Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. Trimer of identical chains each containing 190 kDa of non-triple-helical sequences. The triple-helical tail is stabilized by disulfide bonds at each end. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.