Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Calcium Channels*
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DNA / genetics
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Drosophila Proteins*
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Drosophila melanogaster / genetics*
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Drosophila melanogaster / physiology
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Genes
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Inositol Phosphates / metabolism
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Insect Hormones / genetics*
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Insect Hormones / physiology
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Insect Proteins*
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Membrane Proteins / genetics*
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Membrane Proteins / physiology
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Molecular Sequence Data
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Photoreceptor Cells / physiology*
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Photoreceptor Cells / radiation effects
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Protein Conformation
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Signal Transduction*
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Transient Receptor Potential Channels
Substances
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Calcium Channels
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Drosophila Proteins
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Inositol Phosphates
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Insect Hormones
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Insect Proteins
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Membrane Proteins
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Transient Receptor Potential Channels
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trp protein, Drosophila
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DNA