ADGRL3
entrez
23284
canonical
uniprot
Q9HAR2
canonical
ensembl
ENSG00000150471
resolver
ensp
ENSP00000420931
resolver
ensp
ENSP00000421372
resolver
ensp
ENSP00000421627
resolver
ensp
ENSP00000422533
resolver
ensp
ENSP00000423388
resolver
ensp
ENSP00000423434
resolver
ensp
ENSP00000423787
resolver
ensp
ENSP00000424120
resolver
ensp
ENSP00000424258
resolver
ensp
ENSP00000425033
resolver
ensp
ENSP00000507980
resolver
ensp
ENSP00000552240
resolver
enst
ENST00000506720
resolver
enst
ENST00000507625
resolver
enst
ENST00000509896
resolver
enst
ENST00000511324
resolver
enst
ENST00000683033
resolver
genesymbol
ADGRL3
resolver
genesymbol_syn
KIAA0768
resolver
genesymbol_syn
LEC3
resolver
genesymbol_syn
LPHN3
resolver
hgnc
HGNC:20974
resolver
uniprot
A0A804HKL8
resolver
uniprot
B7Z2G2
resolver
uniprot
E7ESV6
resolver
uniprot
E7EUP0
resolver
uniprot
E7EUW2
resolver
uniprot
E7EVD6
resolver
uniprot
E9PE04
resolver
uniprot
O94867
resolver
uniprot
Q9NWK5
resolver
uniprot_entry
A0A804HKL8_HUMAN
resolver
uniprot_entry
AGRL3_HUMAN
resolver
uniprot_entry
B7Z2G2_HUMAN
resolver
uniprot_entry
E7ESV6_HUMAN
resolver
uniprot_entry
E7EUP0_HUMAN
resolver
uniprot_entry
E7EUW2_HUMAN
resolver
uniprot_entry
E7EVD6_HUMAN
resolver
uniprot_sec
E9PE04
resolver
uniprot_sec
O94867
resolver
uniprot_sec
Q9NWK5
resolver
activity_regulation
ACTIVITY REGULATION: Forms a heterodimer of 2 chains generated by proteolytic processing that remain associated through non-covalent interactions mediated by the GAIN-B domain (PubMed:35418682). In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation (PubMed:35418682). On activation, the Stachel moves into the 7 transmembrane region and adopts a twisted hook-shaped configuration that forms contacts within the receptor, leading to coupling of a G-alpha protein, which activates signaling (PubMed:35418682). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:35418682). {ECO:0000269|PubMed:35418682}.
uniprot
proteins
amino_acid_sequence
MWPSQLLIFMMLLAPIIHAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGQAHHGQVSYISPPIHLDSELERPSVKDISTTGPLGMGSTTTSTTLRTTTLSPGRSTTPSVSGRRNRSTSTPSPAVEVLDDMTTHLPSASSQIPALEESCEAVEAREIMWFKTRQGQIAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLHTVEESAFVLADNLLKTDIVRENTDNIKLEVARLSTEGNLEDLKFPENMGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEALSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNREGLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNLMNKLVNNLGSGREDDAIVLDDATSFNHEESLGLELIHEESDAPLLPPRVYSTENHQPHHYTRRRIPQDHSESFFPLLTNEHTEDLQSPHRDSLYTSMPTLAGVAATESVTTSTQTEPPPAKCGDAEDVYYKSMPNLGSRNHVHQLHTYYQLGRGSSDGFIVPPNKDGTPPEGSSKGPAHLVTSL
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (PubMed:35418682). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:35418682). ADGRL3 is coupled with different classes of G alpha proteins, such as G(12)/G(13), G(s), G(i) or G(q), depending on the context (PubMed:35418682). Coupling to G(12)/G(13) G proteins, which mediates the activation Rho small GTPases is the most efficient (PubMed:35418682). Following G protein-coupled receptor activation, associates with cell adhesion molecules that are expressed at the surface of adjacent cells to direct synapse specificity (PubMed:26235030). Specifically mediates the establishment of Schaffer-collateral synapses formed by CA3-region axons on CA1-region pyramidal neurons in the hippocampus (By similarity). Localizes to postsynaptic spines in excitatory synapses in the S.oriens and S.radiatum and interacts with presynaptic cell adhesion molecules FLRT3 and TENM2, promoting synapse formation (By similarity). Plays a role in the development of glutamatergic synapses in the cortex (By similarity). Important in determining the connectivity rates between the principal neurons in the cortex (By similarity). {ECO:0000250|UniProtKB:Q80TS3, ECO:0000269|PubMed:26235030, ECO:0000269|PubMed:35418682}.; FUNCTION: [Isoform 1]: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. Isoform 1 is specifically coupled to G(s) G proteins and mediates activation of adenylate cyclase activity. Following G protein-coupled receptor activation, undergoes liquid-liquid phase transition, associates with (1) cell adhesion molecules that are expressed at the surface of adjacent cells, as well as (2) PDZ-containing proteins, such as SHANK3 and DLG4, in the cytoplasm to direct synapse formation. {ECO:0000250|UniProtKB:Q80TS3}.
uniprot
proteins
mass_dalton
161812
uniprot
proteins
mutagenesis
MUTAGEN 249..252; /note="YHDT->AHAA: Strongly reduces FLRT3 binding. Abolishes FLRT3 binding; when associated with A-308."; /evidence="ECO:0000269|PubMed:26235030"; MUTAGEN 308; /note="R->A: Abolishes FLRT3 binding; when associated with 249-A--A-252."; /evidence="ECO:0000269|PubMed:26235030"; MUTAGEN 844; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 847; /note="L->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 914; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 938; /note="F->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 1000; /note="W->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682"; MUTAGEN 1068; /note="W->A: Strongly decreased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418682
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {ECO:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
protein_family
LN-TM7 subfamily
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
21184580
uniprot
proteins
pubmed
26235030
uniprot
proteins
pubmed
35418682
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1447
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26235030}; Multi-pass membrane protein {ECO:0000269|PubMed:35418682}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q80TS3}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction {ECO:0000250|UniProtKB:Q80TS3}.
uniprot
proteins
transmembrane_region
TRANSMEM 863..888; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 897..918; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 927..950; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 968..990; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 1006..1027; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 1054..1073; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7"; TRANSMEM 1079..1104; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418682, ECO:0007744|PDB:7SF7
uniprot
proteins