protein_function: Active metalloproteinase with gelatinolytic andcollagenolytic activity. Plays a role in the wound healingprocess. Mediates both heterotypic intraepithelial cell,T-cellinteractions and homotypic T-cell aggregation. Inhibits beta-1integrin-mediated cell adhesion and migration of airway smoothmuscle cells. Suppresses cell motility on or towards fibronectinpossibly by driving alpha-v,beta-1 integrin (ITAGV-ITGB1) cellsurface expression via ERK1,2 inactivation. Cleaves E-cadherin inresponse to growth factor deprivation. Plays a role in glomerularcell migration. Plays a role in pathological neovascularization.May play a role in cartilage remodeling. May be proteolyticallyprocessed, during sperm epididymal maturation and the acrosomereaction. May play a role in sperm-egg binding through itsdisintegrin domain..
Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene. The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as an EGF-like domain. 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. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.
