Latrophilin 1 is a protein that in humans is encoded by the ADGRL1 gene.[5][6] It is a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.[7][8][9]
ADGRL1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | ADGRL1, CIRL1, CL1, LEC2, LPHN1, adhesion G protein-coupled receptor L1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 616416 MGI: 1929461 HomoloGene: 8951 GeneCards: ADGRL1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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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.[6] Latrophilin-1 also binds glucose and possibly other carbohydrates because of its lectin domain.[10] It may be involved in mediating glucose and energy balance as shown recently..[10]
This article incorporates text from the United States National Library of Medicine, which is in the public domain.