CLONING AND SEQUENCE-ANALYSIS OF CDNA-ENCODING RABBIT VITAMIN-D-BINDING PROTEIN (GC-GLOBULIN)

The cDNA sequence of rabbit vitamin D-binding protein (DBP) was determ ined by sequencing clones isolated by immune-screening and PCR amplifi cation from a rabbit liver cDNA library. The 1641-nucleotide sequence included the 5' untranslated region and extended to the poly(A) tail. It encoded a protein of 460 amino acid residues in addition to a signa l sequence of 16 residues, and had 84%, 79% and 78% sequence identitie s with human, rat and mouse DBP cDNA, respectively. In comparison with DBP amino acid sequences of other species, there are at least four he terogeneous regions. In contrast, a putative actin binding domain was conserved in the evolution process.