The, S.M., Xie, X., Smyth, F., Papas, T.S., Watson, D.K., Schulz, R.A. (1992). Molecular characterization and structural organization of D-elg, an ets proto-oncogene-related gene of Drosophila. Oncogene 7: 2471--2478.
FlyBase ID
FBrf0057438
Publication Type
Research paper
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.
