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MMP3 (stromelysin-1) belongs to the peptidase M10A subfamily. It is secreted in its pro-protein form, and is activated by extracellular proteinase cleavage. MMP3 is capable of binding to zinc and calcium ions, and has metallo-endopeptidase activity. The active enzyme degrades collagen, gelatin, fibronectin, and laminin. It is involved in normal cellular processes such as wound repair and tissue remodeling. Mutations in the gene can result in coronary heart disease 6.
CHDS6; EC 3.4.24.17; EMS-2; matrix metallo protease; matrix metallopeptidase 3; matrix metallopeptidase 3 (stromelysin 1, progelatinase); matrix metalloproteinase 3; matrix metalloproteinase 3 (stromelysin 1, progelatinase); matrix metalloproteinase 3 precursor; matrix metalloproteinase-3; metalloproteinase 3 receptor; MMP; MMP10; MMP3; MMP-3; MMP-3 protein; MMPs; progelatinase; proteoglycanase; SL-1; SLN1; SLN-1; STMY; STMY1; Str1; STR-1; stromelysin; stromelysin 1; Stromelysin1; stromelysin-1; Transin1; Transin-1
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