Latrophilins (Latrophilin1-3) are members of the adhesion G-protein coupled receptor subfamily. Like all GPCRs, Latrophilins have seven transmembrane domains and are distinguished by a large extracellular N-terminal tail and a large intracellular C-terminal tail. The N-terminus has several cell adhesion domains and undergoes proteolysis after synthesis, while the C-terminal has various consensus post-translational sites like phosphorylation and palmitoylation. In addition, Latrophilins undergo alternative splicing.nLatrophilin-1 was discovered by its ability to bind α-Latrotoxin (α-LTX), a toxin isolated from the black widow spider venom. α-LTX induces exocytosis by creating a Ca2+ influx in the presynaptic membrane. α-LTX can also stimulate small vesicle exocytosis in a Ca2+ independent manner. Three receptors have been found to bind α-LTX. Of the three, Latrophilins are responsible for the Ca2+-independent effects of α-LTX2. The binding of α-LTX to Latrophilin-1 increases exocytosis of neurotransmitters
