The ADAM9 protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor.
Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling.
This member is a type I transmembrane protein and serves as a marker for dendritic cell differentiation. It has also been demonstrated to be an active metalloproteinase, which may be involved in normal physiological and pathological processes such as cells migration, cell adhesion, cell-cell and cell-matrix interactions, and signal transduction.
^Wolfsberg TG, Straight PD, Gerena RL et al. (1995). "ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain". Dev. Biol.169 (1): 378–383. doi:10.1006/dbio.1995.1152. PMID7750654.
^Liu, P.C. et al. (2006). "Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells.". Cancer Biology and Therapy5 (6): 657–664. doi:10.4161/cbt.5.6.2708. PMID16627989.