This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease degrades soluble and insoluble elastin. This gene may play a role in aneurysm formation and mutations in this gene are associated with lung function and chronic obstructive pulmonary disease (COPD). This gene is part of a cluster of MMP genes on chromosome 11. [provided by RefSeq, Jan 2016],catalytic activity:Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.,cofactor:Binds 2 zinc ions per subunit.,cofactor:Binds 4 calcium ions per subunit.,domain: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.,function:May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1′ site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.,induction:By exposure to lipopolysaccharide. Inhibited by dexamethasone.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Found in alveolar macrophages but not in peripheral blood monocytes.,