ID:MMP27_HUMAN DESCRIPTION: RecName: Full=Matrix metalloproteinase-27; Short=MMP-27; EC=3.4.24.-; Flags: Precursor; FUNCTION: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens (By similarity). COFACTOR: Binds 4 calcium ions per subunit (By similarity). COFACTOR: Binds 2 zinc ions per subunit (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Expressed in B-cells. 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. SIMILARITY: Belongs to the peptidase M10A family. SIMILARITY: Contains 4 hemopexin-like domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9H306
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.