The Drosophila EGF Receptor Gene Homolog: Conservation of Both Hormone Binding and Kinase Domains

Cell. 1985 Mar;40(3):599-607. doi: 10.1016/0092-8674(85)90208-9.

Abstract

Chicken v-erB probe was used to isolate a unique clone of Drosophila melanogaster DNA. It maps by in situ hybridization to position 57F on chromosome 2. A complete nucleotide sequence of the coding region has been obtained. The putative Drosophila EGF receptor protein is similar in overall organization to the human homolog. It shows three distinct domains: an extracellular putative EGF binding domain, a hydrophobic transmembrane region, and a cytoplasmic kinase domain. The overall amino acid homology is 41% in the extracellular domain and 55% in the kinase domain. Two cysteine-rich regions, a hallmark of the human ligand-binding domain, have also been conserved. Fusion of the coding sequences of the kinase and extracellular domains generating the receptor gene must have occurred over 800 million years ago.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacteriophages / genetics
  • Base Sequence
  • Biological Evolution
  • Chickens / genetics
  • Chromosome Mapping
  • Cytoplasm
  • DNA, Recombinant
  • Drosophila melanogaster / genetics*
  • Epidermal Growth Factor / metabolism*
  • ErbB Receptors
  • Humans
  • Nucleic Acid Hybridization
  • Phosphorylation
  • Protein Kinases / genetics*
  • Protein-Tyrosine Kinases
  • Receptors, Cell Surface / genetics*
  • Receptors, Cell Surface / metabolism

Substances

  • DNA, Recombinant
  • Receptors, Cell Surface
  • Epidermal Growth Factor
  • Protein Kinases
  • ErbB Receptors
  • Protein-Tyrosine Kinases

Associated data

  • GENBANK/K03054