Membrane metallopeptidase that sheds many membrane-bound proteins. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.
The major site of expression is the brush border membrane of small intestinal and kidney epithelial cells.
Belongs to the peptidase M12A family. Contains 1 EGF-like domain. Contains 1 MAM domain. Contains 1 MATH domain.
N-glycosylated; contains high mannose and/or complex biantennary structures. O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human. Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.
Cell membrane. Secreted. Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.