ADGRG3
entrez
222487
canonical
uniprot
Q86Y34
canonical
ensembl
ENSG00000182885
resolver
ensp
ENSP00000332900
resolver
ensp
ENSP00000404803
resolver
ensp
ENSP00000456409
resolver
ensp
ENSP00000528918
resolver
ensp
ENSP00000615198
resolver
ensp
ENSP00000797113
resolver
enst
ENST00000333493
resolver
enst
ENST00000450388
resolver
enst
ENST00000567991
resolver
genesymbol
ADGRG3
resolver
genesymbol_syn
GPR97
resolver
genesymbol_syn
PGR26
resolver
hgnc
HGNC:13728
resolver
uniprot
B4DVW2
resolver
uniprot
F8W8F7
resolver
uniprot
H3BRU4
resolver
uniprot
Q6ZMF4
resolver
uniprot
Q86SL9
resolver
uniprot
Q8IZF1
resolver
uniprot_entry
AGRG3_HUMAN
resolver
uniprot_entry
B4DVW2_HUMAN
resolver
uniprot_entry
F8W8F7_HUMAN
resolver
uniprot_entry
H3BRU4_HUMAN
resolver
uniprot_sec
Q6ZMF4
resolver
uniprot_sec
Q86SL9
resolver
uniprot_sec
Q8IZF1
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). {ECO:0000250|UniProtKB:Q6QNK2, ECO:0000255|PROSITE-ProRule:PRU00098}.
uniprot
proteins
amino_acid_sequence
MATPRGLGALLLLLLLPTSGQEKPTEGPRNTCLGSNNMYDIFNLNDKALCFTKCRQSGSDSCNVENLQRYWLNYEAHLMKEGLTQKVNTPFLKALVQNLSTNTAEDFYFSLEPSQVPRQVMKDEDKPPDRVRLPKSLFRSLPGNRSVVRLAVTILDIGPGTLFKGPRLGLGDGSGVLNNRLVGLSVGQMHVTKLAEPLEIVFSHQRPPPNMTLTCVFWDVTKGTTGDWSSEGCSTEVRPEGTVCCCDHLTFFALLLRPTLDQSTVHILTRISQAGCGVSMIFLAFTIILYAFLRLSRERFKSEDAPKIHVALGGSLFLLNLAFLVNVGSGSKGSDAACWARGAVFHYFLLCAFTWMGLEAFHLYLLAVRVFNTYFGHYFLKLSLVGWGLPALMVIGTGSANSYGLYTIRDRENRTSLELCWFREGTTMYALYITVHGYFLITFLFGMVVLALVVWKIFTLSRATAVKERGKNRKKVLTLLGLSSLVGVTWGLAIFTPLGLSTVYIFALFNSLQGVFICCWFTILYLPSQSTTVSSSTARLDQAHSASQE
uniprot
proteins
function
FUNCTION: Adhesion G protein-coupled receptor (aGPCR) for glucocorticoid hormones such as cortisol, cortisone and 11-deoxycortisol (PubMed:33408414). 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:33408414). ADGRG3/GPR97 is coupled to G(o)/GNAO1 G proteins and mediates signaling by inhibiting adenylate cyclase activity (PubMed:33408414). May also signal through G-alpha(q)-proteins; additional evidence are however required to confirm this result in vivo (PubMed:22575658). Plays a role in the regulation of various processes including B-cell development, inflammation or innate immunity (PubMed:30559745, PubMed:36302784). 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 (PubMed:30559745). Additionally, collaborates with protease-activated receptor 2/PAR2 to stimulate neutrophil-driven antimicrobial responses and endothelial cell activation (PubMed:36302784). {ECO:0000269|PubMed:22575658, ECO:0000269|PubMed:24178298, ECO:0000269|PubMed:30559745, ECO:0000269|PubMed:33408414, ECO:0000269|PubMed:36302784}.
uniprot
proteins
mass_dalton
60861
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}.; PTM: O- and N-glycosylated. {ECO:0000269|PubMed:30559745}.
uniprot
proteins
protein_family
Adhesion G protein-coupled receptor (ADGR) subfamily
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12435584
uniprot
proteins
pubmed
12679517
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22575658
uniprot
proteins
pubmed
24178298
uniprot
proteins
pubmed
25713288
uniprot
proteins
pubmed
30559745
uniprot
proteins
pubmed
33408414
uniprot
proteins
pubmed
36302784
uniprot
proteins
sequence_length
549
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22575658}; Multi-pass membrane protein {ECO:0000269|PubMed:33408414}.
uniprot
proteins
transmembrane_region
TRANSMEM 271..295; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 305..326; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 339..364; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 379..400; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 429..454; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 475..495; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77"; TRANSMEM 502..525; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:33408414, ECO:0007744|PDB:7D76, ECO:0007744|PDB:7D77
uniprot
proteins