O51E2_MOUSE
ID O51E2_MOUSE Reviewed; 320 AA.
AC Q8VBV9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Olfactory receptor 51E2;
DE AltName: Full=Olfactory receptor 78 {ECO:0000303|PubMed:23401498};
GN Name=Or51e2;
GN Synonyms=Mol2.3 {ECO:0000303|PubMed:11069588},
GN Olfr78 {ECO:0000303|PubMed:23401498}, Psgr;
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=BALB/cJ;
RX PubMed=11707321; DOI=10.1016/s0378-1119(01)00709-0;
RA Yuan T.T., Toy P., McClary J.A., Lin R.J., Miyamoto N.G., Kretschmer P.J.;
RT "Cloning and genetic characterization of an evolutionarily conserved human
RT olfactory receptor that is differentially expressed across species.";
RL Gene 278:41-51(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11802173; DOI=10.1038/nn800;
RA Zhang X., Firestein S.;
RT "The olfactory receptor gene superfamily of the mouse.";
RL Nat. Neurosci. 5:124-133(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14611657; DOI=10.1186/gb-2003-4-11-r71;
RA Young J.M., Shykind B.M., Lane R.P., Tonnes-Priddy L., Ross J.A.,
RA Walker M., Williams E.M., Trask B.J.;
RT "Odorant receptor expressed sequence tags demonstrate olfactory expression
RT of over 400 genes, extensive alternate splicing and unequal expression
RT levels.";
RL Genome Biol. 4:R71.1-R71.13(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11069588; DOI=10.1046/j.1460-9568.2000.00286.x;
RA Conzelmann S., Levai O., Bode B., Eisel U., Raming K., Breer H.,
RA Strotmann J.;
RT "A novel brain receptor is expressed in a distinct population of olfactory
RT sensory neurons.";
RL Eur. J. Neurosci. 12:3926-3934(2000).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND CAUTION.
RX PubMed=23401498; DOI=10.1073/pnas.1215927110;
RA Pluznick J.L., Protzko R.J., Gevorgyan H., Peterlin Z., Sipos A., Han J.,
RA Brunet I., Wan L.X., Rey F., Wang T., Firestein S.J., Yanagisawa M.,
RA Gordon J.I., Eichmann A., Peti-Peterdi J., Caplan M.J.;
RT "Olfactory receptor responding to gut microbiota-derived signals plays a
RT role in renin secretion and blood pressure regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:4410-4415(2013).
RN [10]
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, CAUTION, AND FUNCTION.
RX PubMed=26560302; DOI=10.1038/nature15721;
RA Chang A.J., Ortega F.E., Riegler J., Madison D.V., Krasnow M.A.;
RT "Oxygen regulation of breathing through an olfactory receptor activated by
RT lactate.";
RL Nature 527:240-244(2015).
RN [11]
RP CAUTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=30258151; DOI=10.1038/s41586-018-0545-9;
RA Torres-Torrelo H., Ortega-Saenz P., Macias D., Omura M., Zhou T.,
RA Matsunami H., Johnson R.S., Mombaerts P., Lopez-Barneo J.;
RT "The role of Olfr78 in the breathing circuit of mice.";
RL Nature 561:E33-E40(2018).
RN [12]
RP REPLY TO PUBMED:30258151.
RX PubMed=30258152; DOI=10.1038/s41586-018-0547-7;
RA Chang A.J., Kim N.S., Hireed H., de Arce A.D., Ortega F.E., Riegler J.,
RA Madison D.V., Krasnow M.A.;
RT "Chang et al. reply.";
RL Nature 561:E41-E41(2018).
