Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
Expressed in heart, brain, placenta, ovary and small intestine. Isoform Short is found in the ovary.
Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
Expressed in tissues undergoing reconstruction. Present in fetal tissues, especially in brain. Expression seems to decline with advanced development.
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.
The precursor is cleaved by a furin endopeptidase.
Cell membrane. Localized at the cell surface of melanoma cells and Secreted > extracellular space > extracellular matrix. Cell surface. Localized at the cell surface of melanoma cells.
Hadchouel A et al. Matrix metalloproteinase gene polymorphisms and bronchopulmonary dysplasia: identification of MMP16 as a new player in lung development. PLoS ONE3:e3188 (2008).
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