P05106 · ITB3_HUMAN

  • Protein
    Integrin beta-3
  • Gene
    ITGB3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets (By similarity).
ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099).
ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778).
ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324).
ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677).
ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119).
ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464).
ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430).
ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877).
ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887).
In brain, plays a role in synaptic transmission and plasticity. Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin. Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition (By similarity).
ITGAV:ITGB3 act as a receptor for CD40LG (PubMed:31331973).
ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428).
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Coxsackievirus A9.
(Microbial infection) Acts as a receptor for Hantaan virus.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Cytomegalovirus/HHV-5.
(Microbial infection) Integrin ITGA5:ITGB3 acts as a receptor for Human metapneumovirus.
(Microbial infection) Integrin ITGAV:ITGB3 acts aP05556s a receptor for Human parechovirus 1.
(Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus.
(Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

Miscellaneous

The constitutive activation of ITGAV:ITGB3 on neoplastic cells may contribute to tumor growth and metastatic potential.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site147Mg2+ (UniProtKB | ChEBI); in MIDAS binding site
Binding site149Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site
Binding site149Mg2+ (UniProtKB | ChEBI); in MIDAS binding site
Binding site152Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site
Binding site153Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site
Binding site184Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site241Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site243Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site245Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site246Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site246Mg2+ (UniProtKB | ChEBI); in MIDAS binding site
Binding site277Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and liganded-open conformation
Binding site277Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site
Binding site361Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and unliganded-closed conformation

GO annotations

AspectTerm
Cellular Componentalpha9-beta1 integrin-ADAM8 complex
Cellular Componentalphav-beta3 integrin-HMGB1 complex
Cellular Componentalphav-beta3 integrin-IGF-1-IGF1R complex
Cellular Componentalphav-beta3 integrin-PKCalpha complex
Cellular Componentalphav-beta3 integrin-vitronectin complex
Cellular Componentapical plasma membrane
Cellular Componentcell surface
Cellular Componentcell-cell junction
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular exosome
Cellular Componentfilopodium membrane
Cellular Componentfocal adhesion
Cellular Componentglutamatergic synapse
Cellular Componentglycinergic synapse
Cellular Componentintegrin alphaIIb-beta3 complex
Cellular Componentintegrin alphav-beta3 complex
Cellular Componentintegrin complex
Cellular Componentlamellipodium membrane
Cellular Componentmelanosome
Cellular Componentmicrovillus membrane
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentplasma membrane
Cellular Componentplatelet alpha granule membrane
Cellular Componentpostsynaptic membrane
Cellular Componentprotein-containing complex
Cellular Componentreceptor complex
Cellular Componentruffle membrane
Cellular Componentsynapse
Molecular Functioncell adhesion molecule binding
Molecular Functioncoreceptor activity
Molecular Functionenzyme binding
Molecular Functionextracellular matrix binding
Molecular Functionfibrinogen binding
Molecular Functionfibronectin binding
Molecular Functionidentical protein binding
Molecular Functionintegrin binding
Molecular Functionmetal ion binding
Molecular Functionplatelet-derived growth factor receptor binding
