Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system

FEBS Lett. 1997 Nov 24;418(1-2):195-9. doi: 10.1016/s0014-5793(97)01380-x.


A novel member of the ionotropic ATP receptor gene family has been identified in human brain. This 422 amino acid long P2X receptor subunit has 62% sequence identity with rat P2X5. Several characteristic motifs of ATP-gated channels are present in its primary structure, but this P2X5-related subunit displays a single transmembrane domain. Heterologous expression of chimeric subunits containing the C-terminal domain of rat P2X5 leads to the formation of desensitizing functional ATP-gated channels in Xenopus oocytes. The developmentally regulated mRNA, found in two splicing variant forms, is expressed at high levels in brain and immune system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Brain / metabolism*
  • Cerebellum / metabolism
  • Female
  • Fetus
  • Genetic Variation
  • Humans
  • Lymphocytes / metabolism*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Multigene Family
  • Oocytes / physiology
  • Organ Specificity
  • RNA, Messenger / biosynthesis
  • Rats
  • Receptors, Purinergic P2 / biosynthesis*
  • Receptors, Purinergic P2 / chemistry*
  • Sequence Alignment
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Transcription, Genetic
  • Xenopus laevis


  • Macromolecular Substances
  • RNA, Messenger
  • Receptors, Purinergic P2

Associated data

  • GENBANK/AF016709