Meprin A subunit beta; endopeptidase-2; Meprin B; N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta; PABA peptide hydrolase; PPH beta (MEP1B)

Function: - hydrolysis of proteins, including azocasein, & peptides - hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 & 19-Cys-|-Gly-20 bonds in insulin B chain - homotetramer consisting of disulfide-linked beta subunits - heterotetramer of two alpha & two beta subunits formed by non-covalent association of two disulfide-linked heterodimers (putative) - interacts with MBL2 through its carbohydrate moiety; interaction may inhibit its catalytic activity (putative) Cofactor: - binds 1 Zn⁺² per subunit (putative) Structure: - N-glycosylated; contains high mannoase &/or complex biantennary structures (putative) - belongs to the peptidase M12A family - contains 1 EGF-like domain - contains 1 MAM domain - contains 1 MATH domain Compartment: - membrane; single-pass type 1 membrane protein

General

glycoprotein plasma membrane protein protein subunit

Properties

SIZE: entity length = 701 aa MW = 80 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-22} Metalloprotease {64-259} MOTIF: cysteine residue {C103} MODIFICATION: cysteine residue {C255} cysteine residue {C124} MODIFICATION: cysteine residue {C144} cysteine residue {C144} MODIFICATION: cysteine residue {C124} Zn+2-binding site SITE: 152-152 glutamate residue {E153} Zn+2-binding site SITE: 156-156 Zn+2-binding site SITE: 162-162 N-glycosylation site {N218} N-glycosylation site {N254} cysteine residue {C255} MODIFICATION: cysteine residue {C103} MAM domain {260-429} MOTIF: cysteine residue {*1} (2) MODIFICATION: cysteine residue {*2} cysteine residue {*2} (2) MODIFICATION: cysteine residue {*1} cysteine residue {C265} MODIFICATION: cysteine residue {C427} cysteine residue {C273} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C305} MODIFICATION: cysteine residue {C-INTERCHAIN} N-glycosylation site {N370} N-glycosylation site {N421} cysteine residue {C427} MODIFICATION: cysteine residue {C265} MATH {430-585} MOTIF: N-glycosylation site {N436} N-glycosylation site {N445} cysteine residue {C492} MODIFICATION: cysteine residue {C-INTERCHAIN} N-glycosylation site {N547} N-glycosylation site {N592} EGF domain {604-644} MOTIF: cysteine residue {C608} MODIFICATION: cysteine residue {C619} cysteine residue {C613} MODIFICATION: cysteine residue {C628} cysteine residue {C619} MODIFICATION: cysteine residue {C608} cysteine residue {C628} MODIFICATION: cysteine residue {C613} cysteine residue {C630} MODIFICATION: cysteine residue {C643} cysteine residue {C643} MODIFICATION: cysteine residue {C630} transmembrane domain {653-673}

Database Correlations

OMIM 600389 UniProt Q16820 PFAM correlations Entrez Gene 4225 Kegg hsa:4225 ENZYME 3.4.24.63

References

UniProt :accession Q16820