Johard_1999_Comp.Biochem.Physiol.B.Biochem.Mol.Biol_122_63

SNAP-25 (synaptosome-associated protein of 25 kD) is attached to the intracellular side of presynaptic membranes where it serves as a target receptor for the vesicle docking machinery prior to release of neurotransmitter. SNAP-25 displays a high degree of sequence conservation between vertebrates and Drosophila melanogaster. To obtain more information about conserved regions of SNAP-25, we have isolated cDNA clones from the cockroach Leucophaea maderae. One clone (Lm1) encoded a full-length SNAP-25 protein and its deduced amino acid sequence is 77% identical to Drosophila SNAP-25. Surprisingly, the cockroach protein is 17 amino acids shorter than Drosophila SNAP-25 at the carboxy terminus. Four other cDNA clones encode parts of SNAP-25 and each clone has distinct characteristics, including amino acid replacements and unique carboxy termini. Thus, the highly conserved protein SNAP-25 displays unexpected sequence variability in the cockroach that may indicate specialized SNAP-25 isoforms.