.1. XM_006532232.2.
XP_006537194.1. XM_006537131.2.
UniGeneiMm.377085.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K15model-A52-216[»]
ProteinModelPortaliO35930.
SMRiO35930. Positions 20-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057563.

PTM databases

iPTMnetiO35930.
PhosphoSiteiO35930.

Proteomic databases

MaxQBiO35930.
PaxDbiO35930.
PRIDEiO35930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055184; ENSMUSP00000057563; ENSMUSG00000050675.
ENSMUST00000108551; ENSMUSP00000104191; ENSMUSG00000050675.
GeneIDi14723.
KEGGimmu:14723.
UCSCiuc007jvq.1. mouse.

Organism-specific databases

CTDi2811.
MGIiMGI:1333744. Gp1ba.

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00840000129945.
HOGENOMiHOG000234361.
HOVERGENiHBG051790.
InParanoidiO35930.
KOiK06261.
OMAiVHSPPVS.
OrthoDBiEOG091G08IS.
PhylomeDBiO35930.
TreeFamiTF351114.

Enzyme and pathway databases

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

Miscellaneous databases

PMAP-CutDBO35930.
PROiO35930.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000050675.
CleanExiMM_GP1BA.
ExpressionAtlasiO35930. baseline and differential.
GenevisibleiO35930. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 6 hits.
SM00082. LRRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGP1BA_MOUSE
AccessioniPrimary (citable) accession number: O35930
Secondary accession number(s): Q5SX47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: September 7, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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
Binding sites for vWF and thrombin (the latter site with unknown function) are in the N-terminal part of the molecule.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.