Metalloprotease which has proteolytic activity against the proteoglycan VCAN, cleaving it at the 'Glu-1401-|-1402-Ala' site (PubMed:24220035). Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (PubMed:23233679). Binds 1 zinc ion per subunit. At 10.5 dpc, strongly and specifically expressed in the developing heart tubes (PubMed:24220035). By 13.5 dpc, widely expressed including in the perichondrium in the developing autopod, brain, ear, whisker follicles, vertebral column and epidermis (PubMed:24220035). Also localizes to the myocardium of the developing right atrium, the bulbous cordis and the airway epithelia of the main bronchiole in the lung bud at 11.5 dpc, the vertebral column and dorsal root ganglia at 14.5 dpc, and the developing hind limb at 15.5 dpc (PubMed:24220035). In the adult colon, highly expressed in the muscularis externa (inner circular smooth muscle and outer longitudinal smooth muscle), muscularis mucosa, submucosal glands, crypt, villi epithelial cells, goblet cells and lamina propria (PubMed:24220035). In embryonic skeletal muscle, significantly increased levels between 13.5 dpc and 15.5 dpc with maximal expression observed at 15.5 dpc (PubMed:23233679). Decreased levels in postnatal skeletal muscle (PubMed:23233679). In myoblasts, up-regulated soon after induction of myoblast differentiation (PubMed:23233679). The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. 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 (PubMed:24220035). 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 (By similarity). Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL (By similarity). Fucosylation mediates the efficient secretion of ADAMTS family members (By similarity). Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs (By similarity). Also N-glycosylated (PubMed:24220035). These other glycosylations can also facilitate secretion (By similarity).