Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system.
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.
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Cell Biology of Excitable Tissue Group, Montreal Neurological Institute, McGill University, Que., Canada.
Paquet
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Nouel
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Babinski
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Séguéla
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D000328:Adult; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001921:Brain / Q000378:metabolism*; D002531:Cerebellum / Q000378:metabolism; D005260:Female; D005333:Fetus; D014644:Genetic Variation; D006801:Humans; D008214:Lymphocytes / Q000378:metabolism*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D005810:Multigene Family; D009865:Oocytes / Q000502:physiology; D009928:Organ Specificity; D012333:RNA, Messenger / Q000096:biosynthesis; D051381:Rats; D018048:Receptors, Purinergic P2 / Q000096:biosynthesis* / Q000737:chemistry*; D016415:Sequence Alignment; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic; D014982:Xenopus laevis
D046911:Macromolecular Substances; D012333:RNA, Messenger; D018048:Receptors, Purinergic P2