O51E2_HUMAN
ID O51E2_HUMAN Reviewed; 320 AA.
AC Q9H255; B2RA63; Q6IF94;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Olfactory receptor 51E2;
DE AltName: Full=HPRAJ;
DE AltName: Full=Olfactory receptor OR11-16;
DE AltName: Full=Prostate-specific G-protein coupled receptor {ECO:0000303|PubMed:11118034};
GN Name=OR51E2 {ECO:0000312|HGNC:HGNC:15195};
GN Synonyms=PSGR {ECO:0000303|PubMed:11118034};
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 [GENOMIC DNA], AND INDUCTION.
RX PubMed=11118034;
RA Xu L.L., Stackhouse B.G., Florence K., Zhang W., Shanmugam N.,
RA Sesterhenn I.A., Zou Z., Srikantan V., Augustus M., Roschke V., Carter K.,
RA McLeod D.G., Moul J.W., Soppet D., Srivastava S.;
RT "PSGR, a novel prostate-specific gene with homology to a G protein-coupled
RT receptor, is overexpressed in prostate cancer.";
RL Cancer Res. 60:6568-6572(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xia C., Ma W., Liu M.;
RT "Identification of a prostate-specific G-protein coupled receptor (PSGR)
RT that interacts with G alpha subunit in yeast two hybrid assay.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 IDENTIFICATION.
RX PubMed=14983052; DOI=10.1073/pnas.0307882100;
RA Malnic B., Godfrey P.A., Buck L.B.;
RT "The human olfactory receptor gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2584-2589(2004).
RN [8]
RP ERRATUM OF PUBMED:14983052.
RA Malnic B., Godfrey P.A., Buck L.B.;
RL Proc. Natl. Acad. Sci. U.S.A. 101:7205-7205(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16491480; DOI=10.1002/pros.20389;
RA Wang J., Weng J., Cai Y., Penland R., Liu M., Ittmann M.;
RT "The prostate-specific G-protein coupled receptors PSGR and PSGR2 are
RT prostate cancer biomarkers that are complementary to alpha-methylacyl-CoA
RT racemase.";
RL Prostate 66:847-857(2006).
RN [10]
RP FUNCTION.
RX PubMed=19389702; DOI=10.1074/jbc.m109.012096;
RA Neuhaus E.M., Zhang W., Gelis L., Deng Y., Noldus J., Hatt H.;
RT "Activation of an olfactory receptor inhibits proliferation of prostate
RT cancer cells.";
RL J. Biol. Chem. 284:16218-16225(2009).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [12]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=27226631; DOI=10.1074/jbc.m116.734517;
RA Gelis L., Jovancevic N., Veitinger S., Mandal B., Arndt H.D., Neuhaus E.M.,
RA Hatt H.;
RT "Functional characterization of the odorant receptor 51E2 in human
RT melanocytes.";
RL J. Biol. Chem. 291:17772-17786(2016).
RN [13]
RP TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29249973; DOI=10.3389/fphys.2017.00888;
RA Jovancevic N., Khalfaoui S., Weinrich M., Weidinger D., Simon A., Kalbe B.,
RA Kernt M., Kampik A., Gisselmann G., Gelis L., Hatt H.;
RT "Odorant receptor 51E2 agonist beta-ionone regulates RPE cell migration and
RT proliferation.";
RL Front. Physiol. 8:888-888(2017).
CC -!- FUNCTION: Olfactory receptor (PubMed:29249973, PubMed:27226631).
CC Activated by the odorant, beta-ionone, a synthetic terpenoid
CC (PubMed:29249973, PubMed:27226631, PubMed:19389702). The activity of
CC this receptor is probably mediated by G-proteins leading to the
CC elevation of intracellular Ca(2+), cAMP and activation of the protein
CC kinases PKA and MAPK3/MAPK1 (PubMed:27226631, PubMed:29249973).
CC Stimulation of OR51E2 by beta-ionone affects melanocyte proliferation,
CC differentiation, and melanogenesis (PubMed:27226631). Activation of
CC OR51E2 by beta-ionone increases proliferation and migration of primary
CC retinal pigment epithelial (RPE) cells (PubMed:29249973). Activated
CC also by the short-chain fatty acids (SCFA) acetate and propionate. In
CC response to SCFA, may positively regulate renin secretion and increase
CC blood pressure (PubMed:23401498). May also be activated by steroid
CC hormones and regulate cell proliferation (PubMed:19389702). Activated
CC by L-lactate in glomus cells (By similarity).
