| Post Translational Modifications | Phosphorylated by PKC at multiple sites of its cytoplasmic part. Phosphorylation dcreases activity at the cell surface, leading to diminished substrate cleavage. 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. |
| 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. Cleaves also the amyloid precursor protein/APP, thereby releasing neurotoxic amyloid beta peptides. |
| Protein Name | Meprin A Subunit BetaEndopeptidase-2Meprin BN-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit BetaPaba Peptide HydrolasePph Beta |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinSecretedHomodimers Are Essentially Membrane Bound But May Also Be Shed From The Surface By Adam-10 And Adam-17 |
| Alternative Protein Names | Meprin A Subunit Beta proteinEndopeptidase-2 proteinMeprin B proteinN-Benzoyl-L-Tyrosyl-P-Amino-Benzoic Acid Hydrolase Subunit Beta proteinPaba Peptide Hydrolase proteinPph Beta proteinMEP1B protein |
Information sourced from Uniprot.org
