Cleaves the propeptides of type I and II collagen prior to fibril assembly (PubMed:7622483). Does not act on type III collagen (PubMed:7622483). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form with reduced collagen-binding activity (By similarity). Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln. Binds 1 zinc ion per subunit. May belong to a multimeric complex. Binds specifically to collagen type XIV. Enzymatic activity is detected at high level in all type I collagen-rich tissues such as skin, bones, tendons and aorta and at low level in brain and thymus. The mRNA levels were disproportionately high in heart, liver, retina and muscle. The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. The N-terminus is blocked. 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). Defects in ADAMTS2 are the cause of dermatosparaxis, a recessively inherited disorder characterized by severe skin fragility and biochemically by the presence in skin of procollagen incompletely processed at the N-terminus. Has sometimes been referred to as ADAMTS3.