Primary structure and functional characterization of a Drosophila dopamine receptor with high homology to human D1/5 receptors

Recept Channels. 1994;2(2):131-41.


Members of the superfamily of G-protein coupled receptors share significant similarities in sequence and transmembrane architecture. We have isolated a Drosophila homologue of the mammalian dopamine receptor family using a low stringency hybridization approach. The deduced amino acid sequence is approximately 70% homologous to the human D1/D5 receptors. When expressed in HEK 293 cells, the Drosophila receptor stimulates cAMP production in response to dopamine application. This effect was mimicked by SKF 38393, a specific D1 receptor agonist, but inhibited by dopaminergic antagonists such as butaclamol and flupentixol. In situ hybridization revealed that the Drosophila dopamine receptor is highly expressed in the somata of the optic lobes. This suggests that the receptor might be involved in the processing of visual information and/or visual learning in invertebrates.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Consensus Sequence
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Exons
  • GTP-Binding Proteins / metabolism
  • Genes, Insect*
  • Genomic Library
  • Humans
  • In Situ Hybridization
  • Introns
  • Molecular Sequence Data
  • Receptors, Dopamine / biosynthesis
  • Receptors, Dopamine / chemistry*
  • Receptors, Dopamine / metabolism*
  • Receptors, Dopamine D1 / chemistry*
  • Restriction Mapping
  • Sequence Homology, Amino Acid
  • Transfection


  • Receptors, Dopamine
  • Receptors, Dopamine D1
  • GTP-Binding Proteins

Associated data

  • GENBANK/X77234