MEP1B

Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes, and in leukocytes and certain cancer cells. They are involved in the hydrolysis of a variety of peptide and protein substrates, and have been implicated in cancer and intestinal inflammation. Mature meprins are oligomers of evolutionarily related, but separately encoded alpha and/or beta subunits. Homooligomers of alpha subunit are secreted, whereas, oligomers containing the beta subunit are plasma membrane-bound. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in kidney and intestine.

MEPRIN A SUBUNIT BETA

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.

Inflammatory response Source: UniProtKB-KW
Toxin transport Source: Ensembl

Secreted
Plasma membrane
Cell membrane
Note: Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.

Extracellular: 23-652
Helical: 653-673
Cytoplasmic: 674-701

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.