This gene encodes the alpha chain of type XIX collagen, a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). Although the function of this collagen is not known, other members of this collagen family are found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. The transcript produced from this gene has an unusually large 3' UTR which has not been completely sequenced.
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Inoguchi K, Yoshioka H, Khaleduzzaman M, Ninomiya Y (1995). "The mRNA for alpha 1(XIX) collagen chain, a new member of FACITs, contains a long unusual 3' untranslated region and displays many unique splicing variants.". J. Biochem. 117 (1): 137–46. PMID7775380.
Myers JC, Yang H, D'Ippolito JA, et al. (1994). "The triple-helical region of human type XIX collagen consists of multiple collagenous subdomains and exhibits limited sequence homology to alpha 1(XVI).". J. Biol. Chem. 269 (28): 18549–57. PMID8034603.
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Sumiyoshi H, Inoguchi K, Khaleduzzaman M, et al. (1997). "Ubiquitous expression of the alpha1(XIX) collagen gene (Col19a1) during mouse embryogenesis becomes restricted to a few tissues in the adult organism.". J. Biol. Chem. 272 (27): 17104–11. doi:10.1074/jbc.272.27.17104. PMID9202028.
Khaleduzzaman M, Sumiyoshi H, Ueki Y, et al. (1998). "Structure of the human type XIX collagen (COL19A1) gene, which suggests it has arisen from an ancestor gene of the FACIT family.". Genomics. 45 (2): 304–12. doi:10.1006/geno.1997.4921. PMID9344653.
Myers JC, Li D, Amenta PS, et al. (2003). "Type XIX collagen purified from human umbilical cord is characterized by multiple sharp kinks delineating collagenous subdomains and by intermolecular aggregates via globular, disulfide-linked, and heparin-binding amino termini.". J. Biol. Chem. 278 (34): 32047–57. doi:10.1074/jbc.M304629200. PMID12788917.
Käpylä J, Jäälinoja J, Tulla M, et al. (2005). "The fibril-associated collagen IX provides a novel mechanism for cell adhesion to cartilaginous matrix.". J. Biol. Chem. 279 (49): 51677–87. doi:10.1074/jbc.M409412200. PMID15383545.