MMP7
Description
The MMP7 (matrix metallopeptidase 7) is a protein-coding gene located on chromosome 11.
Matrilysin, also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase, is an enzyme in humans encoded by the MMP7 gene. The enzyme has a molecular weight around 30 kDa and is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. Matrilysin was discovered in the uterus of the rat in 1988. The complementary DNA (cDNA) of human MMP7 was isolated in 1988. The primary role of cleaved/activated MMP7 is to break down extracellular matrix by degrading macromolecules including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan. The human MMP7 is located on chromosome 11 q22.3. MMP genes are clustered in q region of human Chromosome 11 including matrilysin, collagenase-1, stromelysin1, stromelysin-2, and metalloelastase genes. It consists of 267 amino acids.
MMP7 is also known as MMP-7, MPSL1, PUMP-1.
