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

非质量问题不退换