Collagen, type XVII, alpha 1 Collagen, type XVII, alpha 1 Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion. Collagen XVII is a homotrimer of three alpha1(XVII)-chains and a transmembrane protein in type II orientation. Each 180 kD a-chain contains a globular intracellular domain of approximately 70 kDa, which interacts with beta4-integrin, plectin, and BP230 and is necessary for the stable attachment of hemidesmosomes to keratin intermediate filaments. The large C-terminal ectodomain with a molecular mass of approximately 120 kDa consists of 15 collagenous
Keratin used as fluorescent markers to distinguish subsets of TECs in genetic studies of the thymus. Additionally, the baleen plates of filter-feeding whales are made of keratin. Keratins (also described as cytokeratins) are polymers of type I and type II intermediate filaments, which have only been found in the genomes of chordates (vertebrates, Amphioxus, urochordates). Nematodes and many other non-chordate animals seem to only have type VI intermediate filaments, lamins, which have a long rod domain (vs. a short rod domain for the keratins). The human genome encodes 54 functional keratin genes which are located in two clusters on chromosomes 12