Latrophilin 1

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

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]

PDBOrtholog search: PDBe RCSB
AliasesADGRL1, CIRL1, CL1, LEC2, LPHN1, adhesion G protein-coupled receptor L1
Quick facts ADGRL1, Available structures ...
ADGRL1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesADGRL1, CIRL1, CL1, LEC2, LPHN1, adhesion G protein-coupled receptor L1
External IDsOMIM: 616416; MGI: 1929461; HomoloGene: 8951; GeneCards: ADGRL1; OMA:ADGRL1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001008701
NM_014921

NM_181039

RefSeq (protein)

NP_001008701
NP_055736

NP_851382

Location (UCSC)Chr 19: 14.15 – 14.21 MbChr 8: 83.9 – 83.94 Mb
PubMed search[3][4]
Wikidata
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Function

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]

See also

References

Further reading

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