GPR84_MOUSE
ID GPR84_MOUSE Reviewed; 396 AA.
AC Q8CIM5; Q99MX9;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=G-protein coupled receptor 84;
GN Name=Gpr84;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-224, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
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 system
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in hematopoietic tissues.
CC Expressed mainly in the bone marrow with transcripts also detected in
CC spleen, the lymph node, liver and the lung.
CC {ECO:0000269|PubMed:11273702, ECO:0000269|PubMed:16966319}.
CC -!- INDUCTION: By lipopolysaccharide in the monocyte/macrophage cell lines.
CC {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; AF272948; AAK01859.1; -; mRNA.
DR EMBL; BC023249; AAH23249.1; -; mRNA.
DR CCDS; CCDS27902.1; -.
DR RefSeq; NP_109645.1; NM_030720.1.
DR AlphaFoldDB; Q8CIM5; -.
DR SMR; Q8CIM5; -.
DR STRING; 10090.ENSMUSP00000078753; -.
DR BindingDB; Q8CIM5; -.
DR ChEMBL; CHEMBL4523386; -.
DR GlyGen; Q8CIM5; 2 sites.
DR iPTMnet; Q8CIM5; -.
DR PhosphoSitePlus; Q8CIM5; -.
DR SwissPalm; Q8CIM5; -.
DR jPOST; Q8CIM5; -.
DR MaxQB; Q8CIM5; -.
DR PaxDb; Q8CIM5; -.
DR PeptideAtlas; Q8CIM5; -.
DR PRIDE; Q8CIM5; -.
DR ProteomicsDB; 271458; -.
DR DNASU; 80910; -.
DR GeneID; 80910; -.
DR KEGG; mmu:80910; -.
DR UCSC; uc007xxy.1; mouse.
DR CTD; 53831; -.
DR MGI; MGI:1934129; Gpr84.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q8CIM5; -.
DR OrthoDB; 732872at2759; -.
DR PhylomeDB; Q8CIM5; -.
DR TreeFam; TF333474; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 80910; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Gpr84; mouse.
DR PRO; PR:Q8CIM5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CIM5; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein 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_0000069590"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..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..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..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 241..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
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 CONFLICT 24
FT /note="V -> I (in Ref. 1; AAK01859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43717 MW; 80F0601CBB4B1B03 CRC64;
MWNSSDANFS CYHESVLGYR YFAVIWGVAV AVTGTVGNVL TLLALAIRPK LRTRFNLLIA
NLTLADLLYC TLLQPFSVDT YLHLHWRTGA VFCRIFGLLL FTSNSVSILT LCLIALGRYL
LIAHPKLFPQ VFSAKGIVLA LVGSWVVGVT SFAPLWNVFV LVPVVCTCSF DRMRGRPYTT
ILMGIYFVLG LSSVGVFYCL IHRQVKRAAR ALDQYGLHQA SIRSHQVAGT QEAMPGHFQE
LDSGVASRGP SEGISSEPVS AATTQTLEGD SSEAGGQGIR KAAQQIAERS LPEVHRKPRE
TAGARRATDA PSEFGKVTRM CFAVFLCFAL SYIPFLLLNI LDARGRAPRV VHMVAANLTW
LNSCINPVLY AAMNRQFRHA YGSILKRGPQ SFRRFH
