Open Access Articles- Top Results for CD49c


SymbolsITGA3 ; CD49C; GAP-B3; GAPB3; ILNEB; MSK18; VCA-2; VL3A; VLA3a
External IDsOMIM605025 MGI96602 HomoloGene21129 IUPHAR: 2442 ChEMBL: 3525 GeneCards: ITGA3 Gene
RNA expression pattern
File:PBB GE ITGA3 201474 s at tn.png
More reference expression data
RefSeq (mRNA)NM_002204NM_013565
RefSeq (protein)NP_002195NP_038593
Location (UCSC)Chr 17:
48.13 – 48.17 Mb
Chr 11:
95.04 – 95.08 Mb
PubMed search[1][2]

Integrin alpha-3 is a protein that in humans is encoded by the ITGA3 gene.[1][2] ITGA3 is an integrin alpha subunit. Together with beta-1 subunit, it makes up half of the α3β1 integrin duplex that plays a role in neural migration and corticogenesis, acted upon by such factors as netrin-1 and reelin.

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.

Alternative names

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').[3]


CD49c has been shown to interact with:


  1. ^ Takada Y, Murphy E, Pil P, Chen C, Ginsberg MH, Hemler ME (October 1991). "Molecular cloning and expression of the cDNA for alpha 3 subunit of human alpha 3 beta 1 (VLA-3), an integrin receptor for fibronectin, laminin, and collagen". J Cell Biol 115 (1): 257–66. PMC 2289928. PMID 1655803. doi:10.1083/jcb.115.1.257. 
  2. ^ Jones SD, van der Flier A, Sonnenberg A (September 1998). "Genomic organization of the human alpha 3 integrin subunit gene". Biochem Biophys Res Commun 248 (3): 896–8. PMID 9704023. doi:10.1006/bbrc.1998.9071. 
  3. ^ "Entrez Gene: ITGA3 integrin, alpha 3 (antigen CD49C, alpha 3 subunit of VLA-3 receptor)". 
  4. ^ 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. PMID 10694273. doi:10.1093/molehr/6.3.252. 
  5. ^ 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. PMID 10065872. doi:10.1093/molehr/5.2.162. 
  6. ^ 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. PMID 10906324. doi:10.1074/jbc.M002519200. 
  7. ^ 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. PMID 10852818. 
  8. ^ 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. PMID 9360996. doi:10.1074/jbc.272.46.29181. 

Further reading


External links

Lua error in package.lua at line 80: module 'Module:Buffer' not found.