Chaoptin, a cell surface glycoprotein required for Drosophila photoreceptor cell morphogenesis, contains a repeat motif found in yeast and human.

Chaoptin is a photoreceptor cell-specific membrane protein. Analysis of chaoptin mutants demonstrates that this glycoprotein plays a critical role in photoreceptor cell morphogenesis. We have deduced chaoptin's primary structure from the cDNA sequence and examined its membrane topology. Chaoptin is largely composed of 41 potentially amphipathic repeats. Remarkably homologous repeats have been reported in both yeast and human, suggesting their general importance as a structural and/or functional motif. Chaoptin synthesized in vitro is associated with rough endoplasmic reticulum microsomal membrane in an integral fashion, consistent with its extraction characteristics in vivo. The resistance to proteolytic digestion of in vitro synthesized and processed chaoptin suggests that it is primarily localized to the extracellular leaflet of the lipid bilayer. These data are consistent with the proposal that chaoptin is involved in the adhesion between photoreceptor cell membranes.