The chicken oestrogen receptor sequence: homology with v-erbA and the human oestrogen and glucocorticoid receptors

EMBO J. 1986 May;5(5):891-7.

Abstract

A chicken oviduct cDNA clone containing the complete open reading frame of the oestrogen receptor (ER) has been isolated and sequenced. The mol. wt of the predicted 589-amino acid protein is approximately 66 kd which is very close to that of the human ER. Comparison of the human and chicken amino acid sequences shows that 80% of their amino acids are identical. There are three highly conserved regions; the second and third of which probably represent the DNA- and hormone-binding domains of the receptor. The putative DNA-binding domain is characterised by its high cysteine and basic amino acid content, and the hormone-binding domain by its overall hydrophobicity. These two domains of homology are also present in the human glucocorticoid receptor (GR) and the product of the avian erythroblastosis virus (AEV) gene, v-erbA, indicating that c-erbA, the cellular counterpart of v-erbA, belongs to a multigene family of transcriptional regulatory proteins which bind steroid-related ligands. The first highly conserved ER region is not present in the truncated v-erbA gene, but shares some homology with the N-terminal end of the GR. The function of the v-erbA gene product is discussed in relation to its homology with the ER and GR sequences.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chickens
  • Cloning, Molecular
  • DNA / analysis
  • Female
  • Genes*
  • Humans
  • Nucleic Acid Hybridization
  • Oncogenes*
  • Oviducts / metabolism
  • Receptors, Estrogen / genetics*
  • Receptors, Glucocorticoid / genetics*
  • Sequence Homology, Nucleic Acid
  • Species Specificity

Substances

  • Receptors, Estrogen
  • Receptors, Glucocorticoid
  • DNA

Associated data

  • GENBANK/X03805