ADGRL2
entrez
23266
canonical
uniprot
O95490
canonical
ensembl
ENSG00000117114
resolver
ensp
ENSP00000322270
resolver
ensp
ENSP00000353006
resolver
ensp
ENSP00000359748
resolver
ensp
ENSP00000359750
resolver
ensp
ENSP00000359752
resolver
ensp
ENSP00000359760
resolver
ensp
ENSP00000359763
resolver
ensp
ENSP00000397740
resolver
ensp
ENSP00000501324
resolver
ensp
ENSP00000501431
resolver
ensp
ENSP00000501462
resolver
ensp
ENSP00000501484
resolver
ensp
ENSP00000501532
resolver
ensp
ENSP00000501543
resolver
ensp
ENSP00000509478
resolver
ensp
ENSP00000525624
resolver
ensp
ENSP00000525625
resolver
ensp
ENSP00000525626
resolver
ensp
ENSP00000525627
resolver
ensp
ENSP00000525628
resolver
ensp
ENSP00000525629
resolver
ensp
ENSP00000525630
resolver
ensp
ENSP00000525631
resolver
ensp
ENSP00000525632
resolver
ensp
ENSP00000525633
resolver
ensp
ENSP00000525634
resolver
ensp
ENSP00000525635
resolver
ensp
ENSP00000525636
resolver
ensp
ENSP00000596559
resolver
ensp
ENSP00000596562
resolver
ensp
ENSP00000596564
resolver
ensp
ENSP00000611394
resolver
ensp
ENSP00000611401
resolver
ensp
ENSP00000611408
resolver
ensp
ENSP00000648986
resolver
ensp
ENSP00000648987
resolver
ensp
ENSP00000648988
resolver
ensp
ENSP00000648989
resolver
ensp
ENSP00000648990
resolver
ensp
ENSP00000784725
resolver
enst
ENST00000674208
resolver
enst
ENST00000674209
resolver
enst
ENST00000674442
resolver
enst
ENST00000686636
resolver
enst
ENST00000855574
resolver
enst
ENST00000926503
resolver
genesymbol
ADGRL2
resolver
genesymbol_syn
KIAA0786
resolver
genesymbol_syn
LEC1
resolver
genesymbol_syn
LPHH1
resolver
genesymbol_syn
LPHN2
resolver
hgnc
HGNC:18582
resolver
uniprot
A0A6I8PIV6
resolver
uniprot
A0A6I8PLG0
resolver
uniprot
A0A6I8PTT2
resolver
uniprot
A0A8I5KUX3
resolver
uniprot
A5XEI2
resolver
uniprot
B1ALT8
resolver
uniprot
B1ALT9
resolver
uniprot
B1ALU0
resolver
uniprot
B1ALU2
resolver
uniprot
B1ALU4
resolver
uniprot
B1ALU5
resolver
uniprot
B1ALU6
resolver
uniprot
O94882
resolver
uniprot
Q5VX76
resolver
uniprot
Q9UKY5
resolver
uniprot
Q9UKY6
resolver
uniprot_entry
A0A6I8PIV6_HUMAN
resolver
uniprot_entry
A0A6I8PLG0_HUMAN
resolver
uniprot_entry
A0A6I8PTT2_HUMAN
resolver
uniprot_entry
A0A8I5KUX3_HUMAN
resolver
uniprot_entry
AGRL2_HUMAN
resolver
uniprot_sec
A5XEI2
resolver
uniprot_sec
B1ALT8
resolver
uniprot_sec
B1ALT9
resolver
uniprot_sec
B1ALU0
resolver
uniprot_sec
B1ALU2
resolver
uniprot_sec
B1ALU4
resolver
uniprot_sec
B1ALU5
resolver
uniprot_sec
B1ALU6
resolver
uniprot_sec
O94882
resolver
uniprot_sec
Q5VX76
resolver
uniprot_sec
Q9UKY5
resolver
uniprot_sec
Q9UKY6
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 (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. 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. 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
MVSSGCRMRSLWFIIVISFLPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYIFVCPGTLKAIVDSPCIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETVYDKRAASNAFMICGVLYVVRSVYQDNESETGKNSIDYIYNTRLNRGEYVDVPFPNQYQYIAAVDYNPRDNQLYVWNNNFILRYSLEFGPPDPAQVPTTAVTITSSAELFKTIISTTSTTSQKGPMSTTVAGSQEGSKGTKPPPAVSTTKIPPITNIFPLPERFCEALDSKGIKWPQTQRGMMVERPCPKGTRGTASYLCMISTGTWNPKGPDLSNCTSHWVNQLAQKIRSGENAASLANELAKHTKGPVFAGDVSSSVRLMEQLVDILDAQLQELKPSEKDSAGRSYNKLQKREKTCRAYLKAIVDTVDNLLRPEALESWKHMNSSEQAHTATMLLDTLEEGAFVLADNLLEPTRVSMPTENIVLEVAVLSTEGQIQDFKFPLGIKGAGSSIQLSANTVKQNSRNGLAKLVFIIYRSLGQFLSTENATIKLGADFIGRNSTIAVNSHVISVSINKESSRVYLTDPVLFTLPHIDPDNYFNANCSFWNYSERTMMGYWSTQGCKLVDTNKTRTTCACSHLTNFAILMAHREIAYKDGVHELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTKYAIACPIFAGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLHVDNYFIWSFIGPVTFIILLNIIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGVFIFIFHCALQKKVRKEYGKCFRHSYCCGGLPTESPHSSVKASTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPVFNSPGHSLNNARDTSAMDTLPLNGNFNNSYSLHKGDYNDSVQVVDCGLSLNDTAFEKMIISELVHNNLRGSSKTHNLELTLPVKPVIGGSSSEDDAIVADASSLMHSDNPGLELHHKELEAPLIPQRTHSLLYQPQKKVKSEGTDSYVSQLTAEAEDHLQSPNRDSLYTSMPNLRDSPYPESSPDMEEDLSPSRRSENEDIYYKSMPNLGAGHQLQMCYQISRGNSDGYIIPINKEGCIPEGDVREGQMQLVTSL
uniprot
proteins
function
FUNCTION: Orphan adhesion G protein-coupled receptor (aGPCR), which mediates synapse specificity (By similarity). 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. Specifically mediates the establishment of perforant-path synapses on CA1-region pyramidal neurons in the hippocampus. 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 (By similarity). {ECO:0000250|UniProtKB:Q80TS3, ECO:0000250|UniProtKB:Q8JZZ7}.
uniprot
proteins
mass_dalton
163349
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
10030676
uniprot
proteins
pubmed
10760572
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17456239
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23647072
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1459
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q8JZZ7}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 852..872; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 881..901; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 908..928; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 953..973; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 991..1011; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 1038..1058; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 1063..1083; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins