Using bioinformatics analyses of the completed malaria genome sequence, we have identified a novel protein with a potential role in erythrocyte invasion. The protein (PFD0295c, ) has a predicted signal sequence and transmembrane domain and a sequence near the C-terminus of the protein shows significant similarity with Sushi domains. These domains, which exist in a wide variety of complement and adhesion proteins, have previously been shown to be involved in protein-protein and protein-ligand interactions. Orthologous genes have also been identified in the genomes of several other Plasmodium species, suggesting a conserved function for this protein in Plasmodium. Our results show that this protein is located in apical organelles and we have therefore designated the protein apical Sushi protein (ASP). We show that the expression of ASP is tightly regulated in the intraerythrocytic stages of the parasite and that it undergoes post-translational proteolytic processing. Based on our observations of timing of expression, location and proteolytic processing, we propose a role for ASP in erythrocyte invasion.