Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. 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.
Subcellular locations: Cell membrane, Secreted
Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.
The major site of expression is the brush border membrane of small intestinal and kidney epithelial cells.