Adgrl3
entrez
319387
canonical
uniprot
Q80TS3
canonical
ensembl
ENSMUSG00000037605
resolver
ensp
ENSMUSP00000072336
resolver
ensp
ENSMUSP00000112388
resolver
ensp
ENSMUSP00000112548
resolver
ensp
ENSMUSP00000112731
resolver
ensp
ENSMUSP00000112823
resolver
ensp
ENSMUSP00000113208
resolver
ensp
ENSMUSP00000113243
resolver
ensp
ENSMUSP00000113249
resolver
ensp
ENSMUSP00000113374
resolver
ensp
ENSMUSP00000113600
resolver
ensp
ENSMUSP00000113694
resolver
ensp
ENSMUSP00000113836
resolver
ensp
ENSMUSP00000234691
resolver
ensp
ENSMUSP00000234692
resolver
ensp
ENSMUSP00000234693
resolver
ensp
ENSMUSP00000234695
resolver
ensp
ENSMUSP00000234696
resolver
ensp
ENSMUSP00000234697
resolver
ensp
ENSMUSP00000234698
resolver
ensp
ENSMUSP00000234700
resolver
ensp
ENSMUSP00000234701
resolver
ensp
ENSMUSP00000234702
resolver
enst
ENSMUST00000118078
resolver
enst
ENSMUST00000118442
resolver
enst
ENSMUST00000119385
resolver
enst
ENSMUST00000120128
resolver
enst
ENSMUST00000120292
resolver
enst
ENSMUST00000120445
resolver
enst
ENSMUST00000121707
resolver
enst
ENSMUST00000122037
resolver
genesymbol
Adgrl3
resolver
genesymbol_syn
Kiaa0768
resolver
genesymbol_syn
Lec3
resolver
genesymbol_syn
Lphn3
resolver
uniprot
D3YTW7
resolver
uniprot
D3YU23
resolver
uniprot
D3YWB1
resolver
uniprot
D3Z3X6
resolver
uniprot
D3Z634
resolver
uniprot
D3Z6H7
resolver
uniprot
D3Z6H9
resolver
uniprot
D3Z6J2
resolver
uniprot
Q3UHI7
resolver
uniprot
Q3UM79
resolver
uniprot
Q504Z9
resolver
uniprot
Q5HZJ6
resolver
uniprot
Q80T56
resolver
uniprot_entry
AGRL3_MOUSE
resolver
uniprot_entry
D3YTW7_MOUSE
resolver
uniprot_entry
D3YU23_MOUSE
resolver
uniprot_entry
D3YWB1_MOUSE
resolver
uniprot_entry
D3Z3X6_MOUSE
resolver
uniprot_entry
D3Z634_MOUSE
resolver
uniprot_entry
D3Z6H7_MOUSE
resolver
uniprot_entry
D3Z6H9_MOUSE
resolver
uniprot_entry
D3Z6J2_MOUSE
resolver
uniprot_sec
Q3UHI7
resolver
uniprot_sec
Q3UM79
resolver
uniprot_sec
Q504Z9
resolver
uniprot_sec
Q5HZJ6
resolver
uniprot_sec
Q80T56
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:36244455, PubMed:39798870). In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation (By similarity). 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 (By similarity). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (By similarity). {ECO:0000250|UniProtKB:Q9HAR2, ECO:0000269|PubMed:36244455, ECO:0000269|PubMed:39798870}.
uniprot
proteins
amino_acid_sequence
MWPPQLLILTMLLAPVVHGGKHNERHPALAAPLRHAERSPGGALPPRHLLQQPAAERSTAHRGQGPRGAARGVRGPGAPGAQIAAQAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGPVHHGQVSYISPPIHLDSELERPPVRGISTTGSLGMGSTTTSTTLRTTTWNIGRSTTASLPGRRNRSTSTPSPAVEVLDDVTTHLPSAASQIPAMEESCEAVEAREIMWFKTRQGQVAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKLQKRERSCRAYVQAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLDTVEESAFVLADNLLKTDIVRENTDNIQLEVARLSTEGNLEDLKFPENMGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEAMSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNINYEDNRPFIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNREGLLNNARDTSVMDTLPLNGNHGNSYSIAGGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNMMNKLVNNLGSGSEDDAIVLDDAASFNHEESLGLELIHEESDAPLLPPRVYSTDNHQPHHYSRRRFPQDHSESFFPLLTDEHTEDLQSPHRDSLYTSMPALAGVPAADSVTTSTQTEAAAAKGGDAEDVYYKSMPNLGSRNHVHPLHAYYQLGRGSSDGFIVPPNKDGASPEGTSKGPAHLVTSL
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (PubMed:36244455, PubMed:38233523). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:36244455, PubMed:36309016). 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:32778842, PubMed:36309016, PubMed:39798870). Coupling to G(12)/G(13) G proteins, which mediates the activation Rho small GTPases is the most efficient (PubMed:32778842, PubMed:36244455). 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:22405201, PubMed:25728924, PubMed:26235031, PubMed:30792275, PubMed:39798870). Specifically mediates the establishment of Schaffer-collateral synapses formed by CA3-region axons on CA1-region pyramidal neurons in the hippocampus (PubMed:30792275). 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 (PubMed:30792275). Plays a role in the development of glutamatergic synapses in the cortex (PubMed:22405201, PubMed:24739570). Important in determining the connectivity rates between the principal neurons in the cortex (PubMed:24739570). {ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25728924, ECO:0000269|PubMed:26235031, ECO:0000269|PubMed:30792275, ECO:0000269|PubMed:32778842, ECO:0000269|PubMed:36244455, ECO:0000269|PubMed:36309016, ECO:0000269|PubMed:38233523, ECO:0000269|PubMed:39798870}.; FUNCTION: [Isoform 1]: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (PubMed:38233523). 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 (PubMed:38233523). Isoform 1 is specifically coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:38233523). 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 (PubMed:38233523). {ECO:0000269|PubMed:38233523}.; FUNCTION: [Isoform 7]: Orphan adhesion G protein-coupled receptor (aGPCR) (PubMed:38233523). 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 RhoA pathway (PubMed:38233523). Isoform 7 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:38233523). {ECO:0000269|PubMed:38233523}.
