MMP-15 Antibody – Mouse Monoclonal

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. [provided by RefSeq, Jul 2008]

Function: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. Ref.6

Cofactor: Binds 1 zinc ion per subunit

By similarity.Calcium

By similarity.

Subcellular location: Membrane; Single-pass type I membrane protein; Extracellular side

Potential.

Tissue specificity: Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.

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.

Post-translational modification: The precursor is cleaved by a furin endopeptidase

By similarity.

Sequence similarities: Belongs to the peptidase M10A family.Contains 4 hemopexin repeats.

Sequence caution: The sequence BAA13071.1 differs from that shown. Reason: Erroneous initiation.