Binds 1 zinc ion per subunit. Expressed in fetal lung, liver, and kidney and in adult brain, prostate, submaxillary gland, and endothelium. 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. The precursor is cleaved by a furin endopeptidase. Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). The disease is caused by variants affecting the gene represented in this entry. Variant Leu-179 has been originally reported as disease-causing mutation in a patient with Knobloch syndrome (PubMed:21862674). It has been subsequently shown that Knobloch syndrome in the patient was due to an intronic mutation in COL18A1. Variant Leu-179 is, therefore, not responsible for the disease phenotype (PubMed:23667181). Truncated N-terminus. Probable intron retention. Aberrant splicing.