Q8JZZ7
uniprot
Q8JZZ7
canonical
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 (By similarity). 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:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
amino_acid_sequence
MVSSGCRMRSLWFIIIISFSPSTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYSKMLVFVCPGTLKAIVDSPCIYEAEQKSGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETAYDKRAASNAFMICGVLYVVRSVYQDNESEAGKNTIDYIYNTRLSRGEYVDVPFPNQYQYIAAVDYNPRDNQLYVWNNNFILRYSLEFGPPDPAQVPTTAVTITSSAELFKTTISTTSSASQRGPVSSTAAGPQDGSRGTKPPPAVSTTKIPPVTNIFPLPERFCEALDWKGIKWPQTQRGMMVERPCPKGTRGTASYLCMASTGTWNPKGPDLSNCTSHWVNQLAQKIRSGENAASLANELAKHTKGHVFAGDVSSSVRLMEQLVDILDAQLQELKPSEKDSAGRSYNKLQKREKTCRAYLKAIVDTVDNLLRAEALESWKHMNSSEQAHTATMLLDTLEEGAFVLADNLLEPTRVSMPTENIVLEVAVLSTEGQVQDFKFPLGLKGLGSSIQLSANTVKQNSRNGLAKLVFIIYRSLGQFLSTENATIKLGADLMGRNSTIAVNSPVISVSINKESSRVYLTDPVLFTLPHIDPDNYFNANCSFWNYSERTMMGYWSTQGCKLVDTNKTRTTCACSHLTNFAILMAHREIAYKDGVHHLLLTVITWVGIVVSLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTKYTIACPVFAGLLHFFFLAAFSWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTVQACWLHVDNYFIWSFIGPVTFIILLNIIFLVITLCKMVKHSNTLKPDSSRLENINNYRVCDGYYNTDLPGYEDNKPFIKSWVLGAFALLCLLGLTWSFGLLFVNEETVVMAYLFTAFNAFQGLFIFIFHCALQKKVRKEYGKCFRHWYCCGGLPTESPHSSVKASTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPAFNSPGHSLNNARDTSAMDTLPLNGNFNNSYSLRKADYHDGVQVVDCGLSLNDTAFEKMIISELVHNNLRGGNKTHNLELKLPVKPVIGGSSSEDDAIVADASSLMHGDNPGLEFRHKELEAPLIPQRTHSLLYQPQKKVKPEATDSYVSQLTAEADDHLQSPNRDSLYTSMPNLRDSPYPESSPDMAEDLSPSRRSENEDIYYKSMPNLGAGRHLHMCYQISRGNSDGYIIPINKEGCIPEGDVREGQMQLVTSL
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (PubMed:28972101, PubMed:30792275). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (By similarity). 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:24273166, PubMed:30792275). Specifically mediates the establishment of perforant-path synapses on CA1-region pyramidal neurons in the hippocampus (PubMed:28972101, PubMed:30792275). Localizes to postsynaptic spines in excitatory synapses in the S.lacunosum-moleculare and interacts with presynaptic cell adhesion molecules, such as teneurins, promoting synapse formation (PubMed:30792275). {ECO:0000250|UniProtKB:Q80TS3, ECO:0000269|PubMed:24273166, ECO:0000269|PubMed:28972101, ECO:0000269|PubMed:30792275}.
uniprot
proteins
mass_dalton
166577
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
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24273166
uniprot
proteins
pubmed
28972101
uniprot
proteins
pubmed
30792275
uniprot
proteins
sequence_length
1487
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:28972101, ECO:0000269|PubMed:30792275}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 856..876; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 885..905; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 912..932; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 956..976; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 995..1015; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1065..1085; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1091..1111; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins