| ADGRL1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ADGRL1 , CIRL1, CL1, LEC2, LPHN1, adhesion G protein-coupled receptor L1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 616416; MGI: 1929461; HomoloGene: 8951; GeneCards: ADGRL1; OMA:ADGRL1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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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]
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.