Two distinct cDNA sequences, corresponding to alternative isoforms of
the human nerve terminal protein SNAP-25 (synaptosomal associated prot
ein of 25 kDa), were cloned and characterized. Sequence analysis demon
strated that the two isoforms are generated by alternative splicing be
tween two distinct but homologous exons 5, a and b, each encoding 39 a
mino acids (aa). Although the two isoforms, SNAP-25a and SNAP-25b, dif
fer by only 9 aa, this domain encodes the portion of the protein that
is a substrate for post-translational fatty acylation, and therefore m
ight be important for regulating subcellular localization and membrane
targeting.