ADAM15

ADAM15 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

ADAM Metallopeptidase Domain 15

Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.

Angiogenesis
Cardiac epithelial to mesenchymal transition
Cell-matrix adhesion
Cellular response to phorbol 13-acetate 12-myristate
Collagen catabolic process
Extracellular matrix disassembly
Extracellular matrix organization
Immune response to tumor cell
Innate immune response
Integrin-mediated signaling pathway
Male gonad development
Negative regulation of cell growth
Negative regulation of cell-matrix adhesion
Negative regulation of cell migration
Negative regulation of receptor binding
Response to hypobaric hypoxia
Tissue regeneration

Endomembrane system; Adherens junction. The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity).

Extracellular: 207-696 aa
Helical: 697-717 aa
Cytoplasmic: 718-863 aa

The precursor is cleaved by a furin endopeptidase.
Phosphorylation increases association with PTKs.