Molecular cloning of a multifunctional chicken protein acting as the prolyl 4 hydroxylase beta subunit protein disulfide isomerase and a cellular thyroid hormone binding protein comparison of complementary dna deduced amino acid sequences with those in other species

Parkkonen, T.; Kivirikko, K.I.; Pihlajaniemi, T.

Biochemical Journal 256(3): 1005-1012

1988


ISSN/ISBN: 0264-6021
Accession: 007563295

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Abstract
Several recent studies indicate that a single polypeptide may act as the .beta.-subunit of prolyl 4-hydroxylase, the enzyme protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. We report here the isolation and characterization of cDNA clones encoding this multifunctional protein in the chicken. All the coding sequences were determined on the basis of nucleotide sequencing of five cDNA clones and amino acid sequencing of the N-terminal end of the chicken .beta.-subunit. The processed polypeptide contains 493 amino acid residues, the size of the respective mRNA being about 2.7 kb. The chicken .beta.-subunit cDNA sequences were 78% homologous to the previously reported human .beta.-subunit cDNA sequences at the nucleotide level and 85% homologous at the amino acid level. The homology of the chicken .beta.-subunit sequences to those reported for bovine thyroid-hormone-binding protein and rat protein disulphide-isomerase was also 85% at the amino acid level. Primary-structure comparisons between the four species indicated that the two proposed active sites of protein disulphide-isomerase, the two Trp-Cys-Gly-His-Cys-Lys sequences, are located within highly conserved regions, which are also homologous to the active sites of a number of thioredoxins. The middle of the polypeptide has an additional conserved region 100 amino acid residues in length in which the degree of homology between the four species is 94% at the amino acid level. This long conserved region may also be important for some of the multiple functions of the protein. The four extreme C-terminal amino acids of the polypeptide in all four species are Lys-Asp-Glu-Leu, a sequence that has been suggested to function as a signal for the retention of a protein in the endoplasmic reticulum.