Background information
Integrins are heterodimers composed of noncovalently associated transmembrane Alpha and Beta subunits. The sixteen Alpha and eight Beta subunits heterodimerize to produce more than 20 different receptors. Certain integrins can also bind to soluble ligands such as Fibrinogen, or to counter-receptors on adjacent cells, such as the intracellular adhesion molecules (ICAMs), leading to aggregation of cells. In addition to mediating cell adhesion and cytoskeletal organization, Integrins function as signaling receptors. Signals transduced by Integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis. ITFG3 (Integrin alpha FG-GAP repeat containing 3), also known as C16orf9, is a 552 amino acid single-pass transmembrane protein that contains FG-GAP repeats, a motif commonly found in Integrin proteins. There are two isoforms of ITFG3 that are produced as a result of alternative splicing events.
