catalytic activity:Cleaves aggrecan at the 392-Glu-|-Ala-393 site.,cofactor:Binds 1 zinc ion per subunit.,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.,domain:The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.,function:Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 2 TSP type-1 domains.,tissue specificity:Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.,
Secreted, extracellular space, extracellular matrix .
Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.
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