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. 1993 Feb 15;90(4):1531–1535. doi: 10.1073/pnas.90.4.1531

Calphotin: a Drosophila photoreceptor cell calcium-binding protein.

J H Martin 1, S Benzer 1, M Rudnicka 1, C A Miller 1
PMCID: PMC45908  PMID: 8094559

Abstract

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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