Adgrg3
entrez
54672
canonical
uniprot
Q8R0T6
canonical
ensembl
ENSMUSG00000060470
resolver
ensp
ENSMUSP00000051079
resolver
ensp
ENSMUSP00000200715
resolver
enst
ENSMUST00000051259
resolver
genesymbol
Adgrg3
resolver
genesymbol_syn
Gpr97
resolver
uniprot
Q3U2Q3
resolver
uniprot_entry
AGRG3_MOUSE
resolver
uniprot_sec
Q3U2Q3
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 (By similarity). {ECO:0000250|UniProtKB:Q6QNK2, ECO:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
amino_acid_sequence
MATARSLGLLFFLLLTSDEETTEEPRNVCRRLQEGHEYDTFDLNDTAQCFTKCGQSEHSPCDVGNLQRYWLNYESYLLENSMETVDMPFVKALIQNISTDVSEDLLYSLMLSQIPRQVMQGEDEPADGVRLPKSLFGALPGNRSAVRLAITVLDIGAGNVFKGPKLLEDKGSSVLNNRMVGLSVGQMHATGLSEPVEITFSHERQPPNVILTCVFWDMAKGDWDSHGCSTVPGDGRTVCRCDHLTFFALLLRPILDLATAQTLTRISQAGSAVSMIFLAFTMVLYVAFRFSLQRFKSEDAPKIHMALSISLFLLNLTFLINVGSSSQGPPASCWVRAAIFHYFLLCVFTWMGLEAFHLYLLAIRVFNTYFGHYFLKLSLLAWGLPVLVVIGAGSSNSYGVYTIRDQENRTSLELCWFQKEPALYATVHGYFLVTFLFGAVVLALVAWKIFTLPSVTAGKGQGPTWKSVLTVLGLSSLVGMTWGLAVLTPLGLSTIYVFTLLNSLQGLFIFCWFIILYFPTQSTTASSSGTARLDQAHSVSQE
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for glucocorticoid hormones such as cortisol, cortisone and 11-deoxycortisol (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). ADGRG3/GPR97 is coupled to G(o)/GNAO1 G proteins and mediates signaling by inhibiting adenylate cyclase activity (By similarity). May also signal through G-alpha(q)-proteins; additional evidence are however required to confirm this result in vivo (By similarity). Plays a role in the regulation of various processes including B-cell development, inflammation or innate immunity (PubMed:24113187, PubMed:27089991, PubMed:38345813). Regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42 (PubMed:24178298). Antibody ligation leads to the production and activation of antimicrobial mediators like reactive oxygen species (ROS) and myeloperoxidase (MPO) as well as enhanced bacteria uptake and killing by granulocytes (By similarity). Additionally, collaborates with protease-activated receptor 2/PAR2 to stimulate neutrophil-driven antimicrobial responses and endothelial cell activation (By similarity). {ECO:0000250|UniProtKB:Q86Y34, ECO:0000269|PubMed:24113187, ECO:0000269|PubMed:24178298, ECO:0000269|PubMed:27089991, ECO:0000269|PubMed:38345813}.
uniprot
proteins
mass_dalton
60072
uniprot
proteins
post_translational_modification
PTM: Autoproteolytically processed at the GPS region of the GAIN-B domain; this cleavage modulates receptor activity. {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
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
24113187
uniprot
proteins
pubmed
24178298
uniprot
proteins
pubmed
27089991
uniprot
proteins
pubmed
29531097
uniprot
proteins
pubmed
38345813
uniprot
proteins
sequence_length
542
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86Y34}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86Y34}.
uniprot
proteins
transmembrane_region
TRANSMEM 268..288; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 303..323; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 343..363; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 373..393; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 427..447; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 468..488; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 495..515; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins