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.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 3 TSP type-1 domains.,tissue specificity:Expressed in fetal liver and kidney, but not in any of the adult tissues examined.,
Secreted, extracellular space, extracellular matrix . Cell surface .
Expressed in fetal liver and kidney, but not in any of the adult tissues examined.
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