Integrin alpha 2b

Integrin alpha-IIb is a protein that in humans is encoded by the ITGA2B gene. ITGA2B, also known as CD41, encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.[5]

ITGA2B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DPK, 1DPQ, 1KUP, 1KUZ, 1M8O, 1S4W, 1TYE, 2K1A, 2K9J, 2KNC, 2MTP, 2VC2, 2VDK, 2VDL, 2VDM, 2VDN, 2VDO, 2VDP, 2VDQ, 2VDR, 3FCS, 3FCU, 3NID, 3NIF, 3NIG, 3T3M, 3T3P, 3ZDX, 3ZDY, 3ZDZ, 3ZE0, 3ZE1, 3ZE2, 4CAK, 4Z7O, 4Z7Q, 5HDB, 4Z7N
Identifiers
Aliases	ITGA2B, BDPLT16, BDPLT2, CD41, CD41B, GP2B, GPIIb, GT, GTA, HPA3, PPP1R93, integrin subunit alpha 2b
External IDs	OMIM: 607759 MGI: 96601 HomoloGene: 37304 GeneCards: ITGA2B
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17q21.31 Start 44,372,180 bp[1] End 44,389,649 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 D|11 66.29 cM Start 102,453,297 bp[2] End 102,470,122 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • fibrinogen binding • extracellular matrix binding • identical protein binding • metal ion binding Cellular component • focal adhesion • integrin complex • integral component of plasma membrane • platelet alpha granule membrane • integral component of membrane • membrane • external side of plasma membrane • extracellular exosome • cell membrane • blood microparticle • cell surface Biological process • extracellular matrix organization • cell-matrix adhesion • positive regulation of leukocyte migration • platelet aggregation • platelet degranulation • cell adhesion • integrin-mediated signaling pathway • regulation of megakaryocyte differentiation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3674	16399
Ensembl	ENSG00000005961	ENSMUSG00000034664
UniProt	P08514	Q9QUM0
RefSeq (mRNA)	NM_000419	NM_010575
RefSeq (protein)	NP_000410	NP_034705
Location (UCSC)	Chr 17: 44.37 – 44.39 Mb	Chr 11: 102.45 – 102.47 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

ITGA2B has been shown to interact with AUP1[6] and CLNS1A.[7]

See also

• Cluster of differentiation
• Glycoprotein IIb/IIIa

References

1. GRCh38: Ensembl release 89: ENSG00000005961 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034664 - Ensembl, 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. "Entrez Gene: ITGA2B integrin, alpha 2b (platelet glycoprotein IIb of IIb/IIIa complex, antigen CD41)".
6. Kato, Atsushi; Kawamata Norihiko; Tamayose Kenji; Egashira Motoki; Miura Rika; Fujimura Tsutomu; Murayama Kimie; Oshimi Kazuo (Aug 2002). "Ancient ubiquitous protein 1 binds to the conserved membrane-proximal sequence of the cytoplasmic tail of the integrin alpha subunits that plays a crucial role in the inside-out signaling of alpha IIbbeta 3". J. Biol. Chem. United States. 277 (32): 28934–41. doi:10.1074/jbc.M204340200. ISSN 0021-9258. PMID 12042322.
7. Larkin, Deirdre; Murphy Derek; Reilly Dermot F; Cahill Martha; Sattler Ellen; Harriott Pat; Cahill Dolores J; Moran Niamh (Jun 2004). "ICln, a novel integrin alphaIIbbeta3-associated protein, functionally regulates platelet activation". J. Biol. Chem. United States. 279 (26): 27286–93. doi:10.1074/jbc.M402159200. ISSN 0021-9258. PMID 15075326.

Further reading

• Bray PF (1995). "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization". Thromb. Haemost. 72 (4): 492–502. PMID 7878622.
• Naik UP, Parise LV (1997). "Structure and function of platelet alpha IIb beta 3". Curr. Opin. Hematol. 4 (5): 317–22. PMID 9288464.
• Porter JC, Hogg N (1999). "Integrins take partners: cross-talk between integrins and other membrane receptors". Trends Cell Biol. 8 (10): 390–6. doi:10.1016/S0962-8924(98)01344-0. PMID 9789327.
• Lincoff AM (1998). "Trials of platelet glycoprotein IIb/IIIa receptor antagonists during percutaneous coronary revascularization". Am. J. Cardiol. 82 (8B): 36P–42P. doi:10.1016/S0002-9149(98)00662-6. PMID 9809890.
• Bennett JS (2001). "Platelet-fibrinogen interactions". Ann. N. Y. Acad. Sci. 936: 340–54. Bibcode:2001NYASA.936..340B. doi:10.1111/j.1749-6632.2001.tb03521.x. PMID 11460491.
• Plow EF, Cierniewski CS, Xiao Z, et al. (2002). "AlphaIIbbeta3 and its antagonism at the new millennium". Thromb. Haemost. 86 (1): 34–40. doi:10.1055/s-0037-1616198. PMID 11487023.
• Quinn MJ, Byzova TV, Qin J, et al. (2004). "Integrin alphaIIbbeta3 and its antagonism". Arterioscler. Thromb. Vasc. Biol. 23 (6): 945–52. doi:10.1161/01.ATV.0000066686.46338.F1. PMID 12637342.
• Fullard JF (2004). "The role of the platelet glycoprotein IIb/IIIa in thrombosis and haemostasis". Curr. Pharm. Des. 10 (14): 1567–76. doi:10.2174/1381612043384682. PMID 15134555.
• Watson SP, Auger JM, McCarty OJ, Pearce AC (2005). "GPVI and integrin alphaIIb beta3 signaling in platelets". J. Thromb. Haemost. 3 (8): 1752–62. doi:10.1111/j.1538-7836.2005.01429.x. PMID 16102042.
• Bennett JS (2006). "Structure and function of the platelet integrin alphaIIbbeta3". J. Clin. Invest. 115 (12): 3363–9. doi:10.1172/JCI26989. PMC 1297263. PMID 16322781.
• Ma YQ, Qin J, Plow EF (2007). "Platelet integrin alpha(IIb)beta(3): activation mechanisms". J. Thromb. Haemost. 5 (7): 1345–52. doi:10.1111/j.1538-7836.2007.02537.x. PMID 17635696.

External links

• CD41+Antigen at the US National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: P08514 (Human Integrin alpha-IIb) at the PDBe-KB.