GPR31_MOUSE
ID GPR31_MOUSE Reviewed; 319 AA.
AC F8VQN3; Q9JLS1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor;
DE Short=12-(S)-HETE receptor;
DE Short=12-HETER;
DE AltName: Full=G-protein coupled receptor 31;
GN Name=Gpr31; Synonyms=Gpr31b, Gpr31c;
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 [GENOMIC DNA].
RX PubMed=10501965; DOI=10.1007/s003359901142;
RA Schimenti J.C.;
RT "ORFless, intronless, and mutant transcription units in the mouse t complex
RT responder (Tcr) locus.";
RL Mamm. Genome 10:969-976(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=30675063; DOI=10.1038/s41586-019-0884-1;
RA Morita N., Umemoto E., Fujita S., Hayashi A., Kikuta J., Kimura I.,
RA Haneda T., Imai T., Inoue A., Mimuro H., Maeda Y., Kayama H., Okumura R.,
RA Aoki J., Okada N., Kida T., Ishii M., Nabeshima R., Takeda K.;
RT "GPR31-dependent dendrite protrusion of intestinal CX3CR1+ cells by
RT bacterial metabolites.";
RL Nature 566:110-114(2019).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29227475; DOI=10.1038/nm.4451;
RA Zhang X.J., Cheng X., Yan Z.Z., Fang J., Wang X., Wang W., Liu Z.Y.,
RA Shen L.J., Zhang P., Wang P.X., Liao R., Ji Y.X., Wang J.Y., Tian S.,
RA Zhu X.Y., Zhang Y., Tian R.F., Wang L., Ma X.L., Huang Z., She Z.G., Li H.;
RT "An ALOX12-12-HETE-GPR31 signaling axis is a key mediator of hepatic
RT ischemia-reperfusion injury.";
RL Nat. Med. 24:73-83(2018).
CC -!- FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-
CC eicosatetraenoic acid (12-S-HETE), with much lower affinities for other
CC HETE isomers (By similarity) (PubMed:29227475). 12-S-HETE is a
CC eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid,
CC involved in many physiologic and pathologic processes, such as cell
CC growth, adhesion, inflammation and cancer promotion. 12-S-HETE-binding
CC leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B
CC pathways and leads to cell growth. Plays a crucial role for
CC proliferation, survival and macropinocytosis of KRAS-dependent cancer
CC cells by mediating the translocation of KRAS from the endoplasmic
CC reticulum to the plasma membrane (PM) and its association with the PM
CC (By similarity). Contributes to enhanced immune responses by inducing
CC dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the
CC uptake of luminal antigens (PubMed:30675063). Acts also as a key
CC receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury
CC (PubMed:29227475). {ECO:0000250|UniProtKB:O00270,
CC ECO:0000269|PubMed:29227475, ECO:0000269|PubMed:30675063}.
CC -!- FUNCTION: Proton-sensing G protein-coupled receptor.
CC {ECO:0000250|UniProtKB:O00270}.
CC -!- SUBUNIT: Interacts with KRAS; in a farnesylation-dependent manner.
CC {ECO:0000250|UniProtKB:O00270}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00270};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit a reduced response to
CC enteric bacteria, showing defective dendrite protrusions of CX3CR1(+)
CC cells in the small intestine (PubMed:30675063). Under
CC ischemia/reperfusion injury, liver dysfunction, cell death and
CC inflammatory induction are consistently and significantly inhibited at
CC 6 hours after reperfusion in GPR31-deficient mice (PubMed:29227475).
CC {ECO:0000269|PubMed:29227475, ECO:0000269|PubMed:30675063}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF140708; AAF26668.1; -; Genomic_DNA.
DR EMBL; AC166360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37438.1; -.
DR RefSeq; NP_001013854.2; NM_001013832.2.
DR AlphaFoldDB; F8VQN3; -.
DR SMR; F8VQN3; -.
DR BioGRID; 242929; 3.
DR STRING; 10090.ENSMUSP00000089237; -.
DR GuidetoPHARMACOLOGY; 98; -.
DR GlyGen; F8VQN3; 1 site.
DR PaxDb; F8VQN3; -.
DR PRIDE; F8VQN3; -.
DR Antibodypedia; 2933; 122 antibodies from 26 providers.
DR DNASU; 436440; -.
DR Ensembl; ENSMUST00000091648; ENSMUSP00000089237; ENSMUSG00000071311.
DR GeneID; 436440; -.
DR KEGG; mmu:436440; -.
DR UCSC; uc008alx.1; mouse.
DR CTD; 436440; -.
DR MGI; MGI:1354372; Gpr31b.
DR VEuPathDB; HostDB:ENSMUSG00000071311; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00990000203619; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; F8VQN3; -.
DR OMA; CLPIKAH; -.
DR OrthoDB; 903658at2759; -.
DR PhylomeDB; F8VQN3; -.
DR TreeFam; TF337237; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444209; Free fatty acid receptors.
DR BioGRID-ORCS; 436440; 8 hits in 71 CRISPR screens.
DR PRO; PR:F8VQN3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; F8VQN3; protein.
DR Bgee; ENSMUSG00000071311; Expressed in jejunum and 7 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0050544; F:arachidonic acid binding; ISO:MGI.
DR GO; GO:0045125; F:bioactive lipid receptor activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; IMP:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..319
FT /note="12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid
FT receptor"
FT /id="PRO_0000415340"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..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..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..284
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3
FT /note="R -> H (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="L -> V (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> L (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="R -> C (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="T -> M (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="R -> H (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> T (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="R -> S (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="R -> T (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> M (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="V -> M (in Ref. 1; AAF26668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35642 MW; 562F575FED1DCBA5 CRC64;
MERTNCSAAS TVVETAVGTM LTLECVLGLM GNAVALWTFF YRLKVWKPYA VYLFNLVVAD
LLLATSLPFF AAFYLKGKTW KLGHMPCQVL LFLLAFSRGV GVAFLTTVAL DRYLRVVHPR
LRVNLLSLRA AWGISSLIWL LMVVLTPQNL LTCRTTQNST ECPSFYPTGG AKAIATCQEV
LFFLQVLLPF GLISFCNSGL IRTLQKRLRE SDKQPRIRRA RVLVAIVLLL FGLCFLPSVL
TRVLVHIFQE FKSCSVQQAI VRASDIAGSL TCLHSTLSPA IYCFSNPAFT HSYRKVLKSL
RGRRKAAESP SDNLRDSYS
