Cleaves the large aggregating proteoglycans, aggrecan (at the '1838-Glu-|-Ala-1839' site) and versican (at the '1428-Glu-|-Ala-1429' site). Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos. Binds 1 zinc ion per subunit. Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle. The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities. 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 GON domain mediates protease-independent function in ER to Golgi transport. The precursor is cleaved by a furin endopeptidase. N-glycosylated (PubMed:12514189). 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). May result from the retention of an intron in the cDNA leading to a prematurate stop codon.