Adgrd1
entrez
243277
canonical
uniprot
Q80T32
canonical
ensembl
ENSMUSG00000044017
resolver
ensp
ENSMUSP00000060307
resolver
ensp
ENSMUSP00000121217
resolver
enst
ENSMUST00000056617
resolver
enst
ENSMUST00000156437
resolver
genesymbol
Adgrd1
resolver
genesymbol_syn
Gpr133
resolver
uniprot
A0A0G2JDA8
resolver
uniprot
B2RXC3
resolver
uniprot
B2RXV6
resolver
uniprot
Q8BW80
resolver
uniprot_entry
A0A0G2JDA8_MOUSE
resolver
uniprot_entry
AGRD1_MOUSE
resolver
uniprot_entry
B2RXV6_MOUSE
resolver
uniprot_sec
B2RXC3
resolver
uniprot_sec
Q8BW80
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. 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. Interaction with ESYT1 in absence of cytosolic calcium inhibits the G protein-coupled receptor activity; interaction and inhibition is relieved when cytosolic calcium increases. {ECO:0000250|UniProtKB:Q6QNK2}.
uniprot
proteins
amino_acid_sequence
MKDLPAFPCSWVWLLWSFCSVQVCSTQPRAQEHPGFAVLASASHYWPLENVDGILELQDTTGALRTLNLTVPLSHNATFVFTNDSAYSNLSATVDIMEGKVNKGIYLKEEKGVTFLYYGTYKSSCISNPAQCGPEGVTFSFFWKTQGDQTRPAPYAYGGQVVSDGFKVCSSGGKGSVELYTRDNSMTWKATFNPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSHTYGDPHVNLVIGSEQDQTKRYENGAFDEFIIWERALTPDEIKMYFTAAIGKHALLSSTPPAMPTAHTVIPTDAYHPIITNLTEERKRFQRPGTVLRYLQNVSLRLPNKSLSEETALNLTETFLRTVGEVLLLPSWTHESEDNAMTLGLVDTIDTVMGHISSNLQSREPHVTLTGSSSTAEFTVAKVLPPALSAPHYRFPAHGHSYIEIPREALHSQAWTTIVGLLYHTMHYYLKNIHPTSTEIPEAVNCRDCLLSVASHLISLEVSPPPTLSQNLSGSPLITVHLRHKLTQKQYSDATNESNRLFLYCAFLNFSSGEGVWSSQGCALTEGNLTYSVCHCTHLTNFAILMQVVPLKLTHGHQVALSSISYVGCSLSVLCLAATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFSMEPGTVPCQVLAVLLHYFFLTAFAWMLVEGLHLYSMVIKVFGSEDSKHLYYYGIGWGCPLLICIISISSSMDSYGTSDSCWLALGSGAIWAFVGPALLVIVVNIVILVAVTRVISHISTDSYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVSDRALVFQYMFAILNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTANTKPFSSDTVNGTRPGTASTKLSPWDKSSHSAHRVDLSAV
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for androgen hormone 5alpha-dihydrotestosterone (5alpha-DHT), also named 17beta-hydroxy-5alpha-androstan-3-one, the most potent hormone among androgens (PubMed:39884271). Also activated by methenolone drug (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, such as adenylate cyclase (By similarity). ADGRD1 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (By similarity). Acts as a 5alpha-DHT receptor in muscle cells, thereby increasing intracellular cyclic AMP (cAMP) levels and enhancing muscle strength (PubMed:39884271). {ECO:0000250|UniProtKB:Q6QNK2, ECO:0000269|PubMed:39884271}.
uniprot
proteins
mass_dalton
99277
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity (By similarity). Cleavage takes place early in the secretory pathway before N-glycosylation (By similarity). {ECO:0000250|UniProtKB:Q6QNK2, 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
12679517
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
39884271
uniprot
proteins
sequence_length
903
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6QNK2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6QNK2}.
uniprot
proteins
transmembrane_region
TRANSMEM 600..620; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 633..653; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 663..683; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 702..722; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 741..761; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 790..810; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 814..834; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins