Adgrg1
entrez
14766
canonical
uniprot
Q8K209
canonical
ensembl
ENSMUSG00000031785
resolver
ensp
ENSMUSP00000090959
resolver
ensp
ENSMUSP00000137520
resolver
ensp
ENSMUSP00000309103
resolver
ensp
ENSMUSP00000309108
resolver
ensp
ENSMUSP00000309109
resolver
ensp
ENSMUSP00000309112
resolver
ensp
ENSMUSP00000309114
resolver
ensp
ENSMUSP00000309115
resolver
ensp
ENSMUSP00000309116
resolver
ensp
ENSMUSP00000309119
resolver
ensp
ENSMUSP00000309120
resolver
ensp
ENSMUSP00000309121
resolver
ensp
ENSMUSP00000309122
resolver
ensp
ENSMUSP00000309123
resolver
ensp
ENSMUSP00000309124
resolver
ensp
ENSMUSP00000309126
resolver
ensp
ENSMUSP00000325289
resolver
genesymbol
Adgrg1
resolver
genesymbol_syn
Cyt28
resolver
genesymbol_syn
Gpr56
resolver
uniprot
Q3UR17
resolver
uniprot
Q9QZT2
resolver
uniprot_entry
AGRG1_MOUSE
resolver
uniprot_sec
Q3UR17
resolver
uniprot_sec
Q9QZT2
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 (PubMed:31628191). 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). Activated by the small-molecule agonist, 3-alpha-acetoxydihydrodeoxygedunin (3-alpha-DOG) (PubMed:31628191). {ECO:0000250|UniProtKB:Q9Y653, ECO:0000269|PubMed:31628191}.
uniprot
proteins
amino_acid_sequence
MAVQVLRQMVYFLLSLFSLVQGAHSGSPREDFRFCGQRNQTQQSTLHYDQSSEPHIFVWNTEETLTIRAPFLAAPDIPRFFPEPRGLYHFCLYWSRHTGRLHLRYGKHDYLLSSQASRLLCFQKQEQSLKQGAPLIATSVSSWQIPQNTSLPGAPSFIFSFHNAPHKVSHNASVDMCDLKKELQQLSRYLQHPQKAAKRPTAAFISQQLQSLESKLTSVSFLGDTLSFEEDRVNATVWKLPPTAGLEDLHIHSQKEEEQSEVQAYSLLLPRAVFQQTRGRRRDDAKRLLVVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVTNLSDPVVLTFQHQPQPKNVTLQCVFWVEDPASSSTGSWSSAGCETVSRDTQTSCLCNHLTYFAVLMVSSTEVEATHKHYLTLLSYVGCVISALACVFTIAAYLCSRRKSRDYTIKVHMNLLSAVFLLDVSFLLSEPVALTGSEAACRTSAMFLHFSLLACLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSIVGWGFPVFLVTLVALVDVNNYGPIILAVRRTPERVTYPSMCWIRDSLVSYVTNLGLFSLVFLFNLAMLATMVVQILRLRPHSQNWPHVLTLLGLSLVLGLPWALVFFSFASGTFQLVILYLFSIITSFQGFLIFLWYWSMRFQAQGGPSPLKNNSDSAKLPISSGSTSSSRI
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for steroid hormone 17alpha-hydroxypregnenolone (17-OH), which is involved in cell adhesion and cell-cell interactions (PubMed:31628191, PubMed:39389061). 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 RhoA pathway (PubMed:39389061). ADGRG1 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:18378689, PubMed:33097663, PubMed:39389061). Acts as a potent suppressor of ferroptosis: binding to 17-OH-binding initiates signaling that down-regulates CD36 and alleviates ferroptosis-induced liver injury (PubMed:39389061). Ligand-binding also induces cell adhesion activity via association with proteins such as collagen III/COL3A1 and TGM2 (By similarity). Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells (PubMed:18509043). Involved in cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination: association with COL3A1 in the developing brain inhibits neuronal migration via activation of the RhoA pathway (PubMed:19515912, PubMed:21768377, PubMed:24531968). Together with TGM2, acts as a regulator of myelination and myelin repair in oligodendrocyte precursor cells (PubMed:29809138). Acts as a hemostatic sensor of shear force: G protein-coupled receptor signaling is activated in response to shear force in platelets, promoting G(13) G protein signaling, and platelet shape change and aggregation in a COL3A1-dependent manner (PubMed:33097663). Acts as an inhibitor of VEGFA production thereby inhibiting angiogenesis through a signaling pathway mediated by PRKCA (By similarity). Plays a role in the maintenance of hematopoietic stem cells in bone marrow niche (PubMed:23478665). Plays an essential role in testis development (PubMed:20981830). {ECO:0000250|UniProtKB:Q9Y653, ECO:0000269|PubMed:18378689, ECO:0000269|PubMed:18509043, ECO:0000269|PubMed:19515912, ECO:0000269|PubMed:20981830, ECO:0000269|PubMed:21768377, ECO:0000269|PubMed:23478665, ECO:0000269|PubMed:24531968, ECO:0000269|PubMed:29809138, ECO:0000269|PubMed:31628191, ECO:0000269|PubMed:33097663, ECO:0000269|PubMed:39389061}.; FUNCTION: [Isoform 2]: Adhesion G protein-coupled receptor (aGPCR) for phosphatidylserine, which is involved in microglia-mediated synapse pruning during development (PubMed:32452062). Required to maintain appropriate synaptic numbers in several brain regions in a time- and circuit-dependent fashion: phosphatidylserine-binding acts as a 'eat-me' signal for apoptotic cells, leading to microglial engulfment of phosphatidylserine-positive synapses (PubMed:32452062). {ECO:0000269|PubMed:32452062}.
uniprot
proteins
mass_dalton
77255
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="R->Q,W: Reduced cell surface localization."; /evidence="ECO:0000269|PubMed:17576745, ECO:0000269|PubMed:22238662"; MUTAGEN 88; /note="Y->C: Reduced cell surface localization."; /evidence="ECO:0000269|PubMed:17576745, ECO:0000269|PubMed:22238662"; MUTAGEN 89; /note="H->A: Decreased ability to promote expression of myelin basic protein (mbp)."; /evidence="ECO:0000269|PubMed:27657451"; MUTAGEN 91; /note="C->S: Reduced cell surface localization."; /evidence="ECO:0000269|PubMed:17576745, ECO:0000269|PubMed:22238662"; MUTAGEN 121; /note="C->S: Does not affect ability to promote expression of myelin basic protein (mbp); when associated with S-177."; /evidence="ECO:0000269|PubMed:27657451"; MUTAGEN 150; /note="S->A: Does not affect ability to promote expression of myelin basic protein (mbp)."; /evidence="ECO:0000269|PubMed:27657451"; MUTAGEN 177; /note="C->S: Does not affect ability to promote expression of myelin basic protein (mbp); when associated with S-121."; /evidence="ECO:0000269|PubMed:27657451"; MUTAGEN 346; /note="C->S: Abolishes proteolytic cleavage and cell surface localization."; /evidence="ECO:0000269|PubMed:17576745"; MUTAGEN 349; /note="W->S: Abolishes proteolytic cleavage and cell surface localization."; /evidence="ECO:0000269|PubMed:17576745"; MUTAGEN 381; /note="H->S: Impaired autoproteolytic processing without affecting localization to the cell membrane. Decreased ability to promote expression of myelin basic protein (mbp)."; /evidence="ECO:0000269|PubMed:27657451, ECO:0000269|PubMed:31628191"; MUTAGEN 382; /note="L->A: Impaired autoproteolytic processing without affection localization to the cell membrane."; /evidence="ECO:0000269|PubMed:31628191
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically cleaved into 2 fragments; the large extracellular N-terminal fragment and the membroune-bound C-terminal fragment predominantly remain associated and non-covalently linked. {ECO:0000269|PubMed:22238662, ECO:0000269|PubMed:31628191}.; PTM: N-glycosylated. The secreted ADGRG1 N-terminal fragment is heavily glycosylated. {ECO:0000269|PubMed:17576745}.; PTM: Ubiquitinated. Undergoes polyubiquitination upon activation. {ECO:0000250|UniProtKB:Q9Y653}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
protein_family
LN-TM7 subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17576745
uniprot
proteins
pubmed
18378689
uniprot
proteins
pubmed
18509043
uniprot
proteins
pubmed
19515912
uniprot
proteins
pubmed
20981830
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21768377
uniprot
proteins
pubmed
22238662
uniprot
proteins
pubmed
23478665
uniprot
proteins
pubmed
24531968
uniprot
proteins
pubmed
27068534
uniprot
proteins
pubmed
27657451
uniprot
proteins
pubmed
29809138
uniprot
proteins
pubmed
31628191
uniprot
proteins
pubmed
32452062
uniprot
proteins
pubmed
33097663
uniprot
proteins
pubmed
39389061
uniprot
proteins
sequence_length
687
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17576745, ECO:0000269|PubMed:22238662}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor G1, N-terminal fragment]: Secreted {ECO:0000250|UniProtKB:Q9Y653}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor G1, C-terminal fragment]: Membrane raft {ECO:0000250|UniProtKB:Q9Y653}. Note=Interaction with its ligand COL3A1 leads to the release of ADGRG1 NT from the membrane and triggers the association of ADGRG1 CT with lipid rafts. {ECO:0000250|UniProtKB:Q9Y653}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:27657451}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 403..423; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 443..463; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 472..492; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 513..533; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 571..591; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 604..624; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 631..651; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins