Sequence analysis of a full-length cDNA for the murine pro alpha 2(I) collagen chain: comparison of the derived primary structure with human pro alpha 2(I) collagen.
Comparison of the nucleotide sequence and primary structure of murine and human pro alpha 2(I) collagen indicates a high degree of homology: 87% at the nucleotide level and 87% at the amino acid level, with the greatest degree of variability in the amino- and carboxy-pro-peptide domains. The homology is greatest in the triple helical domain, repeating [Gly-X-Y]338, exhibiting 90% homology at the amino acid level, with only X and Y position residue substitutions. The X and Y residues show 86% homology between murine and human pro alpha 2(I) collagen triple helices, with no truly nonconservative substitutions.
Phillips
C L
CL
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
Morgan
A L
AL
Lever
L W
LW
Wenstrup
R J
RJ
D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011347:Procollagen / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid
D011347:Procollagen; D004247:DNA