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Latrophilin

From Wikipedia, the free encyclopedia
G-protein coupled receptor
Protein family
Latrophilin
Identifiers
SymbolLatrophilin
PfamPF02354
InterProIPR003334
Available protein structures:
Pfam  structures /ECOD  
PDBRCSB PDB;PDBe;PDBj
PDBsumstructure summary
EGF, latrophilin and seven transmembrane domain containing 1
Identifiers
SymbolELTD1
Alt. symbolsETL
NCBI gene64123
HGNC20822
RefSeqNM_022159
UniProtQ9HBW9
Other data
LocusChr. 1p33-p32
Search for
StructuresSwiss-model
DomainsInterPro
latrophilin 1
Identifiers
SymbolLPHN1
Alt. symbolsKIAA0821, CIRL1, LEC2
NCBI gene22859
HGNC20973
RefSeqNM_014921
UniProtO94910
Other data
LocusChr. 19p13.2
Search for
StructuresSwiss-model
DomainsInterPro
latrophilin 2
Identifiers
SymbolLPHN2
Alt. symbolsLPHH1, KIAA0786, LEC1
NCBI gene23266
HGNC18582
OMIM607018
RefSeqNM_012302
UniProtO95490
Other data
LocusChr. 1p31.1
Search for
StructuresSwiss-model
DomainsInterPro
latrophilin 3
Identifiers
SymbolLPHN3
Alt. symbolsKIAA0768, LEC3
NCBI gene23284
HGNC20974
RefSeqNM_015236
UniProtQ9HAR2
Other data
LocusChr. 4q13.1
Search for
StructuresSwiss-model
DomainsInterPro

Latrophilins are a group of highly conservedG-protein coupled receptors from theadhesion G protein-coupled receptor family. These receptors were originally identified based on their ability to bind to a component ofblack widow spidervenom known asalpha-latrotoxin.[1] This conserved family of membrane proteins has up to three homologues in chordate species, including humans.[2]

The precise functions of latrophilins remain unknown.[2] Genetic defects in latrophilin genes have been associated with diseases such asattention-deficit hyperactivity disorder andcancer.[3]

Human proteins containing this domain

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See also

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References

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  1. ^Kreienkamp HJ, Soltau M, Richter D, Böckers T (2002)."Interaction of G-protein-coupled receptors with synaptic scaffolding proteins".Biochem. Soc. Trans.30 (4):464–8.doi:10.1042/BST0300464.PMID 12196116.
  2. ^abSilva, JP; Ushkaryov, YA (2010). "The Latrophilins, "Split-Personality" Receptors".Adhesion-GPCRS. Advances in Experimental Medicine and Biology. Vol. 706. pp. 59–75.doi:10.1007/978-1-4419-7913-1_5.ISBN 978-1-4419-7912-4.PMC 3145135.PMID 21618826.
  3. ^Meza-Aguilar, Diana G; Boucard, Antony A (1 January 2014)."Latrophilins updated".Biomolecular Concepts.5 (6):457–478.doi:10.1515/bmc-2014-0032.PMID 25429599.S2CID 207442054.
Neurotransmitter
Adrenergic
Purinergic
Serotonin
Other
Metabolites and
signaling molecules
Eicosanoid
Other
Peptide
Neuropeptide
Other
Miscellaneous
Taste, bitter
Orphan
Other
Adhesion
Orphan
Other
Taste, sweet
Other
Frizzled
Smoothened
Enzyme
(modulators)
ChATTooltip Choline acetyltransferase
AChETooltip Acetylcholinesterase
BChETooltip Butyrylcholinesterase
Transporter
(modulators)
CHTTooltip Choline transporter
VAChTTooltip Vesicular acetylcholine transporter
Release
(modulators)
Inhibitors
Enhancers
Retrieved from "https://en.wikipedia.org/w/index.php?title=Latrophilin&oldid=1292625166"
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