catalytic activity:Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.,cofactor:Binds 1 zinc ion per subunit.,enzyme regulation:Inhibited by thiorphan and phosphoramidon.,function:Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificiy with MME and cleaves peptides at the same amide bond.,PTM:N-glycosylated.,similarity:Belongs to the peptidase M13 family.,subcellular location:A secreted form produced by proteollytic cleavage also exists.,tissue specificity:Predominantly expressed in testis. Weakly expressed in brain, kidney and heart.,
Membrane; Single-pass type II membrane protein. Secreted. A secreted form produced by proteolytic cleavage also exists. .
Predominantly expressed in testis. Weakly expressed in brain, kidney and heart.
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