Open Access Articles- Top Results for LPHN1


SymbolsLPHN1 ; CIRL1; CL1; LEC2
External IDsMGI1929461 HomoloGene8951 IUPHAR: 206 GeneCards: LPHN1 Gene
RNA expression pattern
File:PBB GE LPHN1 203488 at tn.png
File:PBB GE LPHN1 219145 at tn.png
File:PBB GE LPHN1 47560 at tn.png
More reference expression data
RefSeq (mRNA)NM_001008701NM_181039
RefSeq (protein)NP_001008701NP_851382
Location (UCSC)Chr 19:
14.26 – 14.32 Mb
Chr 8:
83.9 – 83.94 Mb
PubMed search[1][2]

Latrophilin-1 is a protein that in humans is encoded by the LPHN1 gene.[1][2] 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.[3][4][5]


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.[2]

See also


  1. ^ Hayflick JS (Jan 2001). "A family of heptahelical receptors with adhesion-like domains: a marriage between two super families". J Recept Signal Transduct Res 20 (2–3): 119–31. PMID 10994649. doi:10.3109/10799890009150640. 
  2. ^ a b "Entrez Gene: LPHN1 latrophilin 1". 
  3. ^ Stacey M, Yona S (2011). AdhesionGPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. ISBN 1-4419-7912-3. 
  4. ^ Fredriksson R, Lagerstrom MC, Hoglund PJ, Schioth HB (Nov 2002). "Novel human G protein-coupled receptors with long N-terminals containing GPS domains and Ser/Thr-rich regions". FEBS Lett 531 (3): 407–14. PMID 12435584. doi:10.1016/S0014-5793(02)03574-3. 
  5. ^ 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". EMBO J. 31 (6): 1364–78. PMC 3321182. PMID 22333914. doi:10.1038/emboj.2012.26. 

Further reading


This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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