Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (By similarity). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (By similarity). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (By similarity). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (By similarity). Involved in the degradation of the atrial natriuretic factor (ANF) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'. H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9) H2O + substance P = L-Phe-Gly-L-Leu-L-Met-NH2 + substance P(1-7) H2O + neurotensin = L-isoleucyl-L-leucine + neurotensin(1-11) H2O + neurotensin = L-tyrosyl-L-isoleucyl-L-leucine + neurotensin(1-10) Binds 1 zinc ion per subunit. Myristoylation is a determinant of membrane targeting. Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. Mice are overtly normal in appearance and size and do not show obvious abnormalities in motor performance or coordination. Nerve conduction studies reveal no significant differences between mutant and control animals. Belongs to the peptidase M13 family.