Molecular Functionprotease binding
Molecular Functionprotein disulfide isomerase activity
Molecular Functionprotein kinase C binding
Molecular Functionvascular endothelial growth factor receptor 2 binding
Molecular Functionvirus receptor activity
Biological Processactivation of protein kinase activity
Biological Processangiogenesis involved in wound healing
Biological Processapolipoprotein A-I-mediated signaling pathway
Biological Processapoptotic cell clearance
Biological Processblood coagulation
Biological Processblood coagulation, fibrin clot formation
Biological Processcell adhesion
Biological Processcell adhesion mediated by integrin
Biological Processcell-matrix adhesion
Biological Processcell-substrate adhesion
Biological Processcell-substrate junction assembly
Biological Processcellular response to insulin-like growth factor stimulus
Biological Processcellular response to mechanical stimulus
Biological Processcellular response to platelet-derived growth factor stimulus
Biological Processcellular response to xenobiotic stimulus
Biological Processembryo implantation
Biological Processheterotypic cell-cell adhesion
Biological Processintegrin-mediated signaling pathway
Biological Processmaintenance of postsynaptic specialization structure
Biological Processmesodermal cell differentiation
Biological Processnegative chemotaxis
Biological Processnegative regulation of endothelial cell apoptotic process
Biological Processnegative regulation of lipid storage
Biological Processnegative regulation of lipid transport
Biological Processnegative regulation of lipoprotein metabolic process
Biological Processnegative regulation of low-density lipoprotein receptor activity
Biological Processnegative regulation of macrophage derived foam cell differentiation
Biological Processplatelet activation
Biological Processplatelet aggregation
Biological Processplatelet-derived growth factor receptor signaling pathway
Biological Processpositive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway
Biological Processpositive regulation of angiogenesis
Biological Processpositive regulation of bone resorption
Biological Processpositive regulation of cell adhesion mediated by integrin
Biological Processpositive regulation of cell-matrix adhesion
Biological Processpositive regulation of endothelial cell migration
Biological Processpositive regulation of endothelial cell proliferation
Biological Processpositive regulation of ERK1 and ERK2 cascade
Biological Processpositive regulation of fibroblast migration
Biological Processpositive regulation of fibroblast proliferation
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of glomerular mesangial cell proliferation
Biological Processpositive regulation of osteoblast proliferation
Biological Processpositive regulation of peptidyl-tyrosine phosphorylation
Biological Processpositive regulation of protein phosphorylation
Biological Processpositive regulation of smooth muscle cell migration
Biological Processpositive regulation of smooth muscle cell proliferation
Biological Processpositive regulation of substrate adhesion-dependent cell spreading
Biological Processpositive regulation of T cell migration
Biological Processpositive regulation of vascular endothelial growth factor receptor signaling pathway
Biological Processregulation of actin cytoskeleton organization
Biological Processregulation of bone resorption
Biological Processregulation of extracellular matrix organization
Biological Processregulation of postsynaptic neurotransmitter receptor diffusion trapping
Biological Processregulation of postsynaptic neurotransmitter receptor internalization
Biological Processregulation of protein localization
Biological Processregulation of release of sequestered calcium ion into cytosol
Biological Processregulation of serotonin uptake
Biological Processregulation of trophoblast cell migration
Biological Processresponse to activity
Biological Processsmooth muscle cell migration
Biological Processsubstrate adhesion-dependent cell spreading
Biological Processsymbiont entry into host cell
Biological Processtube development
Biological Processwound healing
Biological Processwound healing, spreading of epidermal cells

