Aliases for ITGA4 Gene
External Ids for ITGA4 Gene
Previous HGNC Symbols for ITGA4 Gene
Previous GeneCards Identifiers for ITGA4 Gene
The gene encodes a member of the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain that function in cell surface adhesion and signaling. The encoded preproprotein is proteolytically processed to generate light and heavy chains that comprise the alpha 4 subunit. This subunit associates with a beta 1 or beta 7 subunit to form an integrin that may play a role in cell motility and migration. This integrin is a therapeutic target for the treatment of multiple sclerosis, Crohn's disease and inflammatory bowel disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Oct 2015]
GeneCards Summary for ITGA4 Gene
ITGA4 (Integrin Subunit Alpha 4) is a Protein Coding gene. Diseases associated with ITGA4 include progressive multifocal leukoencephalopathy and breast sarcoma. Among its related pathways are Platelet activation, signaling and aggregation and Sertoli-Sertoli Cell Junction Dynamics. GO annotations related to this gene include cell adhesion molecule binding and fibronectin binding. An important paralog of this gene is ITGA8.
UniProtKB/Swiss-Prot for ITGA4 Gene
Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells.
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.