Adgrg2
entrez
266735
canonical
uniprot
Q8CJ11
canonical
ensembl
ENSRNOG00000032472
resolver
ensp
ENSRNOP00000039239
resolver
ensp
ENSRNOP00000055623
resolver
ensp
ENSRNOP00000055624
resolver
ensp
ENSRNOP00000082277
resolver
ensp
ENSRNOP00000096191
resolver
ensp
ENSRNOP00000098802
resolver
ensp
ENSRNOP00000105097
resolver
enst
ENSRNOT00000058833
resolver
enst
ENSRNOT00000058834
resolver
enst
ENSRNOT00000157644
resolver
genesymbol
Adgrg2
resolver
genesymbol_syn
Gpr64
resolver
genesymbol_syn
Re6
resolver
uniprot
A0A8L2QR31
resolver
uniprot
A0A8L2QR66
resolver
uniprot
A0ABK0LN23
resolver
uniprot
Q8CJ06
resolver
uniprot
Q8CJ07
resolver
uniprot_entry
A0A8L2QR31_RAT
resolver
uniprot_entry
A0A8L2QR66_RAT
resolver
uniprot_entry
A0ABK0LN23_RAT
resolver
uniprot_entry
AGRG2_RAT
resolver
uniprot_sec
Q8CJ06
resolver
uniprot_sec
Q8CJ07
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. Deoxycorticosterone (DOC) acts as an antagonist of ADGRG2 (By similarity). {ECO:0000250|UniProtKB:Q8CJ12, ECO:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
amino_acid_sequence
MLFSGGQYSPVGRPEEVLLIYKIFLVIICFHAILVTSLKENAGNSSLLSPSAESSLVSLVPYSNGTPDAASEVLSTLNRTEKSKITILKTFNASGVKSQRNICNLSSICSDSVFFRGEIVFQHDDHYNVTQNQDIVNSTFAGVLSLSELKRTELNKTLQTLSETYFIVCATAEAQNTLNCTFTVKLNETMNVCAMMVTFKSVQIRPMEQCCCSPRTPCPSSPEELEKLQCDLQDPIVCLADQPHGPPVSSSSKPVPVVPQATIFSHVASDFSLAEPLDHALMTSSTPSLAQETRLPSPQPTISLTSSPAIDLPVQHVVASSSLPQTDLSHTLSPVQSSIPSPTTAAPSVPEKVVAISTPPGETVVNTSSVPDLEAQVSQMEKALSLGSLEPNLAGEMVNRVSKLLHSPLALLAPLAQRLLKVVDAIGLQLNFSSTTISLTSPSLALAVIRVNASNFNTTTFAAQDPANLQVSLEAQAPKNSIGAITLPSSLMSNLPASEVELASRVQFNFFETPALFQDPSLENLSLISYVISSSVTNMTIKNLTRNVTVALKHINPSQDDLTVKCVFWDLNRNGGRGGWSSDGCSVKEKRMNETICTCSHLTSFGILLDLSRTSLPPSQMMALTFITYIGCGLSSIFLSVTLVTYIAFEKIRRDYPSKILIQLCAALLLLNLVFLLDSWIALYNARGFCISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTYIRKYILKFCIVGWGIPAVVVSIVLTISPDNYGIGSYGKFPNGTPDDFCWINSSVVFYITVVGYFCVIFLLNVSMFIVVLVQLCRIKKKKQLGAQRKTSIQDLRSIAGLTFLLGITWGFAFFAWGPVNLTFMYLFAIFNTLQGFFIFIFYCAAKENVRKQWRRYLCCGKLRLAENSDWSKTATNGLKKQTVNQGVSSSSNSLQSSCNSTNSTTLLVNSDCSVHASGNGNASTERNGVSFSVQNGDVCLHDLTGKQHMFSDKEDSCNGKSRMALRRTSKRGSLHFIEQM
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. Involved in a signal transduction pathway controlling epididymal function and male fertility. 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. ADGRG2 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity. Also able to couple with G(q) G proteins in vitro. May regulate fluid exchange within epididymis. {ECO:0000250|UniProtKB:Q8CJ12}.
uniprot
proteins
mass_dalton
110701
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
sequence_length
1013
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12420295}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 624..644; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 664..684; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 689..709; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 734..754; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 786..806; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 831..851; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 854..874; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins