Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV- inducible elastase activity toward skin preelastic and elastic fibers. Inhibited in a dose dependent manner by opiorphin. Belongs to the peptidase M13 family. Note: This description may include information from UniProtKB.
Protein type: EC 22.214.171.124; Protease; Membrane protein, integral
Cellular Component: synaptic vesicle; integral to plasma membrane; axon; dendrite; cytoplasm; integral to membrane; plasma membrane; synapse; brush border
Molecular Function: protein binding; zinc ion binding; metalloendopeptidase activity; endopeptidase activity; peptide binding
Biological Process: cellular protein metabolic process; peptide metabolic process; beta-amyloid metabolic process; creatinine metabolic process; proteolysis; sensory perception of pain; angiotensin maturation; kidney development
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.