HGNC Approved Gene Symbol: COL5A3
Cytogenetic location: 19p13.2 Genomic coordinates (GRCh38): 19:9,959,561-10,010,504 (from NCBI)
Type V collagen is distributed in vertebrate tissues as a heterotrimer of 3 different polypeptide chains, alpha-1 (COL5A1, 120215), alpha-2 (COL5A1, 120190), and alpha-3 (COL5A3), a heterotrimer of 2 copies of alpha-1 and 1 copy of alpha-2, or a homotrimer of alpha-1 polypeptides. For additional background information on collagen V, see 120215.
By database searching, screening of cDNA libraries, and nested PCR, Imamura et al. (2000) cloned full-length human and mouse COL5A3 cDNAs encoding 1,745- and 1,739-amino acid proteins, respectively. COL5A3 is most similar to the fibrillar procollagens COL5A1, COL11A1 (120280), and COL11A2 (120290). Dot-blot analysis demonstrated particularly high levels of COL5A3 expression in mammary gland, high levels in placenta, uterus, fetal heart and lung, and moderately high levels in adult heart and brain. Relatively high levels of COL5A1 and COL5A2 were found in most of the same tissues, indicating the presence of heterotrimers of the collagen V alpha chains in these tissues. An exception was adult brain, in which the levels of COL5A3 were not matched by those of the other two. Northern blot analysis detected particularly high expression of an approximately 6.0-kb transcript in heart, placenta, and uterus. Smaller bands of approximately 4.2 kb and 5.5 kb were found in brain and lung, respectively. In situ hybridization of mouse embryos detected Col5a3 expression primarily in the epimysial sheaths of developing muscles and within nascent ligaments adjacent to forming bones and in joints.
By radiation hybrid analysis, Imamura et al. (2000) mapped the COL5A3 gene to chromosome 19p13.2. By interspecific backcross analysis, they mapped the mouse homolog to a region of syntenic homology on proximal chromosome 9.
Imamura, Y., Scott, I. C., Greenspan, D. S. The pro-alpha3(V) collagen chain: complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains. J. Biol. Chem. 275: 8749-8759, 2000. [PubMed: 10722718] [Full Text: https://doi.org/10.1074/jbc.275.12.8749]