meprin A subunit alpha; endopeptidase-2; N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha; PABA peptide hydrolase; PPH alpha (MEP1A)

Function: - hydrolysis of protein & peptide substrates preferentially on carboxyl side of hydrophobic residues - homotetramer consisting of disulfide-linked alpha subunits - homooligomer consisting of disulfide-linked alpha subunit homodimers - 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) Inhibition: - inhibited by several hydroxamate compounds, the most potent inhibitor is actinonin Kinetic parameters: - KM=110 uM for GRP - KM=18.0 uM for PTH 12-34 - KM=33.9 uM for secretin - KM=41.3 uM for substance P - KM=56.5 uM for LHRH - KM=73.2 uM for orcokinin - KM=292 uM for alpha-MSH - KM=125 uM for bradykinin - KM=200 uM for gastrin Cofactor: - binds 1 Zn⁺² per subunit (putative) Structure: - N-glycosylated; contains GlcNAc, galactose, mannose & a small amount of fucose (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 = 746 aa MW = 84 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-21} Metalloprotease {66-263} MOTIF: cysteine residue {C107} MODIFICATION: cysteine residue {C259} cysteine residue {C128} MODIFICATION: cysteine residue {C147} N-glycosylation site {N140} cysteine residue {C147} MODIFICATION: cysteine residue {C128} Zn+2-binding site SITE: 155-155 glutamate residue {E156} Zn+2-binding site SITE: 159-159 Zn+2-binding site SITE: 165-165 N-glycosylation site {N222} N-glycosylation site {N258} cysteine residue {C259} MODIFICATION: cysteine residue {C107} MAM domain {264-433} MOTIF: cysteine residue {*1} (2) MODIFICATION: cysteine residue {*2} cysteine residue {*2} (2) MODIFICATION: cysteine residue {*1} cysteine residue {C269} MODIFICATION: cysteine residue {C431} cysteine residue {C277} MODIFICATION: cysteine residue {C-INTERCHAIN} cysteine residue {C308} MODIFICATION: cysteine residue {C-INTERCHAIN} N-glycosylation site {N414} cysteine residue {C431} MODIFICATION: cysteine residue {C269} MATH {434-593} MOTIF: N-glycosylation site {N440} N-glycosylation site {N447} N-glycosylation site {N539} EGF domain {670-710} MOTIF: cysteine residue {C674} MODIFICATION: cysteine residue {C685} cysteine residue {C679} MODIFICATION: cysteine residue {C694} cysteine residue {C685} MODIFICATION: cysteine residue {C674} cysteine residue {C694} MODIFICATION: cysteine residue {C679} cysteine residue {C696} MODIFICATION: cysteine residue {C709} cysteine residue {C709} MODIFICATION: cysteine residue {C696} transmembrane domain {713-740}

Database Correlations

OMIM 600388 UniProt Q16819 PFAM correlations Entrez Gene 4224 Kegg hsa:4224 ENZYME 3.4.24.18

References

UniProt :accession Q16819