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GPR84_HUMAN
ID   GPR84_HUMAN             Reviewed;         396 AA.
AC   Q9NQS5; B6V9G7;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=G-protein coupled receptor 84;
DE   AltName: Full=Inflammation-related G-protein coupled receptor EX33;
GN   Name=GPR84; Synonyms=EX33;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11404393;
RA   Yousefi S., Cooper P.R., Potter S.L., Mueck B., Jarai G.;
RT   "Cloning and expression analysis of a novel G-protein-coupled receptor
RT   selectively expressed on granulocytes.";
RL   J. Leukoc. Biol. 69:1045-1052(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11273702; DOI=10.1006/jmbi.2001.4520;
RA   Wittenberger T., Schaller H.C., Hellebrand S.;
RT   "An expressed sequence tag (EST) data mining strategy succeeding in the
RT   discovery of new G-protein coupled receptors.";
RL   J. Mol. Biol. 307:799-813(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Kaighin V.A., Martin A.L., Aronstam R.S.;
RT   "Isolation of cDNA coding for Homo sapiens G protein-coupled receptor 84
RT   (GPR84).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA   Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT   "Identification of G protein-coupled receptor genes from the human genome
RT   sequence.";
RL   FEBS Lett. 520:97-101(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16966319; DOI=10.1074/jbc.m608019200;
RA   Wang J., Wu X., Simonavicius N., Tian H., Ling L.;
RT   "Medium-chain fatty acids as ligands for orphan G protein-coupled receptor
RT   GPR84.";
RL   J. Biol. Chem. 281:34457-34464(2006).
RN   [8]
RP   VARIANT ARG-367.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
CC   -!- FUNCTION: Receptor for medium-chain free fatty acid (FFA) with carbon
CC       chain lengths of C9 to C14. Capric acid (C10:0), undecanoic acid
CC       (C11:0) and lauric acid (C12:0) are the most potent agonists. Not
CC       activated by short-chain and long-chain saturated and unsaturated FFAs.
CC       Activation by medium-chain free fatty acid is coupled to a pertussis
CC       toxin sensitive G(i/o) protein pathway. May have important roles in
CC       processes from fatty acid metabolism to regulation of the immune
CC       system. {ECO:0000269|PubMed:16966319}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in hematopoietic tissues.
CC       High levels detected in the bone marrow and lower levels in the
CC       peripheral leukocytes and lung. Also expressed in brain, heart, muscle,
CC       colon, thymus, spleen, kidney, liver, placenta and intestine. Within
CC       the leukocyte population expression is higher in neutrophils and
CC       eosinophils relative to T- or B-lymphocytes.
CC       {ECO:0000269|PubMed:11273702, ECO:0000269|PubMed:11404393,
CC       ECO:0000269|PubMed:16966319}.
CC   -!- INDUCTION: By bacterial lipopolysaccharides (LPS) in the monocytic
CC       leukemia cell line THP-1. {ECO:0000269|PubMed:16966319}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF282693; AAF91467.1; -; mRNA.
DR   EMBL; AF237762; AAK01857.1; -; mRNA.
DR   EMBL; FJ348261; ACI96305.1; -; mRNA.
DR   EMBL; AB083586; BAB89299.1; -; Genomic_DNA.
DR   EMBL; CH471054; EAW96776.1; -; Genomic_DNA.
DR   EMBL; BC020614; AAH20614.1; -; mRNA.
DR   CCDS; CCDS8878.1; -.
DR   RefSeq; NP_065103.1; NM_020370.2.
DR   RefSeq; XP_011536797.1; XM_011538495.2.
DR   AlphaFoldDB; Q9NQS5; -.
DR   SMR; Q9NQS5; -.
DR   BioGRID; 119803; 30.
DR   IntAct; Q9NQS5; 1.
DR   STRING; 9606.ENSP00000450310; -.
DR   BindingDB; Q9NQS5; -.
DR   ChEMBL; CHEMBL3714079; -.
DR   GuidetoPHARMACOLOGY; 120; -.
DR   GlyGen; Q9NQS5; 2 sites.
DR   iPTMnet; Q9NQS5; -.
DR   PhosphoSitePlus; Q9NQS5; -.
DR   BioMuta; GPR84; -.
DR   DMDM; 66774035; -.
DR   EPD; Q9NQS5; -.
DR   MassIVE; Q9NQS5; -.
DR   PaxDb; Q9NQS5; -.
DR   PeptideAtlas; Q9NQS5; -.
DR   PRIDE; Q9NQS5; -.
DR   ProteomicsDB; 82180; -.
DR   Antibodypedia; 15347; 307 antibodies from 30 providers.
DR   DNASU; 53831; -.
DR   Ensembl; ENST00000267015.4; ENSP00000267015.3; ENSG00000139572.4.
DR   Ensembl; ENST00000551809.1; ENSP00000450310.1; ENSG00000139572.4.
DR   GeneID; 53831; -.
DR   KEGG; hsa:53831; -.
DR   MANE-Select; ENST00000267015.4; ENSP00000267015.3; NM_020370.3; NP_065103.1.
DR   UCSC; uc001sfu.4; human.
DR   CTD; 53831; -.
DR   DisGeNET; 53831; -.
DR   GeneCards; GPR84; -.
DR   HGNC; HGNC:4535; GPR84.
DR   HPA; ENSG00000139572; Tissue enhanced (bone marrow, urinary bladder).
DR   MIM; 606383; gene.
DR   neXtProt; NX_Q9NQS5; -.
DR   OpenTargets; ENSG00000139572; -.
DR   PharmGKB; PA28928; -.
DR   VEuPathDB; HostDB:ENSG00000139572; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000161671; -.
DR   HOGENOM; CLU_009579_3_10_1; -.
DR   InParanoid; Q9NQS5; -.
DR   OMA; QVLHMFC; -.
DR   OrthoDB; 732872at2759; -.
DR   PhylomeDB; Q9NQS5; -.
DR   TreeFam; TF333474; -.
DR   PathwayCommons; Q9NQS5; -.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   SignaLink; Q9NQS5; -.
DR   SIGNOR; Q9NQS5; -.
DR   BioGRID-ORCS; 53831; 9 hits in 1068 CRISPR screens.
DR   GeneWiki; GPR84; -.
DR   GenomeRNAi; 53831; -.
DR   Pharos; Q9NQS5; Tchem.
DR   PRO; PR:Q9NQS5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9NQS5; protein.
DR   Bgee; ENSG00000139572; Expressed in bone marrow and 98 other tissues.
DR   Genevisible; Q9NQS5; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR   GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0001604; F:urotensin II receptor activity; IBA:GO_Central.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..396
FT                   /note="G-protein coupled receptor 84"
FT                   /id="PRO_0000069589"
FT   TOPO_DOM        1..26
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        27..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..94
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..320
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..396
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          244..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CIM5"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CIM5"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         37
FT                   /note="G -> D (in dbSNP:rs11170883)"
FT                   /id="VAR_049397"
FT   VARIANT         367
FT                   /note="P -> R"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069393"
SQ   SEQUENCE   396 AA;  43705 MW;  BEEA467DFEB7520B CRC64;
     MWNSSDANFS CYHESVLGYR YVAVSWGVVV AVTGTVGNVL TLLALAIQPK LRTRFNLLIA
     NLTLADLLYC TLLQPFSVDT YLHLHWRTGA TFCRVFGLLL FASNSVSILT LCLIALGRYL
     LIAHPKLFPQ VFSAKGIVLA LVSTWVVGVA SFAPLWPIYI LVPVVCTCSF DRIRGRPYTT
     ILMGIYFVLG LSSVGIFYCL IHRQVKRAAQ ALDQYKLRQA SIHSNHVART DEAMPGRFQE
     LDSRLASGGP SEGISSEPVS AATTQTLEGD SSEVGDQINS KRAKQMAEKS PPEASAKAQP
     IKGARRAPDS SSEFGKVTRM CFAVFLCFAL SYIPFLLLNI LDARVQAPRV VHMLAANLTW
     LNGCINPVLY AAMNRQFRQA YGSILKRGPR SFHRLH
 
 
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