MMP9
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
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity).
Post-translational modifications
N- and O-glycosylated.
Sequence Similarities
Belongs to the peptidase M10A family.
Tissue Specificity
Osteoclasts.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
Alternative names
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB, MMP9