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Developmental stage

Present in unfertilized eggs and at the zygote and cleavage stages. Levels increase at the blastocyst stage and with endoderm differentiation.

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

Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Acts also intracellularly. For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:17116747). In addition, plays a role in immune response and possesses antiviral activity against various viruses (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311).

Sequence similarities

Belongs to the peptidase M10A family.

Cellular localization

  • Secreted
  • Extracellular space
  • Extracellular matrix

Alternative names

Stromelysin-1, SL-1, EMS-2, Matrix metalloproteinase-3, Transin-1, MMP-3, Mmp3

Target type

Proteins

Primary research area

Immunology & Infectious Disease

Other research areas

  • Neuroscience

Molecular weight

53845Da