Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:23142597, PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity). Cleavage of gelatin types I and V and collagen types IV and V. Binds 2 Zn(2+) ions per subunit. Binds 3 Ca(2+) ions per subunit. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. (Microbial infection) Induced in macrophages as well as in whole animals (spleen, lung and liver) by incubation or infection with M.bovis BCG and M.tuberculosis H37Rv (at protein level) (PubMed:11500442). The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. N- and O-glycosylated. Belongs to the peptidase M10A family.