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Integrin beta 3

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Mammalian protein found in Homo sapiens

ITGB3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4O02, 1JV2, 1KUP, 1KUZ, 1L5G, 1M1X, 1M8O, 1MIZ, 1MK7, 1MK9, 1S4X, 1TYE, 1U8C, 2K9J, 2KNC, 2KV9, 2L1C, 2L91, 2LJD, 2LJE, 2LJF, 2MTP, 2Q6W, 2RMZ, 2RN0, 2VC2, 2VDK, 2VDL, 2VDM, 2VDN, 2VDP, 2VDQ, 2VDR, 3FCS, 3FCU, 3IJE, 3NID, 3NIF, 3NIG, 3T3M, 3T3P, 3ZDX, 3ZDY, 3ZDZ, 3ZE0, 3ZE1, 3ZE2, 4CAK, 4G1E, 4G1M, 4MMX, 4MMY, 4MMZ, 5HDB, 4Z7Q, 4Z7O, 4Z7N

Identifiers
AliasesITGB3, BDPLT16, BDPLT2, CD61, GP3A, GPIIIa, GT, integrin subunit beta 3, BDPLT24, GT2
External IDsOMIM: 173470; MGI: 96612; HomoloGene: 55444; GeneCards: ITGB3; OMA:ITGB3 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)
Chromosome 17 (human)Genomic location for ITGB3Genomic location for ITGB3
Band17q21.32Start47,253,827 bp
End47,313,743 bp
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)
Chromosome 11 (mouse)Genomic location for ITGB3Genomic location for ITGB3
Band11 E1|11 67.84 cMStart104,498,826 bp
End104,561,302 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • thoracic aorta

  • ascending aorta

  • Descending thoracic aorta

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • tendon of biceps brachii

  • popliteal artery

  • tibial arteries

  • right coronary artery
Top expressed in
  • ascending aorta

  • aortic valve

  • decidua

  • blood

  • endothelial cell of lymphatic vessel

  • granulocyte

  • superior surface of tongue

  • femur

  • body of femur

  • zygote
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3690

16416

Ensembl

ENSG00000259207

ENSMUSG00000020689

UniProt

P05106

O54890

RefSeq (mRNA)

NM_000212

NM_016780

RefSeq (protein)

NP_000203

NP_058060

Location (UCSC)Chr 17: 47.25 – 47.31 MbChr 11: 104.5 – 104.56 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene. CD61 is a cluster of differentiation found on thrombocytes.

Structure and function

The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.

Role in endometriosis

Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.

Interactions

CD61 has been shown to interact with PTK2, ITGB3BP, TLN1 and CIB1.

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000259207Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000020689Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, et al. (June 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". The Journal of Clinical Investigation. 81 (6): 1993–1998. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
  6. Heemskerk JW, Mattheij NJ, Cosemans JM (January 2013). "Platelet-based coagulation: different populations, different functions" (PDF). Journal of Thrombosis and Haemostasis. 11 (1): 2–16. doi:10.1111/jth.12045. PMID 23106920. S2CID 206157070.
  7. "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".
  8. May KE, Villar J, Kirtley S, Kennedy SH, Becker CM (2011). "Endometrial alterations in endometriosis: a systematic review of putative biomarkers". Human Reproduction Update. 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902.
  9. Eliceiri BP, Puente XS, Hood JD, Stupack DG, Schlaepfer DD, Huang XZ, et al. (April 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". The Journal of Cell Biology. 157 (1): 149–160. doi:10.1083/jcb.200109079. PMC 2173263. PMID 11927607.
  10. Chung J, Gao AG, Frazier WA (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". The Journal of Biological Chemistry. 272 (23): 14740–14746. doi:10.1074/jbc.272.23.14740. PMID 9169439.
  11. Fujimoto TT, Katsutani S, Shimomura T, Fujimura K (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thrombosis Research. 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. PMID 11864709.
  12. Shattil SJ, O'Toole T, Eigenthaler M, Thon V, Williams M, Babior BM, et al. (November 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". The Journal of Cell Biology. 131 (3): 807–816. doi:10.1083/jcb.131.3.807. PMC 2120613. PMID 7593198.
  13. Patil S, Jedsadayanmata A, Wencel-Drake JD, Wang W, Knezevic I, Lam SC (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". The Journal of Biological Chemistry. 274 (40): 28575–28583. doi:10.1074/jbc.274.40.28575. PMID 10497223.
  14. Calderwood DA, Yan B, de Pereda JM, Alvarez BG, Fujioka Y, Liddington RC, et al. (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". The Journal of Biological Chemistry. 277 (24): 21749–21758. doi:10.1074/jbc.M111996200. PMID 11932255.
  15. Naik UP, Patel PM, Parise LV (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". The Journal of Biological Chemistry. 272 (8): 4651–4654. doi:10.1074/jbc.272.8.4651. PMID 9030514.

Further reading

External links

PDB gallery
  • 1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3 1jv2: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHAVBETA3
  • 1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND 1l5g: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN AVB3 IN COMPLEX WITH AN ARG-GLY-ASP LIGAND
  • 1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+ 1m1x: CRYSTAL STRUCTURE OF THE EXTRACELLULAR SEGMENT OF INTEGRIN ALPHA VBETA3 BOUND TO MN2+
  • 1m8o: Platelet integrin alfaIIb-beta3 cytoplasmic domain 1m8o: Platelet integrin alfaIIb-beta3 cytoplasmic domain
  • 1txv: 1txv:
  • 1ty3: 1ty3:
  • 1ty5: 1ty5:
  • 1ty6: 1ty6:
  • 1ty7: 1ty7:
  • 1tye: Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen 1tye: Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen
  • 1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure 1u8c: A novel adaptation of the integrin PSI domain revealed from its crystal structure
Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50
51–100
101–150
151–200
201–250
251–300
301–350
Coagulation cascade
Coagulation factors
Primary hemostasis
(platelet activation)
Intrinsic pathway
(contact activation)
Extrinsic pathway
(tissue factor)
Common pathway
Anticoagulant factors
Fibrinolytic factors
Coagulation markers
Platelet activation
Thrombin generation
Fibrin generation
Fibrinolysis
Integrins
Alpha
Beta
Dimers
Cytoadhesin receptor:
Fibrinogen receptor:
Fibronectin receptor:
Leukocyte-adhesion receptor:
Very late antigen receptor:
Vitronectin receptor:
see also cell surface receptor deficiencies
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