Proceedings of the National Academy of Sciences · 1993 · 33 citations · 24 references
Life SciencesCell BiologyMolecular BiologyCalcium HomeostasisCell SignalingGene ExpressionCalcium SignalingCalcium Transport ProteinsCalcium-binding ProteinsIntracellular Calcium SignalingPhotoreceptor PhysiologyRetinal AnatomyAmino Acid Composition AnalysisBasic Leucine Zipper DomainsCalcium Signaling In PhotoreceptorsCalcium-binding Proteins In PhototransductionCdna CloningCdna SynthesisLeucine Zipper ProteinsPhotoreceptor Cells
Monoclonal antibody 23E9 identifies a calcium-binding protein, calphotin, in photoreceptor cells of the Drosophila melanogaster compound eyes and ocelli. The antigen is restricted to a defined cytoplasmic region; it is not present in the rhabdomeres, nuclei, mitochondria, or rough endoplasmic reticulum. A corresponding cDNA recognizes a 3-kb mRNA with retinal specificity similar to the antigen and maps to band 86E/F-87A/B on chromosome 3. An open reading frame of 2595 bp encodes an estimated 85-kDa protein of unusual amino acid composition, with > 50% proline, alanine, and valine and very few basic residues. The C-terminal segment contains a leucine zipper motif uninterrupted by prolines. We found no significant similarities with the GenBank or National Biomedical Resource Foundation data bases. The location of the protein within a distinct cytoplasmic region suggests that it might function as a calcium-sequestering "sponge" to regulate the amount of free cytoplasmic calcium.
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A comprehensive set of sequence analysis programs for the VAX
John Devereux, Paul Haeberli, Oliver Smithies · Nucleic Acids Research · 1984 · 14.4K citations · Full text
Drosophila — A Practical Approach
Biochemical Education · 1987 · 1.8K citations