Molecular characterization and structural organization of D-elg, an ets proto-oncogene-related gene of Drosophila.
We have continued the molecular analysis of D-elg, a member of the Drosophila ets gene family. Based on the characterization of cDNA and genomic sequences, the D-elg gene contains five exons and four introns and produces a mRNA with an open reading frame of 464 amino acids. Consistent with this analysis, in vitro translation of a near full-length D-elg cRNA yields a protein with a molecular weight of approximately 56 kDa. D-elg shows significant homology to other ets proteins in the amino-terminal A domain and strong homology in the carboxy-terminal ETS domain. The D-elg protein is most similar to the alpha-subunit of the mouse GA-binding protein.
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Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.
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Smyth
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Watson
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D004330:Drosophila / Q000235:genetics*; D029721:Drosophila Proteins; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D005810:Multigene Family; D014176:Protein Biosynthesis; D011505:Protein-Tyrosine Kinases / Q000235:genetics*; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D050783:Proto-Oncogene Proteins c-ets; D011519:Proto-Oncogenes; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
D029721:Drosophila Proteins; C000715470:MAS1 protein, human; D000090063:Proto-Oncogene Mas; D011518:Proto-Oncogene Proteins; D050783:Proto-Oncogene Proteins c-ets; D014157:Transcription Factors; C070138:Ets97D protein, Drosophila; D004247:DNA; D011505:Protein-Tyrosine Kinases