Molecular cloning of a widely expressed human homologue for the <i>Drosophila trp</i>gene

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Abstract

The Drosophila transient receptor potential (trp) gene and its homologue, trpl, have been suggested to mediate calcium entry during the insect's phototransduction process. We isolated a human cDNA, human trp-1 (Htrp-1), encoding a polypeptide of 793 amino acids that is 37% identical (62% similar) to Drosophila trp and trpl. Northern analysis showed that the Htrp-1 transcript is approximately 5.5 kb and expressed in most human tissues, with higher amounts in ovary, testis, heart, and brain. Isolation of Htrp-1 suggests that a trp-type protein is present in mammals and should provide a useful tool in studying calcium-depletion induced calcium influx processes.

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Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.

Craig Montell, Gerald M Rubin (1989)

Recent studies suggest that the fly uses the inositol lipid signaling system for visual excitation and that the Drosophila transient receptor potential (trp) mutation disrupts this process subsequent to the production of IP3. In this paper, we show that trp encodes a novel 1275 amino acid protein with eight putative transmembrane segments. Immunolocalization indicates that the trp protein is expressed predominantly in the rhabdomeric membranes of the photoreceptor cells.