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:Metalloprotease that may play a role in the degradation of COMP.,induction:Up-regulated in articular cartilage and synovium from arthritis patients.,PTM:May be cleaved by a furin endopeptidase (By similarity). The precursor is sequentially processed.,PTM:N-glycosylated.,PTM:O-glycosylated proteoglycan. Contains chondroitin sulfate.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 1 PLAC domain.,similarity:Contains 8 TSP type-1 domains.,subcellular location:Also found associated with the external cell surface.,subunit:Interacts with COMP.,tissue specificity:Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments.,
Secreted, extracellular space, extracellular matrix . Also found associated with the external cell surface. .
Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments.