An adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors. Homotrimer. Wide tissue distribution; high presence in dense connective tissue in skeletal muscle. Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding. Belongs to the fibril-associated collagens with interrupted helices (FACIT) family.