cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region

• Published in: Genomics (San Diego, Calif.) Calif.), 1996-08, Vol.35 (3), p.600-602
• Main Authors: ANDO, A, KIKUTI, Y. Y, INOKO, H, SHIGENARI, A, KAWATA, H, OKAMOTO, N, SHIINA, T, CHEN, L, IKEMURA, T, ABE, K, KIMURA, M
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Cation Transport Proteins; Cell Line; Centromere; Chromosomes, Human, Pair 6; Cloning, Molecular; DNA, Complementary; Fundamental and applied biological sciences. Psychology; Gene Dosage; Genes. Genome; Histocompatibility Antigens - genetics; HLA Antigens - genetics; Humans; Membrane Proteins - genetics; Mice; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Oxidoreductases; Proteins - genetics; Sequence Homology, Amino Acid
• ISSN: 0888-7543; 1089-8646
• DOI: 10.1006/geno.1996.0405

cDNA clones corresponding to the HKE4 and HKE6 genes at the centromeric end of the HLA region on human chromosome 6p21.3 were isolated and characterized. The predicted amino acid sequences of HKE4 and HKE6 exhibited 81.5 and 85.6% identity to the mouse homologues, Ke4 and Ke6, respectively. HKE4 may encode a membrane protein with histidine-rich charge clusters. HKE6 possesses remarkable amino acid sequence conservation with several bacterial proteins with oxidoreductase function and also shows significant homology with the two unique functional domains containing the nucleotide cofactor binding site and the consensus motif characteristic of the members of the superfamily of short-chain alcohol dehydrogenases such as human and rat steroid and prostaglandin dehydrogenases.