Latrophilin-1 Rabbit Polyclonal Antibody

This gene encodes a member of the latrophilin subfamily of G-protein coupled receptors (GPCR) . Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. Latrophilin-1 has been shown to recruit the neurotoxin from black widow spider venom, alpha-latrotoxin, to the synapse plasma membrane. Alternative splicing results in multiple variants encoding distinct isoforms.[provided by RefSeq, Oct 2008], domain:The extracellular domain coupled to the a single transmembrane region are sufficient for full responsiveness to alpha-latrotoxin., function:Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor propably implicated in the regulation of exocytosis., PTM:Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus., similarity:Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily., similarity:Contains 1 GPS domain., similarity:Contains 1 olfactomedin-like domain., similarity:Contains 1 SUEL-type lectin domain., subunit:Forms a heterodimer, consisting of a large extracellular region (p120) non-covalently linked to a seven-transmembrane moiety (p85) . Interacts with syntaxin and with proteins of the SHANK family via the PDZ domain.