GPR64
entrez
10149
canonical
uniprot
Q8IZP9
canonical
ensembl
ENSG00000173698
resolver
ensp
ENSP00000349015
resolver
ensp
ENSP00000350152
resolver
ensp
ENSP00000350680
resolver
ensp
ENSP00000353421
resolver
ensp
ENSP00000369198
resolver
ensp
ENSP00000369202
resolver
ensp
ENSP00000369205
resolver
ensp
ENSP00000369207
resolver
ensp
ENSP00000539069
resolver
ensp
ENSP00000586603
resolver
ensp
ENSP00000586609
resolver
ensp
ENSP00000586611
resolver
genesymbol
ADGRG2
resolver
genesymbol
GPR64
resolver
genesymbol_syn
GPR64
resolver
genesymbol_syn
HE6
resolver
genesymbol_syn
TM7LN2
resolver
hgnc
HGNC:4516
resolver
uniprot
A8K4P7
resolver
uniprot
B1AWB3
resolver
uniprot
B1AWB4
resolver
uniprot
B1AWB6
resolver
uniprot
B1AWB7
resolver
uniprot
O00406
resolver
uniprot
Q14CE0
resolver
uniprot
Q499H0
resolver
uniprot
Q8IWT2
resolver
uniprot
Q8IZE4
resolver
uniprot
Q8IZE5
resolver
uniprot
Q8IZE6
resolver
uniprot
Q8IZE7
resolver
uniprot
Q8IZP3
resolver
uniprot
Q8IZP4
resolver
uniprot_entry
A8K4P7_HUMAN
resolver
uniprot_entry
AGRG2_HUMAN
resolver
uniprot_entry
Q499H0_HUMAN
resolver
uniprot_sec
B1AWB3
resolver
uniprot_sec
B1AWB4
resolver
uniprot_sec
B1AWB6
resolver
uniprot_sec
B1AWB7
resolver
uniprot_sec
O00406
resolver
uniprot_sec
Q14CE0
resolver
uniprot_sec
Q8IWT2
resolver
uniprot_sec
Q8IZE4
resolver
uniprot_sec
Q8IZE5
resolver
uniprot_sec
Q8IZE6
resolver
uniprot_sec
Q8IZE7
resolver
uniprot_sec
Q8IZP3
resolver
uniprot_sec
Q8IZP4
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 (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). Deoxycorticosterone (DOC) acts as an antagonist of ADGRG2 (PubMed:35982227). {ECO:0000250|UniProtKB:Q8CJ12, ECO:0000269|PubMed:35982227}.
uniprot
proteins
amino_acid_sequence
MVFSVRQCGHVGRTEEVLLTFKIFLVIICLHVVLVTSLEEDTDNSSLSPPPAKLSVVSFAPSSNGTPEVETTSLNDVTLSLLPSNETEKTKITIVKTFNASGVKPQRNICNLSSICNDSAFFRGEIMFQYDKESTVPQNQHITNGTLTGVLSLSELKRSELNKTLQTLSETYFIMCATAEAQSTLNCTFTIKLNNTMNACAVIAALERVKIRPMEHCCCSVRIPCPSSPEELEKLQCDLQDPIVCLADHPRGPPFSSSQSIPVVPRATVLSQVPKATSFAEPPDYSPVTHNVPSPIGEIQPLSPQPSAPIASSPAIDMPPQSETISSPMPQTHVSGTPPPVKASFSSPTVSAPANVNTTSAPPVQTDIVNTSSISDLENQVLQMEKALSLGSLEPNLAGEMINQVSRLLHSPPDMLAPLAQRLLKVVDDIGLQLNFSNTTISLTSPSLALAVIRVNASSFNTTTFVAQDPANLQVSLETQAPENSIGTITLPSSLMNNLPAHDMELASRVQFNFFETPALFQDPSLENLSLISYVISSSVANLTVRNLTRNVTVTLKHINPSQDELTVRCVFWDLGRNGGRGGWSDNGCSVKDRRLNETICTCSHLTSFGVLLDLSRTSVLPAQMMALTFITYIGCGLSSIFLSVTLVTYIAFEKIRRDYPSKILIQLCAALLLLNLVFLLDSWIALYKMQGLCISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTYIRKYILKFCIVGWGVPAVVVTIILTISPDNYGLGSYGKFPNGSPDDFCWINNNAVFYITVVGYFCVIFLLNVSMFIVVLVQLCRIKKKKQLGAQRKTSIQDLRSIAGLTFLLGITWGFAFFAWGPVNVTFMYLFAIFNTLQGFFIFIFYCVAKENVRKQWRRYLCCGKLRLAENSDWSKTATNGLKKQTVNQGVSSSSNSLQSSSNSTNSTTLLVNNDCSVHASGNGNASTERNGVSFSVQNGDVCLHDFTGKQHMFNEKEDSCNGKGRMALRRTSKRGSLHFIEQM
uniprot
proteins
disease_involvement
DISEASE: Congenital bilateral aplasia of the vas deferens, X-linked (CBAVDX) [MIM:300985]: A disease characterized by bilateral absence of vas deferens, obstructive azoospermia, and infertility. {ECO:0000269|PubMed:27476656, ECO:0000269|PubMed:30389958, ECO:0000269|PubMed:31845523, ECO:0000269|PubMed:32314195, ECO:0000269|PubMed:37273165}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:29393851, PubMed:35982227, PubMed:39884271). Involved in a signal transduction pathway controlling epididymal function and male fertility (PubMed:29393851). 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:33303626, PubMed:34234254). ADGRG2 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:29393851, PubMed:34234254). Also able to couple with G(q) G proteins in vitro (PubMed:29393851). Together with CFTR, required to promote fluid reabsorption within efferent ductule (PubMed:29393851). {ECO:0000269|PubMed:29393851, ECO:0000269|PubMed:33303626, ECO:0000269|PubMed:34234254, ECO:0000269|PubMed:35982227, ECO:0000269|PubMed:39884271}.
