cofactor:Binds 2 zinc ions per subunit.,cofactor:Binds 4 calcium ions per subunit.,disease:Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia type 2 (SEMD2) [MIM:602111]; also known as spondyloepimetaphyseal dysplasia type Missouri. SEMDs are a heterogeneous group of skeletal disorders characterized by defective growth and modeling of the spine and long bones. The SEMDs are distinguished from the spondylometaphyseal dysplasias and the spondyloepiphyseal dysplasias by the combined involvement of the epiphyses and metaphyses. The 3 disorders have malformations of the vertebrae in common.,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:Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Seems to be specific to breast carcinomas.,
Secreted, extracellular space, extracellular matrix . Secreted .
Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.
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