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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 (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:23142597, PubMed:32883094). 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.

Cellular localization

  • Secreted
  • Extracellular space
  • Extracellular matrix

Alternative names

Clg4b, Mmp9, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB

Target type

Proteins

Primary research area

Oncology

Other research areas

  • Cardiovascular
  • Immunology & Infectious Disease
  • Neuroscience

Molecular weight

80535Da