A collagen homotrimer of alpha1(VII) chains; type VII collagen triple helices form antiparallel dimer, which in turn associate laterally to form anchoring fibrils that connect type IV collagen in the basal lamina to plaques in the underlying connective tissue.

A collagen heterotrimer containing type VIII alpha chains; [alpha1(VIII)2]alpha2(VIII) and alpha1(VIII)[alpha2(VIII)]2 trimers have been observed; type VIII collagen triple helices associate to form regular hexagonal nets.

A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils.

Any collagen polymer associated with collagen fibrils and in which the collagen monomers contain two or more relatively short triple-helical domains connected by non-triple-helical sequences; the acronym FACIT stands for fibril-associated collagen with interrupted triple helix.

Catalysis of the reaction: RS-CH2-CH(NH3+)COO- = RSH + NH3 + pyruvate.

A collagen heterotrimer containing type IX alpha chains in alpha1(IX)alpha2(IX)alpha3(IX) trimers; type IX collagen triple helices associate to form a structure that links glycosaminoglycans to type II collagen fibrils.

A collagen homotrimer of alpha1(XIV) chains; type XIV collagen triple helices may link sheet-forming or fibrillar collagens to other structures.

A collagen trimer containing alpha(XVI) chains; type XVI trimers can associate with microfibrils.

Any assembly of collagen in which the collagen chains are relatively short compared to the fibrillar collagens.

The process by which the cellular identity of auditory hair cells is acquired and determined.

The process whereby a relatively unspecialized cell acquires specialized features of an epidermal cell, any of the cells making up the epidermis.

The directed movement of hormones into, out of, within or between cells.

The modification of peptidyl-glutamic acid.

Interacting selectively with neurexins, synaptic cell surface proteins related to latrotoxin receptor, laminin and agrin. Neurexins act as cell recognition molecules at nerve terminals.