Abstract:
GPI anchors consist of three parts; protein, glycan and the phospholipids. The GPI anchored proteins work as cell surface hydrolases, protozoal antigens, adhesion molecules, mammalian antigens and involved in other significant cellular functions like dense packing of proteins on cell surface, increased protein mobility on cell surface , specific release from cell surface, control of exit from endoplasmic reticulum and toxin binding. Mutations in these proteins lead to Paroxysomal Nocturnal Haemogolbinuria and other disorders. This study was executed by combining comparative proteomics and phylogenetic approaches in order to address a cross family evolution of GPI anchor proteins from 23 different species. The results of revealed some unexplored specifics about the conserved domains GPI anchored proteins across different taxa of organisms. The results also demonstrated hierarchical assemblage based inconsistency in variation in the GPI anchored proteins
