Aliases for ITGA5 Gene
External Ids for ITGA5 Gene
Previous HGNC Symbols for ITGA5 Gene
Previous GeneCards Identifiers for ITGA5 Gene
The product of this gene belongs to the integrin alpha chain family. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 5 subunit. This subunit associates with the beta 1 subunit to form a fibronectin receptor. This integrin may promote tumor invasion, and higher expression of this gene may be correlated with shorter survival time in lung cancer patients. Note that the integrin alpha 5 and integrin alpha V subunits are encoded by distinct genes. [provided by RefSeq, Oct 2015]
GeneCards Summary for ITGA5 Gene
ITGA5 (Integrin, Alpha 5 (Fibronectin Receptor, Alpha Polypeptide)) is a Protein Coding gene. Diseases associated with ITGA5 include colon carcinoma in situ and congenital epulis. Among its related pathways are PI3K-Akt signaling pathway and Regulation of actin cytoskeleton. GO annotations related to this gene include integrin binding and epidermal growth factor receptor binding. An important paralog of this gene is ITGA8.
UniProtKB/Swiss-Prot for ITGA5 Gene
Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands
(Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for human metapneumovirus (PubMed:12907437). Integrin ITGA2:ITGB1 acts as a receptor for human parvovirus B19 (PubMed:24478423). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposis sarcoma lesions (PubMed:10397733).
Integrins are ubiquitously expressed adhesion molecules. They are cell-surface receptors that exist as heterodimers of alpha and beta subunits. Under physiological conditions, integrins are highly glycosylated and contain a Ca2+ or Mg2+ ion, which is essential for ligand binding.