The complete primary structure of the bovine alpha 1(X) collagen chain was determined by nucleotide sequencing of cDNA clones. The overlapping cDNA clones encode 3144 bp with a 5′-terminal untranslated region of 148 bp, a 2025 bp reading frame and a 3′-terminal untranslated region of 971 bp. This represents the first complete sequence of a mammalian type X collagen cDNA and has allowed a number of informative comparisons to be made with the previously published chick alpha 1(X) sequence. The primary translation products of both bovine and chick type X collagen are 674 amino acid residues in length and there is a 73.3% identity at the amino acid level (67.8% at the base level). Sequence analyses reveal that the greatest degree of identity between the two species occurs within the triple-helical domain and the C-terminal non-collagenous domain, whereas the identity within the N-terminal non-collagenous domain is markedly lower. The interchain disulphide-bonding observed previously within the triple helix of bovine type X collagen is explained by the presence of two cysteine residues within an imperfection of the triple-helical domain encoded by -Gly-Xaa-Cys-Xaa-Yaa-Cys-Xaa-Yaa-Gly-. Southern blot analyses of bovine genomic DNA demonstrate that the bovine type X collagen gene is likely to have a condensed structure, similar to that of the chick, with at least 1.3 kb of the coding sequence being contained within one exon.
