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
Orthologs
SpeciesHumanMouse
Entrez

22859

330814

Ensembl

ENSG00000072071
ENSG00000288324

ENSMUSG00000013033

UniProt

O94910

Q80TR1

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
View/Edit HumanView/Edit Mouse

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]

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

  1. 1 2 3 ENSG00000288324 GRCh38: Ensembl release 89: ENSG00000072071, ENSG00000288324 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000013033 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Hayflick JS (Jan 2001). "A family of heptahelical receptors with adhesion-like domains: a marriage between two super families". Journal of Receptor and Signal Transduction Research. 20 (2–3): 119–131. doi:10.3109/10799890009150640. PMID 10994649. S2CID 19919738.
  6. 1 2 "Entrez Gene: LPHN1 latrophilin 1".
  7. Stacey M, Yona S (2011). AdhesionGPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. ISBN 978-1-4419-7912-4.
  8. Fredriksson R, Lagerström MC, Höglund PJ, Schiöth HB (November 2002). "Novel human G protein-coupled receptors with long N-terminals containing GPS domains and Ser/Thr-rich regions". FEBS Letters. 531 (3): 407–414. doi:10.1016/S0014-5793(02)03574-3. PMID 12435584. S2CID 7449692.
  9. Araç D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Südhof TC, Brunger AT (March 2012). "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis". The EMBO Journal. 31 (6): 1364–1378. doi:10.1038/emboj.2012.26. PMC 3321182. PMID 22333914.
  10. 1 2 Chhabra KH, Bathina S, Faniyan TS, Samuel DJ, Raza MU, de Souza Cordeiro LM, et al. (September 2023). "ADGRL1 is a glucose receptor involved in mediating energy and glucose homeostasis". Diabetologia. 67 (1): 170–189. doi:10.1007/s00125-023-06010-6. PMC 10709246. PMID 37712955. S2CID 261886742.

Further reading

  • PDBe-KB provides an overview of all the structure information available in the PDB for Mouse Adhesion G protein-coupled receptor L1

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