MMP17
Domain
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.
Function
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. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. 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.
Post-translational modifications
The precursor is cleaved by a furin endopeptidase.
Sequence Similarities
Belongs to the peptidase M10A family.
Tissue Specificity
Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.
Cellular localization
- Isoform Long
- Cell membrane
- Lipid-anchor
- GPI-anchor
- Extracellular side
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
MT4MMP, MMP17, Matrix metalloproteinase-17, MMP-17, Membrane-type matrix metalloproteinase 4, Membrane-type-4 matrix metalloproteinase, MT-MMP 4, MTMMP4, MT4-MMP