Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.
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.
Montell
C
C
Howard Hughes Medical Institute, University of California, Berkeley 94720.
Rubin
G M
GM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015220:Calcium Channels; D004247:DNA / Q000235:genetics; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics* / Q000502:physiology; D005796:Genes; D007295:Inositol Phosphates / Q000378:metabolism; D007301:Insect Hormones / Q000235:genetics* / Q000502:physiology; D019476:Insect Proteins; D008565:Membrane Proteins / Q000235:genetics* / Q000502:physiology; D008969:Molecular Sequence Data; D010786:Photoreceptor Cells / Q000502:physiology* / Q000528:radiation effects; D011487:Protein Conformation; D015398:Signal Transduction; D050051:Transient Receptor Potential Channels
D015220:Calcium Channels; D029721:Drosophila Proteins; D007295:Inositol Phosphates; D007301:Insect Hormones; D019476:Insect Proteins; D008565:Membrane Proteins; D050051:Transient Receptor Potential Channels; C063169:trp protein, Drosophila; D004247:DNA