Abstract
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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cloning, Molecular
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DNA / genetics
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DNA / isolation & purification
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Drosophila / genetics*
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Drosophila Proteins*
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Humans
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Molecular Sequence Data
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Molecular Weight
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Multigene Family*
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Protein Biosynthesis
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Protein-Tyrosine Kinases / genetics*
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Proto-Oncogene Mas
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Proto-Oncogene Proteins / biosynthesis
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Proto-Oncogene Proteins / genetics*
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Proto-Oncogene Proteins / isolation & purification
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Proto-Oncogene Proteins c-ets
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Proto-Oncogenes*
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Sequence Homology, Amino Acid
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Transcription Factors*
Substances
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Drosophila Proteins
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MAS1 protein, human
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Proto-Oncogene Mas
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-ets
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Transcription Factors
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Ets97D protein, Drosophila
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DNA
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Protein-Tyrosine Kinases