uniprot
proteins
mass_dalton
171080
uniprot
proteins
mutagenesis
MUTAGEN 244; /note="P->N: Strongly reduces FLRT2 binding; when associated with T-246."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 246; /note="R->T: Strongly reduces FLRT2 binding; when associated with N-244."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 267; /note="T->N: Strongly reduces FLRT2 binding; when associated with T-269."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 269; /note="K->T: Strongly reduces FLRT2 binding; when associated with N-267."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 292; /note="R->N: Abolishes interaction with FLRT2; when associated with T-294."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 294; /note="R->T: Abolishes interaction with FLRT2; when associated with N-292."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 317..320; /note="YHDT->AHAA: In 4A mutant; abolished binding to FLRT proteins; when associated with A-376."; /evidence="ECO:0000269|PubMed:30792275"; MUTAGEN 323; /note="Y->A: Abolishes FLRT3 binding."; /evidence="ECO:0000269|PubMed:26235031"; MUTAGEN 324; /note="R->N: Abolishes interaction with FLRT2; when associated with T-326."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 326; /note="G->T: Abolishes interaction with FLRT2; when associated with N-324."; /evidence="ECO:0000269|PubMed:25728924"; MUTAGEN 332; /note="D->A: Strongly reduces FLRT3 binding."; /evidence="ECO:0000269|PubMed:26235031"; MUTAGEN 376; /note="R->A: In 4A mutant; abolished binding to FLRT proteins; when associated with 317-A--A-321."; /evidence="ECO:0000269|PubMed:30792275"; MUTAGEN 923; /note="T->A,G: Abolished autocatalytic processing, leading to impaired G protein-coupled activity."; /evidence="ECO:0000269|PubMed:30792275, ECO:0000269|PubMed:36244455"; MUTAGEN 923; /note="T->Y: Does not affect G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 925; /note="F->A,G: Abolished autocatalytic processing, leading to abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36244455, ECO:0000269|PubMed:36309016"; MUTAGEN 926; /note="A->T: Abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 926; /note="A->V: Does not affect G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 927; /note="V->I: Does not affect G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 927; /note="V->T: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 928..929; /note="LM->AA: Abolished G protein-coupled activity without affecting autocatalytic processing."; /evidence="ECO:0000269|PubMed:36244455"; MUTAGEN 928; /note="L->A: Abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 929; /note="M->A: Abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 930; /note="Missing: Does not affect G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 931; /note="H->A: Does not affect G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 945; /note="L->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 946; /note="D->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 953; /note="I->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 995; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1000; /note="N->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1019; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1023; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1041; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1081; /note="W->F: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1090; /note="W->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1092; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1155; /note="G->F,I,T,S,A: Abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1155; /note="G->P: Decreased but not abolished G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1158; /note="W->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1162; /note="L->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1176; /note="F->A: Strongly decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016"; MUTAGEN 1180; /note="N->A: Decreased G protein-coupled receptor signaling."; /evidence="ECO:0000269|PubMed:36309016
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, ECO:0000269|PubMed:36244455, ECO:0000269|PubMed:39798870}.; PTM: O-glycosylated (major) and N-glycosylated. {ECO:0000269|PubMed:24739570}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
protein_family
LN-TM7 subfamily
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22405201
uniprot
proteins
pubmed
22575564
uniprot
proteins
pubmed
24739570
uniprot
proteins
pubmed
25728924
uniprot
proteins
pubmed
26235031
uniprot
proteins
pubmed
30792275
uniprot
proteins
pubmed
32778842
uniprot
proteins
pubmed
36244455
uniprot
proteins
pubmed
36309016
uniprot
proteins
pubmed
38233523
uniprot
proteins
pubmed
39798870
uniprot
proteins
sequence_length
1537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:36244455}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:30792275}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:22405201}. Cell junction {ECO:0000269|PubMed:22405201}.
uniprot
proteins
transmembrane_region
TRANSMEM 944..969; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 976..999; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 1007..1034; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 1049..1071; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 1087..1112; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 1143..1163; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10"; TRANSMEM 1169..1195; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:36309016, ECO:0007744|PDB:7WY5, ECO:0007744|PDB:7WY8, ECO:0007744|PDB:7WYB, ECO:0007744|PDB:7X10
uniprot
proteins