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      Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene.

      Neuron
      Amino Acid Sequence, Animals, Ankyrins, Blood Proteins, chemistry, Blotting, Western, Calcium Channels, Calmodulin, metabolism, Calmodulin-Binding Proteins, genetics, Chromosome Mapping, Cloning, Molecular, DNA, Drosophila Proteins, Drosophila melanogaster, Gene Expression, Genes, Membrane Proteins, Molecular Sequence Data, Nucleic Acid Hybridization, Photoreceptor Cells, physiology, Protein Conformation, Sequence Alignment, Transient Receptor Potential Channels

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          Abstract

          We have isolated a number of Drosophila cDNAs on the basis of their encoding calmodulin-binding proteins. A full-length cDNA clone corresponding to one of these genes has been cloned and sequenced. Conservation of amino acid sequence and tissue-specific expression are observed between this gene and the transient receptor potential (trp) gene. We propose the name transient receptor potential-like (trpl) to describe this newly isolated gene. The trpl protein contains two possible calmodulin-binding sites, six transmembrane regions, and a sequence homologous to an ankyrin-like repeat. Structurally, the trpl and trp proteins resemble cation channel proteins, particularly the brain isoform of the voltage-sensitive Ca2+ channel. The identification of a protein similar to the trp gene product, yet also able to bind Ca2+/calmodulin, allows for a reinterpretation of the phenotype of the trp mutations and suggests that both genes may encode light-sensitive ion channels.

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