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membrane metallo-endopeptidase-like 1; membrane metallo-endopeptidase-like 2; nNeprilysin-2; NL2; NEP2m [Contains: membrane metallo-endopeptidase-like 1, soluble form (neprilysin-2 secreted) (NEP2(s))] (MMEL1, MELL1, MMEL2, NEP2)
Function:
1) metalloprotease involved in sperm function
2) role in fertilization & early embryonic development
3) degrades broad variety of small peptides with preference for peptides shorter than 3 kD containing neutral bulky aliphatic or aromatic amino acid residues
4) shares the same substrate specificiy with MME & cleaves peptides at same amide bond
5) preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'
Cofactor: binds 1 Zn+2 per subunit
Inhibition:
- inhibited by thiorphan & phosphoramidon
Structure:
- N-glycosylated
- belongs to the peptidase M13 family
Compartment: membrane, secreted
Alternative splicing: named isoforms=3
Expression:
- predominantly expressed in testis
- weakly expressed in brain, kidney, heart
General
glycoprotein
membrane protein
metalloprotease
Properties
SIZE: MW = 89 kD
entity length = 779 aa
COMPARTMENT: cellular membrane
MOTIF: transmembrane domain {28-48}
proteolytic site {73-74}
cysteine residue {C89}
MODIFICATION: cysteine residue {C94}
cysteine residue {C94}
MODIFICATION: cysteine residue {C89}
cysteine residue {C112}
MODIFICATION: cysteine residue {C764}
cysteine residue {C120}
MODIFICATION: cysteine residue {C724}
binding site
SITE: 135-135
FOR-BINDING-OF: Substrate carboxyl
cysteine residue {C175}
MODIFICATION: cysteine residue {C439}
N-glycosylation site {N177}
N-glycosylation site {N207}
N-glycosylation site {N350}
cysteine residue {C439}
MODIFICATION: cysteine residue {C175}
coiled coil {515-560}
MOTIF: N-glycosylation site {N530}
Zn+2-binding site
SITE: 613-613
Zn+2-binding site
SITE: 617-617
aspartate residue {D620}
cysteine residue {C650}
MODIFICATION: cysteine residue {C776}
N-glycosylation site {N657}
Zn+2-binding site
SITE: 676-676
aspartate residue {D680}
cysteine residue {C724}
MODIFICATION: cysteine residue {C120}
cysteine residue {C764}
MODIFICATION: cysteine residue {C112}
cysteine residue {C776}
MODIFICATION: cysteine residue {C650}
Database Correlations
UniProt Q495T6
PFAM correlations
ENZYME 3.4.24.11
References
UniProt :accession Q495T6