Abstract
The sevenless (sev) gene determines the fate of a single photoreceptor cell type in the eye of Drosophila. It encodes a putative cell-surface protein with homology to tyrosine kinases. Here we have determined the complete structure of the sev gene and have demonstrated that the role of the sev protein in this developmental decision is critically dependent on the tyrosine kinase function. In comparison with other known tyrosine kinases, the sev gene product is unique in size and structure. It is a polypeptide of 2554 amino acids with two putative transmembrane segments. A single amino acid substitution in the ATP-binding site of the putative kinase domain results in the synthesis of an inactive sev protein unable to determine cell fate.
