Group V sPLA(2) is unique among the family of secretory sPLA(2) enzymes in being able to bind to cell membranes through both interfacial-binding and through binding to proteoglycan. The function of group V sPLA(2) as an enzyme and its cross-talk with cPLA(2)alpha in initiating eicosanoid generation is well documented. Evidence, though, is emerging on the ability of this molecule to act as a regulator of several intracellular and extracellular pathways independently of its ability to provide arachidonic acid for eicosanoid generation, acting within the cell or as a secreted enzyme. In this article we will provide an overview of the properties of the enzyme and how they relate to our current understanding of its function.