Matrix Metalloproteinase 7 (MMP7) Active Protein

Proteins of the matrix metalloproteinase (MMP) 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

MMP7: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. Belongs to the peptidase M10A family.

Protein type: EC 3.4.24.23; Secreted; Secreted, signal peptide; Protease

Chromosomal Location of Human Ortholog: 11q22.2

Cellular Component: proteinaceous extracellular matrix; extracellular space; extracellular region

Molecular Function: zinc ion binding; metalloendopeptidase activity

Biological Process: response to drug; collagen catabolic process; extracellular matrix disassembly; defense response to Gram-positive bacterium; extracellular matrix organization and biogenesis; antibacterial peptide biosynthetic process; defense response to Gram-negative bacterium; proteolysis; antibacterial peptide secretion; regulation of cell proliferation