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Integrin beta-3
  • Alternative names
    • Platelet membrane glycoprotein IIIa
      (GPIIIa
      )
  • CD Antigen Name
    • CD61

Gene names

    • Name
      ITGB3
    • Synonyms
      GP3A

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P05106
  • Secondary accessions
    • A0PJW2
    • D3DXJ8
    • O15495
    • Q12806
    • Q13413

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain27-718Extracellular
Transmembrane719-741Helical
Topological domain742-788Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Glanzmann thrombasthenia 2 (GT2)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of Glanzmann thrombasthenia, a disorder characterized by failure of platelet aggregation, absent or diminished clot retraction, and mucocutaneous bleeding of mild-to-moderate severity. Glanzmann thrombasthenia has been classified into clinical types I and II. In type I, platelets show absence of glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express glycoprotein IIb-IIIa complexes at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
  • See also
    MIM:619267
Natural variants in GT2
Variant IDPosition(s)ChangeDescription
VAR_06992064C>Yin GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression; dbSNP:rs74554539
VAR_030473119R>Win GT2; dbSNP:rs781062792
VAR_030474141Y>Cin GT2; dbSNP:rs1739770567
VAR_010649143L>Win GT2; dbSNP:rs121918452
VAR_069921144M>Rin GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; dbSNP:rs77963874
VAR_030475145D>Nin GT2; dbSNP:rs121918445
VAR_003998145D>Yin GT2; type B; dbSNP:rs121918445
VAR_030476150M>Vin GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor; dbSNP:rs767548512
VAR_010651188S>Lin GT2; type II; dbSNP:rs143146734
VAR_030478222L>Pin GT2; variant form; dbSNP:rs79208797
VAR_003999240R>Qin GT2; type B; dbSNP:rs121918444
VAR_004000240R>Win GT2; variant Strasbourg-1; dbSNP:rs121918446
VAR_030479242R>Qin GT2; dbSNP:rs377162158
VAR_030480243D>Vin GT2; dbSNP:rs2143097053
VAR_069922247G>Din GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein; dbSNP:rs79560904
VAR_069923279K>Min GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation interupts the interaction of the ITGA2B/ITGB3 complex; dbSNP:rs79775494
VAR_030481288L>Pin GT2
VAR_004001306H>Pin GT2; dbSNP:rs13306476
VAR_030482321M>Lin GT2
VAR_030483330I>Nin GT2; not expressed on the surface and absent inside the transfected cells; dbSNP:rs2143105830
VAR_004002400C>Yin GT2; dbSNP:rs121918449
VAR_030484532C>Yin GT2; dbSNP:rs2065130922
VAR_010671568C>Rin GT2; type I; dbSNP:rs2065157102
VAR_004003586C>Fin GT2; dbSNP:rs2143129874
VAR_030485586C>Rin GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1
VAR_004004598G>Sin GT2
VAR_030486601C>Rin GT2; dbSNP:rs747534508
VAR_010672605G>Sin GT2; type II; dbSNP:rs144884023
VAR_004005778S>Pin GT2; variant Strasbourg-1; dbSNP:rs121918447

Bleeding disorder, platelet-type, 24 (BDPLT24)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal dominant disorder of platelet production characterized by congenital macrothrombocytopenia and platelet anisocytosis. Affected individuals may have no or only mildly increased bleeding tendency.
  • See also
    MIM:619271
Natural variants in BDPLT24
Variant IDPosition(s)ChangeDescription
VAR_081732746missingin BDPLT24; the mutant protein is constitutively active; decreased platelet surface expression; spontaneous FAK phosphosphorylation; abnormal cell shape
VAR_069924749D>Hin BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape; dbSNP:rs398122372

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_00399359in alloantigen HPA-1B; dbSNP:rs5918
Natural variantVAR_06992064in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression; dbSNP:rs74554539
Natural variantVAR_04963366in dbSNP:rs36080296
Natural variantVAR_030473119in GT2; dbSNP:rs781062792
Natural variantVAR_030474141in GT2; dbSNP:rs1739770567
Natural variantVAR_010649143in GT2; dbSNP:rs121918452
Natural variantVAR_069921144in GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; dbSNP:rs77963874
Natural variantVAR_030475145in GT2; dbSNP:rs121918445
Natural variantVAR_003998145in GT2; type B; dbSNP:rs121918445
Natural variantVAR_030476150in GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor; dbSNP:rs767548512
Natural variantVAR_030477166probable risk factor for neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function; dbSNP:rs74708909
Natural variantVAR_003994169in alloantigen HPA-4B; dbSNP:rs5917
Natural variantVAR_010651188in GT2; type II; dbSNP:rs143146734
Natural variantVAR_030478222in GT2; variant form; dbSNP:rs79208797
Natural variantVAR_003999240in GT2; type B; dbSNP:rs121918444
Natural variantVAR_004000240in GT2; variant Strasbourg-1; dbSNP:rs121918446
Natural variantVAR_030479242in GT2; dbSNP:rs377162158
Natural variantVAR_030480243in GT2; dbSNP:rs2143097053
Natural variantVAR_069922247in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation may interfere with correct folding of the protein; dbSNP:rs79560904
Natural variantVAR_069923279in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface; the mutation interupts the interaction of the ITGA2B/ITGB3 complex; dbSNP:rs79775494
Natural variantVAR_030481288in GT2
Natural variantVAR_004001306in GT2; dbSNP:rs13306476
Natural variantVAR_030482321in GT2
Natural variantVAR_030483330in GT2; not expressed on the surface and absent inside the transfected cells; dbSNP:rs2143105830
Natural variantVAR_004002400in GT2; dbSNP:rs121918449
Natural variantVAR_003995433in alloantigen MO+; in a case of neonatal alloimmune thrombocytopenia; dbSNP:rs121918448
Natural variantVAR_014178453in dbSNP:rs5921
Mutagenesis502-508Increases ligand-binding activity.
Natural variantVAR_003996515in alloantigen CA+/TU+; dbSNP:rs13306487
Natural variantVAR_030484532in GT2; dbSNP:rs2065130922
Natural variantVAR_010671568in GT2; type I; dbSNP:rs2065157102
Natural variantVAR_004003586in GT2; dbSNP:rs2143129874
Natural variantVAR_030485586in GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1
Natural variantVAR_004004598in GT2
Natural variantVAR_030486601in GT2; dbSNP:rs747534508
Natural variantVAR_010672605in GT2; type II; dbSNP:rs144884023
Mutagenesis659Slight increase in ligand-binding activity; when associated with 698-D--K-702 del.
Natural variantVAR_003997662in alloantigen SR(A); dbSNP:rs151219882
Mutagenesis698-702Slight increase in ligand-binding activity; when associated with A-659.
Natural variantVAR_081732746in BDPLT24; the mutant protein is constitutively active; decreased platelet surface expression; spontaneous FAK phosphosphorylation; abnormal cell shape
Natural variantVAR_069924749in BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape; dbSNP:rs398122372
Mutagenesis773No effect on cell surface location but impairs interaction with TNS3 and PEAK1.
Natural variantVAR_004005778in GT2; variant Strasbourg-1; dbSNP:rs121918447
Mutagenesis785No effect on cell surface location but impairs interaction with TNS3 and PEAK1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 907 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
Signal1-26UniProt
ChainPRO_000001634427-788UniProtIntegrin beta-3
Disulfide bond31↔49UniProt
Disulfide bond39↔461UniProt
Disulfide bond42↔64UniProt
Disulfide bond52↔75UniProt
Glycosylation125UniProtN-linked (GlcNAc...) asparagine
Disulfide bond203↔210UniProt
Modified residue (large scale data)221PRIDEPhosphothreonine
Disulfide bond258↔299UniProt
Glycosylation346UniProtN-linked (GlcNAc...) asparagine
Glycosylation397UniProtN-linked (GlcNAc...) asparagine
Disulfide bond400↔412UniProt
Disulfide bond432↔459UniProt
Disulfide bond463↔483UniProt
Disulfide bond474↔486UniProt
Glycosylation478UniProtN-linked (GlcNAc...) asparagine
Disulfide bond488↔497UniProt
Disulfide bond499↔529UniProt
Disulfide bond512↔527UniProt
Disulfide bond521↔532UniProt
Disulfide bond534↔547UniProt
Disulfide bond549↔570UniProt
Disulfide bond554↔568UniProt
Disulfide bond562↔573UniProt
Disulfide bond575↔584UniProt
Glycosylation585UniProtN-linked (GlcNAc...) asparagine
Disulfide bond586↔609UniProt
Disulfide bond593↔607UniProt
Disulfide bond601↔612UniProt
Disulfide bond614↔624UniProt
Disulfide bond627↔630UniProt
Disulfide bond634↔681UniProt
Disulfide bond640↔661UniProt
Disulfide bond643↔657UniProt
Glycosylation680UniProtN-linked (GlcNAc...) asparagine
Disulfide bond689↔713UniProt
Modified residue767UniProtPhosphothreonine
Modified residue (large scale data)767PRIDEPhosphothreonine
Modified residue773UniProtPhosphotyrosine
Modified residue (large scale data)773PRIDEPhosphotyrosine
Modified residue (large scale data)777PRIDEPhosphothreonine
Modified residue (large scale data)778PRIDEPhosphoserine
Modified residue779UniProtPhosphothreonine; by PDPK1 and PKB/AKT1; in vitro
Modified residue (large scale data)779PRIDEPhosphothreonine
Modified residue (large scale data)781PRIDEPhosphothreonine
Modified residue (large scale data)784PRIDEPhosphothreonine
Modified residue785UniProtPhosphotyrosine
Modified residue (large scale data)785PRIDEPhosphotyrosine
Modified residue (large scale data)788PRIDEPhosphothreonine

Post-translational modification

Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. A peptide (AA 740-762) is capable of binding GRB2 only when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation of Thr-779 inhibits SHC binding.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Isoform beta-3A and isoform beta-3C are widely expressed. Isoform beta-3A is specifically expressed in osteoblast cells; isoform beta-3C is specifically expressed in prostate and testis.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Heterodimer of an alpha and a beta subunit. Beta-3 (ITGB3) associates with either alpha-IIb (ITGA2B) or alpha-V (ITGAV). Isoform Beta-3C interacts with FLNB. Interacts with COMP. Interacts with PDIA6 following platelet stimulation. Interacts with SYK; upon activation by ITGB3 promotes platelet adhesion. Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2. Interacts with EMP2; regulates the levels of the heterodimer ITGA5:ITGB3 integrin expression on the plasma membrane (PubMed:16216233).
Integrin ITGAV:ITGB3 interacts with FBLN5 (via N-terminus) (By similarity).
ITGAV:ITGB3 interacts with CCN3 (PubMed:12695522).
ITGAV:ITGB3 and ITGA2B:ITGB3 interact with SELP (via C-type lectin domain); the interaction mediates cell-cell interaction and adhesion (PubMed:37184585).
ITGAV:ITGB3 is found in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415).
ITGAV:ITGB3 is found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778).
ITGAV:ITGB3 is found in a ternary complex with FGF1 and FGFR1 (PubMed:18441324).
ITGAV:ITGB3 interacts with FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors (PubMed:28302677).
ITGAV:ITGB3 binds to IL1B (PubMed:29030430).
ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (PubMed:19578119).
ITGAV:ITGB3 interacts with IGF2 (PubMed:28873464).
ITGAV:ITGB3 interacts with FBN1 (PubMed:12807887).
ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second extracellular domain) (PubMed:27993971).
Interacts (via the allosteric site (site 2)) with CXCL12 in a CXCR4-independent manner (PubMed:29301984).
Interacts with MXRA8/DICAM; the interaction inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581).
ITGAV:ITGB3 interacts with PTN (PubMed:19141530).
Forms a complex with PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3 Tyr-773 phosphorylation (PubMed:19141530).
ITGAV:ITGB3 interacts with SLC6A4. Interacts with SLC6A4 (via C-terminus); this interaction regulates SLC6A4 trafficking (By similarity).
ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction is ROS and PPIase activity-dependent and is increased in the presence of thrombin (By similarity).
Interacts with tensin TNS3; TNS3 also interacts with PEAK1, thus acting as an adapter molecule to bridge the association of PEAK1 with ITGB3 (PubMed:35687021).
(Microbial infection) Integrin ITGAV:ITGB3 interacts with herpes virus 8/HHV-8 glycoprotein B.
(Microbial infection) Integrin ITGAV:ITGB3 interacts with coxsackievirus A9 capsid proteins.
(Microbial infection) Interacts with Hantaan virus glycoprotein G.
(Microbial infection) Integrin ITGAV:ITGB3 interacts with cytomegalovirus/HHV-5 gH:gL proteins.
(Microbial infection) Integrin ITGA5:ITGB3 interacts with human metapneumovirus fusion protein.
(Microbial infection) Integrin ITGAV:ITGB3 interacts with human parechovirus 1 capsid proteins.
(Microbial infection) Integrin ITGAV:ITGB3 interacts with west nile virus envelope protein E.
(Microbial infection) Interacts with HIV-1 Tat (PubMed:10397733).
ITGAV:ITGB3 interacts with AGRA2 (PubMed:16982628).

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for domain, region, motif.

TypeIDPosition(s)Description
Domain30-76PSI
Domain135-377VWFA
Region203-210Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding
Region293-313CX3CL1-binding
Domain436-498EGF-like 1
Domain499-548EGF-like 2
Domain549-585EGF-like 3
Domain586-629EGF-like 4
Motif777-783LIR

Domain

The VWFA domain (or beta I domain) contains three cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS). This domain is also part of the ligand-binding site.

Sequence similarities

Belongs to the integrin beta chain family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 3 isoforms produced by Alternative splicing.

