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

Full Name

ADAM Metallopeptidase Domain 15

Function

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.

Biological Process

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

Cellular Location

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).

Topology

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

PTM

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