Phospholipases A2 (PLA2s) are important constituents of snake venom that, depending on their amino acid composition, possess several toxic properties whose main ones are neurotoxicity, myotoxicity, cardiotoxicity and impairing of haemostasis. They are proteins of about 120 amino acids, having a structure conserved since basal metazoa, and very similar to that of mammalian secretory PLA2s. Some snake venom PLA2s are heteromultimers, others are monomers or homodimers.

In this work we analyse the sequence alignment of monomeric or homodimeric snake venom PLA2s, grouped according to their myotoxic and neurotoxic properties, and we compare this alignment with that of the most similar mammalian secretory PLA2s. We found short linear motifs, present in three regions of secretory PLA2s that can have a role in their toxic and physiological functions. This work suggests important molecular interactions of secretory PLA2s that can focus and shorten the experimental work of characterization of the mechanism of action of these proteins.