MMP16

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 encoded protein activates MMP2 by cleavage. This gene was once referred to as MT-MMP2, but was renamed as MT-MMP3 or MMP16.

MATRIX METALLOPEPTIDASE 16

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.

Chondrocyte proliferation Source: Ensembl
Collagen catabolic process Source: GO_Central
Craniofacial suture morphogenesis Source: Ensembl
Embryonic cranial skeleton morphogenesis Source: Ensembl
Endochondral ossification Source: Ensembl
Extracellular matrix organization Source: GO_Central
Protein processing Source: ParkinsonsUK-UCL
Proteolysis Source: ParkinsonsUK-UCL
Skeletal system development Source: GO_Central

Isoform Long:
Plasma membrane
Cell membrane
Note: Localized at the cell surface of melanoma cells.
Isoform Short:
Extracellular region or secreted
extracellular matrix
Other locations
Cell surface
Note: Localized at the cell surface of melanoma cells.

Extracellular: 120-564
Helical: 565-585
Cytoplasmic: 586-607

The precursor is cleaved by a furin endopeptidase.