Adgrg2
entrez
237175
canonical
uniprot
Q8CJ12
canonical
ensembl
ENSMUSG00000031298
resolver
ensp
ENSMUSP00000108019
resolver
ensp
ENSMUSP00000108020
resolver
ensp
ENSMUSP00000108021
resolver
ensp
ENSMUSP00000108023
resolver
ensp
ENSMUSP00000108024
resolver
ensp
ENSMUSP00000108027
resolver
ensp
ENSMUSP00000331930
resolver
enst
ENSMUST00000112401
resolver
genesymbol
Adgrg2
resolver
genesymbol_syn
Gpr64
resolver
genesymbol_syn
Me6
resolver
uniprot
A0A0J9YRV1
resolver
uniprot
A2AHP8
resolver
uniprot
A2AHP9
resolver
uniprot
A2AHQ0
resolver
uniprot
A2AHQ3
resolver
uniprot
Q14AX7
resolver
uniprot
Q14BH6
resolver
uniprot
Q8BL10
resolver
uniprot
Q8CJ08
resolver
uniprot
Q8CJ09
resolver
uniprot
Q8CJ10
resolver
uniprot_entry
A0A0J9YRV1_MOUSE
resolver
uniprot_entry
AGRG2_MOUSE
resolver
uniprot_entry
Q14AX7_MOUSE
resolver
uniprot_entry
Q14BH6_MOUSE
resolver
uniprot_sec
A2AHP8
resolver
uniprot_sec
A2AHP9
resolver
uniprot_sec
A2AHQ0
resolver
uniprot_sec
A2AHQ3
resolver
uniprot_sec
Q8BL10
resolver
uniprot_sec
Q8CJ08
resolver
uniprot_sec
Q8CJ09
resolver
uniprot_sec
Q8CJ10
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 (PubMed:35418677). 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:35418677). The cleaved GAIN-B and N-terminal domains can then dissociate from the rest of the receptor (PubMed:35418677). Deoxycorticosterone (DOC) acts as an antagonist of ADGRG2 (PubMed:35982227). {ECO:0000255|PROSITE-ProRule:PRU00098, ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227}.
uniprot
proteins
amino_acid_sequence
MLFSGGQYSPVGRPEEVLLIYKIFLVIICFHVILVTSLKENGNSSLLSPSAESSLVSLIPYSNGTPDAASEVLSTLNKTEKSKITIVKTFNASGVKSQRNICNLSSLCNDSVFFRGEIVFQHDEDHNVTQNQDTANGTFAGVLSLSELKRSELNKTLQTLSETYFIVCATAEAQSTVNCTFTVKLNETMNVCAMMVTFQTVQIRPMEQCCCSPRTPCPSSPEELEKLQCELQDPIVCLADQPHGPPLSSSSKPVVPQATIISHVASDFSLAEPLDHALMTPSTPSLTQESNLPSPQPTIPLASSPATDLPVQSVVVSSLPQTDLSHTLSPVQSSIPSPTTPAPSVPTELVTISTPPGETVVNTSTVSDLEAQVSQMEKALSLGSLEPNLAGEMVNRVSKLLHSPPALLAPLAQRLLKVVDAIGLQLNFSSTTISLTSPSLALAVIRVNASNFNTTTFAAQDPTNLQVSLETPPPENSIGAITLPSSLMNNLPANDVELASRIQFNFFETPALFQDPSLENLTLISYVISSSVTNMTIKNLTRNVTVALKHINPSPDDLTVKCVFWDLGRNGGKGGWSSDGCSVKDKRMNETICTCSHLTSFGILLDLSRTSLPPSQMMALTFITYIGCGLSSIFLSVTLVTYIAFEKIRRDYPSKILIQLCAALLLLNLIFLLDSWIALYNTRGFCIAVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTYIRKYILKFCIVGWGIPAVVVSIVLTISPDNYGIGSYGKFPNGTPDDFCWINSNVVFYITVVGYFCVIFLLNVSMFIVVLVQLCRIKKKKQLGAQRKTSIQDLRSIAGLTFLLGITWGFAFFAWGPVNVTFMYLFAIFNTLQGFFIFIFYCAAKENVRKQWRRYLCCGKLRLAENSDWSKTATNGLKKQTVNQGVSSSSNSLQSSCNSTNSTTLLVNSDCSVHASGNGNASTERNGVSFSVQNGDVCLHDLTGKQHMFSDKEDSCNGKSRIALRRTSKRGSLHFIEQM
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for steroid hormones, such as dehydroepiandrosterone (DHEA; also named 3beta-hydroxyandrost-5-en-17-one) and androstenedione (PubMed:35982227). Involved in a signal transduction pathway controlling epididymal function and male fertility (PubMed:15367682). 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:35982227). ADGRG2 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:35982227). Also able to couple with G(q) G proteins in vitro (PubMed:35982227). May regulate fluid exchange within epididymis (PubMed:15367682). {ECO:0000269|PubMed:15367682, ECO:0000269|PubMed:35982227}.
uniprot
proteins
mass_dalton
110200
uniprot
proteins
mutagenesis
MUTAGEN 544..546; /note="VTV->ATA: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 564; /note="F->A: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 576; /note="W->A: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 599; /note="T->V,I: Increased G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 601; /note="F->A: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 605; /note="L->A: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 614; /note="P->A: Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 617; /note="M->A: Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 624; /note="T->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone. Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 667; /note="L->A: Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 671; /note="F->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 763; /note="N->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 765; /note="T->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 769; /note="F->A: Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 771; /note="W->A: Impaired G protein-coupled receptor activity."; /evidence="ECO:0000269|PubMed:35418677"; MUTAGEN 838; /note="W->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227"; MUTAGEN 842; /note="F->A: Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227"; MUTAGEN 853; /note="M->A: Strongly decreased G protein-coupled receptor activity in response to dehydroepiandrosterone. Impaired structural change induced by deoxycorticosterone."; /evidence="ECO:0000269|PubMed:35982227
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000255|PROSITE-ProRule:PRU00098}.; PTM: Highly glycosylated. {ECO:0000269|PubMed:12420295}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12420295
uniprot
proteins
pubmed
15367682
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18469038
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
35418677
uniprot
proteins
pubmed
35982227
uniprot
proteins
sequence_length
1009
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein {ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227}.
uniprot
proteins
transmembrane_region
TRANSMEM 618..640; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 656..679; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 684..709; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 729..751; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 777..802; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 824..845; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7"; TRANSMEM 851..872; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:35418677, ECO:0000269|PubMed:35982227, ECO:0007744|PDB:7WUI, ECO:0007744|PDB:7WUQ, ECO:0007744|PDB:7XKD, ECO:0007744|PDB:7XKE, ECO:0007744|PDB:7XKF, ECO:0007744|PDB:7YP7
uniprot
proteins