ITGB3
entrez
3690
canonical
uniprot
P05106
canonical
ensembl
ENSG00000259207
resolver
ensp
ENSP00000452786
resolver
genesymbol
ITGB3
resolver
genesymbol_syn
GP3A
resolver
hgnc
HGNC:6156
resolver
uniprot
A0PJW2
resolver
uniprot
D3DXJ8
resolver
uniprot
O15495
resolver
uniprot
Q12806
resolver
uniprot
Q13413
resolver
uniprot
Q14648
resolver
uniprot
Q16499
resolver
uniprot_entry
ITB3_HUMAN
resolver
uniprot_sec
A0PJW2
resolver
uniprot_sec
D3DXJ8
resolver
uniprot_sec
O15495
resolver
uniprot_sec
Q12806
resolver
uniprot_sec
Q13413
resolver
uniprot_sec
Q14648
resolver
uniprot_sec
Q16499
resolver
amino_acid_sequence
MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT
uniprot
proteins
disease_involvement
DISEASE: Fetomaternal alloimmune thrombocytopenia 1 (FMAIT1) [MIM:621264]: A form of fetomaternal alloimmune thrombocytopenia, a bleeding disorder caused by maternal/fetal incompatibility for platelet alloantigens and arising when a fetus inherits a paternal platelet alloantigen that the mother does not possess. During pregnancy, as well as parturition, maternal alloantibodies against paternally-inherited platelet antigens cause destruction of fetal platelets and fetal/neonatal thrombocytopenia. Disease severity and clinical features in the fetus or neonate are heterogeneous. While most fetuses remain asymptomatic, others develop skin bleedings (petechiae) or internal organ bleedings. The most severe symptom is intracranial hemorrhage that is mostly discovered postnatally and can result in neurological complications or even death. Mothers with circulating platelet alloantibodies may experience miscarriage. FMAIT1 transmission pattern is consistent with autosomal dominant paternal inheritance. {ECO:0000269|PubMed:12036875, ECO:0000269|PubMed:1430225, ECO:0000269|PubMed:19821948, ECO:0000269|PubMed:22116617, ECO:0000269|PubMed:25494608, ECO:0000269|PubMed:2565345, ECO:0000269|PubMed:28518345, ECO:0000269|PubMed:31859394, ECO:0000269|PubMed:33724573, ECO:0000269|PubMed:3798869, ECO:0000269|PubMed:7694683, ECO:0000269|PubMed:8093349}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Glanzmann thrombasthenia 2 (GT2) [MIM:619267]: 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. {ECO:0000269|PubMed:10233432, ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046, ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082, ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206, ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267, ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006, ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682, ECO:0000269|PubMed:29084015, ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749, ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783, ECO:0000269|PubMed:9790984}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bleeding disorder, platelet-type, 24 (BDPLT24) [MIM:619271]: 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. {ECO:0000269|PubMed:18065693, ECO:0000269|PubMed:29380037}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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 (VWF). 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 (By similarity). Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen (PubMed:9111081). 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). Integrin ITGA2B:ITGB3 is also the receptor of the erythrocyte-specific ICAM4 ligand involved in heterotypic cell-cell adhesion between erythrocytes and activated platelets (PubMed:12477717). ITGAV:ITGB3 acts as a receptor for SNED1 and mediates R-G-D-dependent cell adhesion to SNED1 (PubMed:39713860). {ECO:0000250|UniProtKB:O54890, ECO:0000269|PubMed:10640428, ECO:0000269|PubMed:12477717, ECO:0000269|PubMed:12807887, ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:18635536, ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099, ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:28873464, ECO:0000269|PubMed:29030430, ECO:0000269|PubMed:31331973, ECO:0000269|PubMed:39713860, ECO:0000269|PubMed:9111081, ECO:0000269|PubMed:9195946, ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Herpes virus 8/HHV-8. {ECO:0000269|PubMed:18045938}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Coxsackievirus A9. {ECO:0000269|PubMed:7519807}.; FUNCTION: (Microbial infection) Acts as a receptor for Hantaan virus. {ECO:0000269|PubMed:9618541}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for Cytomegalovirus/HHV-5. {ECO:0000269|PubMed:15834425}.; FUNCTION: (Microbial infection) Integrin ITGA5:ITGB3 acts as a receptor for Human metapneumovirus. {ECO:0000269|PubMed:24478423}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts aP05556s a receptor for Human parechovirus 1. {ECO:0000269|PubMed:11160695}.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a receptor for West nile virus. {ECO:0000269|PubMed:23658209}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. {ECO:0000269|PubMed:10397733}.
uniprot
proteins
mass_dalton
87058
uniprot
proteins
mutagenesis
MUTAGEN 502..508; /note="Missing: Increases ligand-binding activity."; /evidence="ECO:0000269|PubMed:19704023"; MUTAGEN 659; /note="R->A: Slight increase in ligand-binding activity; when associated with 698-D--K-702 del."; /evidence="ECO:0000269|PubMed:19704023"; MUTAGEN 698..702; /note="Missing: Slight increase in ligand-binding activity; when associated with A-659."; /evidence="ECO:0000269|PubMed:19704023"; MUTAGEN 773; /note="Y->A: No effect on cell surface location but impairs interaction with TNS3 and PEAK1."; /evidence="ECO:0000269|PubMed:35687021"; MUTAGEN 785; /note="Y->A: No effect on cell surface location but impairs interaction with TNS3 and PEAK1."; /evidence="ECO:0000269|PubMed:35687021
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:10896934}.
uniprot
proteins
protein_family
Integrin beta chain family
uniprot
proteins
pubmed
10233432
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10397733
uniprot
proteins
pubmed
10640428
uniprot
proteins
pubmed
10896934
uniprot
proteins
pubmed
11160695
uniprot
proteins
pubmed
11546839
uniprot
proteins
pubmed
11588040
uniprot
proteins
pubmed
11807098
uniprot
proteins
pubmed
11897046
uniprot
proteins
pubmed
11940607
uniprot
proteins
pubmed
12036875
uniprot
proteins
pubmed
12083483
uniprot
proteins
pubmed
12353082
uniprot
proteins
pubmed
12477717
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12695522
uniprot
proteins
pubmed
12807887
uniprot
proteins
pubmed
1371279
uniprot
proteins
pubmed
1382574
uniprot
proteins
pubmed
1430225
uniprot
proteins
pubmed
1438206
uniprot
proteins
pubmed
15156152
uniprot
proteins
pubmed
15378069
uniprot
proteins
pubmed
15466936
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15583747
uniprot
proteins
pubmed
15634267
uniprot
proteins
pubmed
15748237
uniprot
proteins
pubmed
15834425
uniprot
proteins
pubmed
1602006
uniprot
proteins
pubmed
16051604
uniprot
proteins
pubmed
16216233
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16322781
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16982628
uniprot
proteins
pubmed
17583734
uniprot
proteins
pubmed
17635696
uniprot
proteins
pubmed
18045938
uniprot
proteins
pubmed
18065693
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18317590
uniprot
proteins
pubmed
18441324
uniprot
proteins
pubmed
18635536
uniprot
proteins
pubmed
19111664
uniprot
proteins
pubmed
19141530
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19494351
uniprot
proteins
pubmed
1953640
uniprot
proteins
pubmed
19578119
uniprot
proteins
pubmed
19704023
uniprot
proteins
pubmed
19821948
uniprot
proteins
pubmed
2001252
uniprot
proteins
pubmed
20020534
uniprot
proteins
pubmed
20682778
uniprot
proteins
pubmed
20702409
uniprot
proteins
pubmed
2145280
uniprot
proteins
pubmed
22116617
uniprot
proteins
pubmed
22492581
uniprot
proteins
pubmed
23125415
uniprot
proteins
pubmed
2341395
uniprot
proteins
pubmed
2345548
uniprot
proteins
pubmed
23658209
uniprot
proteins
pubmed
2392682
uniprot
proteins
pubmed
24478423
uniprot
proteins
pubmed
2452834
uniprot
proteins
pubmed
24789099
uniprot
proteins
pubmed
25398877
uniprot
proteins
pubmed
25494608
uniprot
proteins
pubmed
2565345
uniprot
proteins
pubmed
2787511
uniprot
proteins
pubmed
27993971
uniprot
proteins
pubmed
28302677
uniprot
proteins
pubmed
28518345
uniprot
proteins
pubmed
28873464
uniprot
proteins
pubmed
29030430
uniprot
proteins
pubmed
29084015
uniprot
proteins
pubmed
29301984
uniprot
proteins
pubmed
29380037
uniprot
proteins
pubmed
31331973
uniprot
proteins
pubmed
3165296
uniprot
proteins
pubmed
31859394
uniprot
proteins
pubmed
33436497
uniprot
proteins
pubmed
33436498
uniprot
proteins
pubmed
33724573
uniprot
proteins
pubmed
3494014
uniprot
proteins
pubmed
35687021
uniprot
proteins
pubmed
37184585
uniprot
proteins
pubmed
3798869
uniprot
proteins
pubmed
38016540
uniprot
proteins
pubmed
3801670
uniprot
proteins
pubmed
39197621
uniprot
proteins
pubmed
39713860
uniprot
proteins
pubmed
7519807
uniprot
proteins
pubmed
7694683
uniprot
proteins
pubmed
7878622
uniprot
proteins
pubmed
8093349
uniprot
proteins
pubmed
8132570
uniprot
proteins
pubmed
8298129
uniprot
proteins
pubmed
8631894
uniprot
proteins
pubmed
8781422
uniprot
proteins
pubmed
9111081
uniprot
proteins
pubmed
9195946
uniprot
proteins
pubmed
9215749
uniprot
proteins
pubmed
9376589
uniprot
proteins
pubmed
9618541
uniprot
proteins
pubmed
9684783
uniprot
proteins
pubmed
9790984
uniprot
proteins
sequence_length
788
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-pass type I membrane protein {ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:20702409}. Cell junction, focal adhesion {ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:35687021}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:O54890}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O54890}. Synapse {ECO:0000250|UniProtKB:O54890}.
uniprot
proteins
transmembrane_region
TRANSMEM 719..741; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins