The N-terminal sequences encoded by the mouse and rat Kalrn B promoters are identical, as are the N-terminal sequences encoded by the mouse and rat Kalrn C promoters. Most of the full-length Kalirin isoforms in the NAc will begin with the more hydrophobic N-terminal sequence encoded by the Kalrn C promoter [48]. The functional consequences of this difference have not yet been explored, but the proximity of this short sequence to the Sec14p domain, which is known to bind phosphatidylinositol-3-phosphate [24], suggests that future studies might identify an important role for the N-terminus of Kalirin.
