Plasmodium falciparum, the causative agent of malaria, relies on a complex 
protein-secretion system for protein targeting into numerous subcellular 
destinations. Recently, a homologue of the Golgi re-assembly stacking protein 
(GRASP) was identified and used to characterise the Golgi organisation in this 
parasite. Here, we report on the presence of a splice variant that leads to the 
expression of a GRASP isoform. Although the first GRASP protein (GRASP1) relies 
on a well-conserved myristoylation motif, the variant (GRASP2) displays a 
different N-terminus, similar to GRASPs found in fungi. Phylogenetic analyses 
between GRASP proteins of numerous taxa point to an independent evolution of the 
unusual N-terminus that could reflect unique requirements for Golgi-dependent 
protein sorting and organelle biogenesis in P. falciparum. Golgi association of 
GRASP2 depends on the hydrophobic N-terminus that resembles a signal anchor, 
leading to a unique mode of Golgi targeting and membrane attachment.