Sequence, Genomic Structure, and Chromosomal Assignment of Human DOC-2

• Published in: Genomics (San Diego, Calif.) Calif.), 1996-04, Vol.33 (2), p.207-213
• Main Authors: Albertsen, Hans M., Smith, Simon A., Melis, Roberta, Williams, Briana, Holik, Pilar, Stevens, Jeff, White, Ray
• Format: Article
• Language: English
• Subjects: Adaptor Proteins, Signal Transducing; Adaptor Proteins, Vesicular Transport; Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Caenorhabditis elegans; Cell Line; Chromosomes, Human, Pair 5; DNA, Complementary; Drosophila melanogaster; Exons; Female; Fundamental and applied biological sciences. Psychology; Genes, Tumor Suppressor; Genes. Genome; Humans; Introns; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Proteins - genetics; Rodentia; Sequence Homology, Amino Acid; Tumor Suppressor Proteins
• ISSN: 0888-7543; 1089-8646
• DOI: 10.1006/geno.1996.0185

DOC-2 is a human gene originally identified as a 767-bp cDNA fragment isolated from normal ovarian epithelial cells by differential display against ovarian carcinoma cells. We have now determined the complete cDNA sequence of the 3.2-kb DOC-2 transcript and localized the gene to chromosome 5. A 12.5-kb genomic fragment at the 5′-end of DOC-2 has also been sequenced, revealing the intron–exon structure of the first eight exons (788 bases) of the DOC-2 gene. Translation of the DOC-2 cDNA predicts a hydrophobic protein of 770 amino acid residues with a molecular weight of 82.5 kDa. Comparison of the DNA and amino acid sequences of DOC-2 to publicly accessible sequence databases revealed 83% identity to p96, a murine protein of similar size, thought to be a mitogen-responsive phosphoprotein. In addition, about 45% identity was observed between the first 140 N-terminal residues of DOC-2 and theCaenorhabditas elegansM110.5 andDrosophila melanogasterDab genes.