P05106-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Beta-3A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    788
  • Mass (Da)
    87,058
  • Last updated
    2007-02-06 v2
  • Checksum
    F246623608E05F9E
MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT

P05106-2

  • Name
    Beta-3B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 768-788: ANNPLYKEATSTFTNITYRGT → VRDGAGRFLKSLV

P05106-3

  • Name
    Beta-3C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 768-788: ANNPLYKEATSTFTNITYRGT → HYAQSLRKWNQPVSIDG

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q16157Q16157_HUMANITGB335
I3L4X8I3L4X8_HUMANITGB3443

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict12in Ref. 1; AAA52589 and 3; AAA35927
Sequence conflict151in Ref. 11; AAA67537 and 14; AAB23689
Sequence conflict205in Ref. 11; AAA67537
Sequence conflict649-653in Ref. 1; AAA52589, 2; AAA60122 and 4; AAB71380
Sequence conflict716in Ref. 8
Sequence conflict737-741in Ref. 11; AAA67537
Alternative sequenceVSP_002745768-788in isoform Beta-3B
Alternative sequenceVSP_002746768-788in isoform Beta-3C

Polymorphism

Position 59 is associated with platelet-specific alloantigen HPA-1 (ZW or PL(A)). HPA-1A/ZW(A)/PL(A1) has Leu-59 and HPA-1B/ZW(B)/PL(A2) has Pro-59. HPA-1A is involved in fetal-maternal alloimmune thromobocytopenia (FMAIT) as well as in neonatal alloimmune thrombocytopenia (NAIT).
Position 169 is associated with platelet-specific alloantigen HPA-4 (PEN or YUK). HPA-4A/PEN(A)/YUK(A) has Arg-169 and HPA-4B/PEN(B)/YUK(B) has Gln-169. HPA-4B is involved in neonatal alloimmune thrombocytopenia (NAIT or NATP).
Position 433 is associated with platelet-specific alloantigen MO. MO- has Pro-433 and MO+ has Ala-433. MO+ is involved in NAIT.
Position 515 is associated with platelet-specific alloantigen CA/TU. CA-/TU- has Arg-515 and CA+/TU+ has Gln-515. CA+ is involved in NAIT.
Position 662 is associated with platelet-specific alloantigen SR(A). SR(A)- has Arg-662 and SR(A)+ has Cys-662.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J02703
EMBL· GenBank· DDBJ
AAA52589.1
EMBL· GenBank· DDBJ
mRNA
M20311
EMBL· GenBank· DDBJ
AAA60122.1
EMBL· GenBank· DDBJ
mRNA
M35999
EMBL· GenBank· DDBJ
AAA35927.1
EMBL· GenBank· DDBJ
mRNA
U95204
EMBL· GenBank· DDBJ
AAB71380.1
EMBL· GenBank· DDBJ
mRNA
CH471231
EMBL· GenBank· DDBJ
EAW57682.1
EMBL· GenBank· DDBJ
Genomic DNA
BC127666
EMBL· GenBank· DDBJ
AAI27667.1
EMBL· GenBank· DDBJ
mRNA
BC127667
EMBL· GenBank· DDBJ
AAI27668.1
EMBL· GenBank· DDBJ
mRNA
L28832
EMBL· GenBank· DDBJ
AAA20880.2
EMBL· GenBank· DDBJ
Genomic DNA
M32686
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32667
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32672
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32673
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32674
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32675
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32680
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32681
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32682
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M32685
EMBL· GenBank· DDBJ
AAA67537.1
EMBL· GenBank· DDBJ
Genomic DNA
M57494
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57481
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57482
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57483
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57484
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57485
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57486
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57487
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57488
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57489
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57490
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57491
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57492
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
M57493
EMBL· GenBank· DDBJ
AAA52600.1
EMBL· GenBank· DDBJ
Genomic DNA
U03881
EMBL· GenBank· DDBJ
AAA16076.1
EMBL· GenBank· DDBJ
Genomic DNA
S49379
EMBL· GenBank· DDBJ
AAB23689.2
EMBL· GenBank· DDBJ
Genomic DNA
M25108
EMBL· GenBank· DDBJ
AAA36121.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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