CC -!- FUNCTION: Olfactory receptor. The activity of this receptor is probably
CC mediated by G-proteins wich induce elevation of intracellular Ca(2+),
CC cAMP and activation of phosphorylation of the protein kinases PKA and
CC MAPK3/MAPK1. Activation of OR51E2 may affect melanocyte proliferation,
CC differentiation, and melanogenesis and may increase proliferation and
CC migration of primary retinal pigment epithelial (RPE) cells (By
CC similarity). Activated by the short chain fatty acids (SCFA), acetate
CC and propionate (PubMed:23401498). In response to SCFA, may positively
CC regulate renin secretion and increase blood pressure (PubMed:23401498).
CC May also be activated by steroid hormones and regulate cell
CC proliferation (By similarity). Activated by L-lactate in glomus cells
CC (PubMed:26560302, PubMed:30258151). {ECO:0000250|UniProtKB:Q9H255,
CC ECO:0000269|PubMed:23401498, ECO:0000269|PubMed:26560302,
CC ECO:0000269|PubMed:30258151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23401498};
CC Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H255}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In brain, expressed in medulla oblongata by cells
CC close to the fourth ventricle, in the area postrema, the nucleus
CC tractus solitarius (PubMed:11707321). Expressed in olfactory epithelium
CC and vomeronasal organ (PubMed:11069588). Expressed in kidney by large
CC renal vessels, renal afferent arterioles, and extrarenal vascular beds.
CC In small resistance vessels the expression is restricted to cells of
CC the juxtaglomerular afferent arteriole, which mediate renin secretion.
CC Also detected in small blood vessels in a variety of tissues including
CC heart, diaphragm, skeletal muscle, and skin. In the heart, esophagus,
CC and stomach it is detected in axons of autonomic neurons and neurons of
CC the enteric plexus (PubMed:23401498). Also detected in colon and liver
CC (PubMed:23401498). Expressed in the glomus cells of the carotid body
CC (PubMed:26560302). {ECO:0000269|PubMed:11069588,
CC ECO:0000269|PubMed:11707321, ECO:0000269|PubMed:23401498,
CC ECO:0000269|PubMed:26560302}.
CC -!- DEVELOPMENTAL STAGE: Primarily detected between 11 dpc and 12 dpc.
CC Expressed at 12 dpc in the dorsal region of the developing nasal cavity
CC and in the mesenchyme located between the olfactory epithelium and the
CC presumptive olfactory bulb. In the medulla oblongata, first detected at
CC 17 dpc. In the area postrema and the nucleus tractus solitarius
CC expression peaks at P20 and then decreases slightly.
CC {ECO:0000269|PubMed:11069588}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice display reduced baseline blood
CC pressure. {ECO:0000269|PubMed:23401498}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Contradictory results have been reported for activation by
CC beta-ionone in human and mouse. Beta-ionone does not activate OR51E2 in
CC mouse. This difference may depend on the different methods used for
CC these experiments, or may be due to species difference.
CC {ECO:0000250|UniProtKB:Q9H255, ECO:0000269|PubMed:23401498}.
CC -!- CAUTION: Conflicting results for the role of OR51E2 in the regulation
CC of breathing and its role as a hypoxia sensor activated by lactate are
CC reported (PubMed:26560302, PubMed:30258151). It was first described as
CC a hypoxia sensor in the breathing circuit by sensing lactate produced
CC when oxygen levels decline (PubMed:26560302). A recent study fails to
CC confirm a role for OR52E2 in this pathway (PubMed:30258151).
CC Conflicting results may reflect the use of different strain backgrounds
CC (PubMed:30258152, PubMed:26560302, PubMed:30258151).
CC {ECO:0000269|PubMed:26560302, ECO:0000269|PubMed:30258151,
CC ECO:0000269|PubMed:30258152}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF378854; AAL35109.1; -; mRNA.
DR EMBL; AY073011; AAL60674.1; -; Genomic_DNA.
DR EMBL; AY317674; AAP71053.1; -; Genomic_DNA.
DR EMBL; AK028467; BAC25966.1; -; mRNA.
DR EMBL; AK036356; BAC29396.1; -; mRNA.
DR EMBL; AC162175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL16625.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL16627.1; -; Genomic_DNA.
DR EMBL; BC120603; AAI20604.1; -; mRNA.
DR EMBL; BC120629; AAI20630.1; -; mRNA.
DR CCDS; CCDS21546.1; -.
DR RefSeq; NP_001161975.1; NM_001168503.1.
DR RefSeq; NP_570936.1; NM_130866.4.
DR AlphaFoldDB; Q8VBV9; -.
DR SMR; Q8VBV9; -.
DR STRING; 10090.ENSMUSP00000058085; -.
DR GlyGen; Q8VBV9; 1 site.
DR PaxDb; Q8VBV9; -.
DR PRIDE; Q8VBV9; -.
DR ProteomicsDB; 293822; -.
DR Antibodypedia; 23521; 127 antibodies from 25 providers.
DR Ensembl; ENSMUST00000060187; ENSMUSP00000058085; ENSMUSG00000043366.
DR Ensembl; ENSMUST00000168007; ENSMUSP00000133255; ENSMUSG00000043366.
DR Ensembl; ENSMUST00000217123; ENSMUSP00000149274; ENSMUSG00000043366.
DR GeneID; 170639; -.
DR KEGG; mmu:170639; -.
DR UCSC; uc009isl.2; mouse.
DR CTD; 170639; -.
DR MGI; MGI:2157548; Olfr78.
DR VEuPathDB; HostDB:ENSMUSG00000043366; -.
DR eggNOG; ENOG502QVRN; Eukaryota.
DR GeneTree; ENSGT01050000244899; -.
DR HOGENOM; CLU_012526_0_0_1; -.
DR InParanoid; Q8VBV9; -.
DR OMA; MNLACAN; -.
DR OrthoDB; 1159837at2759; -.
DR PhylomeDB; Q8VBV9; -.
DR TreeFam; TF342735; -.
DR Reactome; R-MMU-381753; Olfactory Signaling Pathway.
DR BioGRID-ORCS; 170639; 3 hits in 67 CRISPR screens.
DR ChiTaRS; Olfr78; mouse.
DR PRO; PR:Q8VBV9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VBV9; protein.
DR Bgee; ENSMUSG00000043366; Expressed in umbilical cord and 56 other tissues.
DR Genevisible; Q8VBV9; MM.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0003707; F:nuclear steroid receptor activity; ISS:UniProtKB.
DR GO; GO:0004984; F:olfactory receptor activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISA:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB.
DR GO; GO:0097325; P:melanocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:1900135; P:positive regulation of renin secretion into blood stream; IMP:UniProtKB.
DR GO; GO:0007608; P:sensory perception of smell; ISA:MGI.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000725; Olfact_rcpt.
DR Pfam; PF13853; 7tm_4; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00245; OLFACTORYR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; G-protein coupled receptor;
KW Glycoprotein; Membrane; Olfaction; Receptor; Reference proteome;
KW Sensory transduction; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="Olfactory receptor 51E2"
FT /id="PRO_0000430209"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 320 AA; 35578 MW; 7161ACA8F4328959 CRC64;
MSSCNFTHAT FLLIGIPGLE EAHFWFGFPL LSMYAVALFG NCIVVFIVRT ERSLHAPMYL
FLCMLAAIDL ALSTSTMPKI LALFWFDSRE ITFDACLAQM FFIHTLSAIE STILLAMAFD
RYVAICHPLR HAAVLNNTVT VQIGMVALVR GSLFFFPLPL LIKRLAFCHS NVLSHSYCVH
QDVMKLAYTD TLPNVVYGLT AILLVMGVDV MFISLSYFLI IRTVLQLPSK SERAKAFGTC
VSHISVVLAF YVPLIGLSVV HRFGNSLDPI VHVLMGDVYL LLPPVINPII YGAKTKQIRT
RVLAMFKISC DKDIEAGGNT
