Mep1b
Function
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.
Post-translational modifications
N-glycosylated; contains high mannose and/or complex biantennary structures.
Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.
Phosphorylated by PKC at multiple sites of its cytoplasmic part. Phosphorylation dcreases activity at the cell surface, leading to diminished substrate cleavage.
Tissue Specificity
Kidney, intestinal brush borders and salivary ducts.
Cellular localization
- Cell membrane
- Single-pass type I membrane protein
- Secreted
- Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.
Alternative names
Meprin A subunit beta, Endopeptidase-2, Meprin B, Mep1b