title: Identification and analysis of collagen alpha 1(XXI), a novel member of the FACIT collagen family.
abstract: The FACIT collagens bind to the surface of collagen fibrils linking them with other matrix molecules. Bioinformatics analysis of cDNA clone DKFZp564B052 showed that it resembled the FACIT collagens and was therefore designated collagen alpha 1(XXI). Phylogenetic analyses of the N-terminal NC3 domains of alpha 1(XXI) and other FACIT collagens showed that (i) alpha 1(XXI) clustered with the FACIT collagens; (ii) collagen alpha 1(XXI) arose before the divergence of alpha 1(XII), alpha 1(XIV) and alpha 1(XX); (iii) collagen alpha 1(XIV) derived from the C-terminal region of the NC3 domain of a collagen alpha 1(XII)-like molecule; and (iv) collagen alpha 1(XX) derived from a collagen alpha 1(XIV)-like molecule. This study provides a framework for the evolution of the FACIT collagens which will be of value in linking NC3 domains with their functions.
authors.affiliation: 2.205 Stopford Building, School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK. danny.tuckwell@man.ac.uk
authors.forename: Danny
authors.initials: D
authors.lastname: Tuckwell
mesh_terms: D000818:Animals; D019295:Computational Biology / Q000379:methods* / Q000639:trends; D030541:Databases, Genetic; D019143:Evolution, Molecular; D024021:Fibril-Associated Collagens / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D006801:Humans; D010802:Phylogeny; D017434:Protein Structure, Tertiary
chemical_list: D024021:Fibril-Associated Collagens