uniprot
proteins
mass_dalton
111593
uniprot
proteins
mutagenesis
MUTAGEN 679; /note="F->A: Decreased activation by dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:39884271"; MUTAGEN 705; /note="L->A: Decreased activation by dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:39884271"; MUTAGEN 720; /note="Y->A: Impaired ability to activate G-alpha protein G(s) without affecting ability to activate G(q)."; /evidence="ECO:0000269|PubMed:29393851"; MUTAGEN 727; /note="F->A: Impaired ability to activate G-alpha protein G(s) without affecting ability to activate G(q)."; /evidence="ECO:0000269|PubMed:29393851"; MUTAGEN 730; /note="Y->A: Impaired ability to activate G-alpha protein G(q) without affecting ability to activate G(s)."; /evidence="ECO:0000269|PubMed:29393851"; MUTAGEN 779..780; /note="WI->AA: Accelerated degradation; reduced expression to the cell surface; reduced ability to activate G-alpha G(s)."; /evidence="ECO:0000269|PubMed:34234254"; MUTAGEN 779; /note="W->A: Accelerated degradation; reduced expression to the cell surface; reduced ability to activate G-alpha G(s)."; /evidence="ECO:0000269|PubMed:34234254"; MUTAGEN 780; /note="I->A: Accelerated degradation; reduced expression to the cell surface; reduced ability to activate G-alpha G(s)."; /evidence="ECO:0000269|PubMed:34234254"; MUTAGEN 786; /note="F->A: Increased ability to activate G proteins."; /evidence="ECO:0000269|PubMed:33303626"; MUTAGEN 787; /note="Y->A: Increased ability to activate G proteins."; /evidence="ECO:0000269|PubMed:33303626"; MUTAGEN 790; /note="V->A: Decreased ability to activate G proteins."; /evidence="ECO:0000269|PubMed:33303626"; MUTAGEN 794; /note="F->A: Decreased ability to activate G proteins."; /evidence="ECO:0000269|PubMed:33303626"; MUTAGEN 825..826; /note="RK->EE: Impaired ability to activate G-alpha protein G(q) without affecting ability to activate G(s)."; /evidence="ECO:0000269|PubMed:29393851"; MUTAGEN 846; /note="W->A: Decreased activation by dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:39884271"; MUTAGEN 864; /note="F->M: Decreased activation by dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:39884271"; MUTAGEN 868; /note="N->A: Decreased activation by dehydroepiandrosterone."; /evidence="ECO:0000269|PubMed:39884271
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
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
18469038
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23092983
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23338946
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
27476656
uniprot
proteins
pubmed
28397838
uniprot
proteins
pubmed
29393851
uniprot
proteins
pubmed
30389958
uniprot
proteins
pubmed
31845523
uniprot
proteins
pubmed
32314195
uniprot
proteins
pubmed
33303626
uniprot
proteins
pubmed
34234254
uniprot
proteins
pubmed
35982227
uniprot
proteins
pubmed
37273165
uniprot
proteins
pubmed
39884271
uniprot
proteins
pubmed
9150425
uniprot
proteins
sequence_length
1017
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12420295, ECO:0000269|PubMed:29393851, ECO:0000269|PubMed:32314195, ECO:0000269|PubMed:33303626, ECO:0000269|PubMed:34234254}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 628..648; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 668..688; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 694..714; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 738..758; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 790..810; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 835..855; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 858..878; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins