By screening retinal cDNA libraries for photoreceptor-specifically expressed genes we have isolated and sequenced a cDNA clone encoding the rhodopsin (Rh6) of a subset of R8 photoreceptor cells of the Drosophila compound eye. Compared to the other visual pigments of Drosophila, this rhodopsin is equally homologous to Rh1 and Rh2 (51% amino acid identity) but shows only 32% and 33% amino acid identity with Rh3 and Rh4, respectively. The open reading frame codes for a protein of 369 amino acids (MW = 41691). The primary structure of Rh6 displays sites typical for rhodopsin molecules in general, for example, a chromophore binding site in transmembrane domain VII, sequence motifs in the intracellular loops 2 and 3 required for the binding of a heterotrimeric G-protein, and a glycosylation site near the N-terminus which seems to be important for protein transport and maturation. Since R8 cells are founder cells in the developing compound eye, the isolation of a rhodopsin gene expressed in these cells may aid the understanding of terminal differentiation of photoreceptor cells.
Huber, A., Schulz, S., Bentrop, J., Groell, C., Wolfrum, U., & Paulsen, R. (1997). Molecular cloning of Drosophila Rh6 rhodopsin: The visual pigment of a subset of R8 photoreceptor cells. FEBS Letters, 406(1–2), 6–10. https://doi.org/10.1016/S0014-5793(97)00210-X