Collagen type XVI is a member of the FACIT (fibril-associated collagens with interrupted helices) collagen family. During early mouse development it occurs in many tissues and is co-distributed with the major fibrillar collagens (Lai & Chu 1996). In skin, collagen type XVI occurs in narrow zones near basement membranes at the dermo-epidermal junction (DEJ) of blood vessels (Grässel et al. 1999). In papillary dermis, the protein unexpectedly does not occur in banded collagen fibrils but as a component of specialized fibrillin-1-containing microfibrils. However, in cartilage it does not aggregate with fibrillin-1, rather it exists as a discrete population of thin, weakly-banded collagen fibrils in association with collagens II and XI (Kassner et al. 2003, 2004). Collagen XVI induces the recruitment of integrins alpha1 beta1 and alpha1 beta 2 into focal adhesion plaques, a principal step in integrin signaling (Eble et al. 2006), allowing cells to affect the architecture of the ECM networks by binding and moving ECM proteins.

Collagen type XVI is cleaved by MMP9 (Sires et al. 1995).