A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS2) cleaves the propeptides of type I and II collagen prior to fibril assembly. ADAM-TS2 does not act on type III collagen. ADAM-TS2 also plays a role in development that is independent of its role in collagen biosynthesis. ADAM-TS2 cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln. It is expressed at high level in skin, bone, tendon and aorta and at low levels in thymus and brain. Defects in ADAMTS2 are the cause of Ehlers-Danlos syndrome type 7C (EDS7C). EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity.