ITGA3 encodes the integrin alpha 3 chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 3 undergoes post-translational cleavage in the extracellular domain to yield disulfide-linked light and heavy chains that join with beta 1 to form an integrin that interacts with many extracellular matrix proteins.
The alpha 3 beta 1 integrin is known variously as: very late (activation) antigen 3 ('VLA-3'), very common antigen 2 ('VCA-2'), extracellular matrix receptor 1 ('ECMR1'), and galactoprotein b3 ('GAPB3').
^Jones SD, van der Flier A, Sonnenberg A (September 1998). "Genomic organization of the human alpha 3 integrin subunit gene". Biochem Biophys Res Commun248 (3): 896–8. doi:10.1006/bbrc.1998.9071. PMID9704023.
^Park KR, Inoue T, Ueda M, Hirano T, Higuchi T, Maeda M et al. (March 2000). "CD9 is expressed on human endometrial epithelial cells in association with integrins alpha(6), alpha(3) and beta(1)". Mol. Hum. Reprod.6 (3): 252–7. doi:10.1093/molehr/6.3.252. PMID10694273.
^Hirano T, Higuchi T, Ueda M, Inoue T, Kataoka N, Maeda M et al. (February 1999). "CD9 is expressed in extravillous trophoblasts in association with integrin alpha3 and integrin alpha5". Mol. Hum. Reprod.5 (2): 162–7. doi:10.1093/molehr/5.2.162. PMID10065872.
^Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M et al. (October 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem.275 (43): 33669–78. doi:10.1074/jbc.M002519200. PMID10906324.
^Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R et al. (July 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". J. Cell. Sci.113 (13): 2385–97. PMID10852818.
^Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (November 1997). "NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins". J. Biol. Chem.272 (46): 29181–9. doi:10.1074/jbc.272.46.29181. PMID9360996.