JavaScript is disabled in your browser. Please enable JavaScript to view this website.

MMP24

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.

The PDZ-binding motif (also named EWV motif) is required for interaction with PDZ domains of APBA3 and recycling through the trans-Golgi network.

Function

Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity).

Post-translational modifications

Cleaved by a furin endopeptidase in the trans-Golgi network.

Sequence Similarities

Belongs to the peptidase M10A family.

Tissue Specificity

Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.

Cellular localization

Alternative names

MT5MMP, MMP24, Matrix metalloproteinase-24, MMP-24, Membrane-type matrix metalloproteinase 5, Membrane-type-5 matrix metalloproteinase, MT-MMP 5, MTMMP5, MT5-MMP

swissprot:Q9Y5R2 entrezGene:10893 omim:604871