GPR84
entrez
53831
canonical
uniprot
Q9NQS5
canonical
ensembl
ENSG00000139572
resolver
ensp
ENSP00000267015
resolver
ensp
ENSP00000450310
resolver
ensp
ENSP00000549336
resolver
enst
ENST00000267015
resolver
enst
ENST00000551809
resolver
enst
ENST00000879277
resolver
genesymbol
GPR84
resolver
genesymbol_syn
EX33
resolver
hgnc
HGNC:4535
resolver
uniprot
B6V9G7
resolver
uniprot_entry
GPR84_HUMAN
resolver
uniprot_sec
B6V9G7
resolver
amino_acid_sequence
MWNSSDANFSCYHESVLGYRYVAVSWGVVVAVTGTVGNVLTLLALAIQPKLRTRFNLLIANLTLADLLYCTLLQPFSVDTYLHLHWRTGATFCRVFGLLLFASNSVSILTLCLIALGRYLLIAHPKLFPQVFSAKGIVLALVSTWVVGVASFAPLWPIYILVPVVCTCSFDRIRGRPYTTILMGIYFVLGLSSVGIFYCLIHRQVKRAAQALDQYKLRQASIHSNHVARTDEAMPGRFQELDSRLASGGPSEGISSEPVSAATTQTLEGDSSEVGDQINSKRAKQMAEKSPPEASAKAQPIKGARRAPDSSSEFGKVTRMCFAVFLCFALSYIPFLLLNILDARVQAPRVVHMLAANLTWLNGCINPVLYAAMNRQFRQAYGSILKRGPRSFHRLH
uniprot
proteins
function
FUNCTION: G protein-coupled receptor that responds endogenously to dietary fatty acids or nutrient, specifically medium-chain free fatty acid (FFA) with carbon chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid (C11:0) and lauric acid (C12:0) are the most potent agonists (PubMed:16966319). In immune cells, functions as a pro-inflammatory receptor via 6-OAU and promotes the expression of pro-inflammatory mediators such as TNFalpha, IL-6 and IL-12B as well as stimulating chemotactic responses through activation of signaling mediators AKT, ERK and NF-kappa-B (By similarity). In addition, triggers increased bacterial adhesion and phagocytosis in macrophages and regulates pro-inflammatory function via enhancing NLRP3 inflammasome activation (By similarity). Also plays an important role in inflammation by modulating neutrophil functions (By similarity). Mechanistically, promotes neutrophil chemotaxis, reactive oxygen species (ROS) production and degranulation via LYN-AKT/ERK pathway (By similarity). To regulate ROS, communicates with the two formyl peptide receptors FPR2 and FPR1 to control the NADPH oxidase activity in neutrophils (PubMed:33789297). {ECO:0000250|UniProtKB:Q8CIM5, ECO:0000269|PubMed:16966319, ECO:0000269|PubMed:33789297}.
uniprot
proteins
mass_dalton
43705
uniprot
proteins
mutagenesis
MUTAGEN 263; /note="T->A: More than 50% loss of interaction with ARR3."; /evidence="ECO:0000269|PubMed:35427647"; MUTAGEN 264; /note="T->A: More than 50% loss of interaction with ARR3."; /evidence="ECO:0000269|PubMed:35427647
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by a subset of GPR84-activating ligands. Constitutively phosphorylated at Ser-221 and Ser-224 in the absence of 2-HTP. By contrast, Thr-263 and Thr-264 are phosphorylated only following prior cell treatment with 2-HTP. {ECO:0000269|PubMed:35427647}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
11273702
uniprot
proteins
pubmed
11404393
uniprot
proteins
pubmed
12044878
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16966319
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
33789297
uniprot
proteins
pubmed
35427647
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35427647}; Multi-pass membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 27..47; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 58..78; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 95..115; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 145..165; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 181..201; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 321..341; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 353..373; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins