Matrix Metalloproteinase 17 MT4 Catalytic Domain (MMP17) 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 protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage. [provided by RefSeq, Jul 2008]

MMP17: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. Belongs to the peptidase M10A family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Membrane protein, GPI anchor; Membrane protein, integral; Protease; Activator; EC 3.4.24.-

Chromosomal Location of Human Ortholog: 12q24.3

Cellular Component: proteinaceous extracellular matrix; integral to plasma membrane

Molecular Function: zinc ion binding; metalloendopeptidase activity; enzyme activator activity; calcium ion binding

Biological Process: positive regulation of catalytic activity; proteolysis