CC {ECO:0000250|UniProtKB:Q8VBV9, ECO:0000269|PubMed:19389702,
CC ECO:0000269|PubMed:23401498, ECO:0000269|PubMed:27226631,
CC ECO:0000269|PubMed:29249973}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23401498,
CC ECO:0000269|PubMed:27226631, ECO:0000269|PubMed:29249973}; Multi-pass
CC membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:27226631}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the prostate (PubMed:11707321).
CC Also expressed in spleen, liver, olfactory epithelium, retinal pigment
CC epithelium and medulla oblongata (PubMed:29249973, PubMed:11707321,
CC PubMed:16491480). In the retinal pigment epithelium expression is
CC restricted to the pigment cells and choroid (at protein level)
CC (PubMed:29249973). Expressed in epidermal melanocytes (at protein
CC level) (PubMed:27226631). {ECO:0000269|PubMed:11707321,
CC ECO:0000269|PubMed:16491480, ECO:0000269|PubMed:27226631,
CC ECO:0000269|PubMed:29249973}.
CC -!- INDUCTION: Up-regulated in prostate cancer.
CC {ECO:0000269|PubMed:11118034}.
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 of
CC this receptor by beta-ionone in human and mouse. Beta-ionone does not
CC activate OR51E2 in mouse. This difference may depend on the different
CC methods used for the experiment or may be due to species difference.
CC {ECO:0000269|PubMed:23401498, ECO:0000269|PubMed:27226631,
CC ECO:0000269|PubMed:29249973}.
CC -!- WEB RESOURCE: Name=Human Olfactory Receptor Data Exploratorium (HORDE);
CC URL="http://genome.weizmann.ac.il/horde/card/index/symbol:OR51E2";
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DR EMBL; AF311306; AAG40776.1; -; Genomic_DNA.
DR EMBL; AF369708; AAK38728.1; -; mRNA.
DR EMBL; AY033942; AAK57550.1; -; mRNA.
DR EMBL; AK314051; BAG36760.1; -; mRNA.
DR EMBL; CH471064; EAW68829.1; -; Genomic_DNA.
DR EMBL; BC020768; AAH20768.1; -; mRNA.
DR EMBL; BK004368; DAA04766.1; -; Genomic_DNA.
DR CCDS; CCDS7751.1; -.
DR RefSeq; NP_110401.1; NM_030774.3.
DR AlphaFoldDB; Q9H255; -.
DR SMR; Q9H255; -.
DR BioGRID; 123434; 10.
DR IntAct; Q9H255; 8.
DR STRING; 9606.ENSP00000380153; -.
DR ChEMBL; CHEMBL4523454; -.
DR TCDB; 9.A.14.8.3; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9H255; 1 site.
DR BioMuta; OR51E2; -.
DR DMDM; 18202936; -.
DR MassIVE; Q9H255; -.
DR PaxDb; Q9H255; -.
DR PeptideAtlas; Q9H255; -.
DR PRIDE; Q9H255; -.
DR ProteomicsDB; 80502; -.
DR Antibodypedia; 23521; 127 antibodies from 25 providers.
DR DNASU; 81285; -.
DR Ensembl; ENST00000396950.4; ENSP00000380153.3; ENSG00000167332.9.
DR Ensembl; ENST00000641638.1; ENSP00000493442.1; ENSG00000167332.9.
DR GeneID; 81285; -.
DR KEGG; hsa:81285; -.
DR MANE-Select; ENST00000396950.4; ENSP00000380153.3; NM_030774.4; NP_110401.1.
DR UCSC; uc001lzk.3; human.
DR CTD; 81285; -.
DR DisGeNET; 81285; -.
DR GeneCards; OR51E2; -.
DR HGNC; HGNC:15195; OR51E2.
DR HPA; ENSG00000167332; Group enriched (intestine, prostate).
DR MIM; 611268; gene.
DR neXtProt; NX_Q9H255; -.
DR OpenTargets; ENSG00000167332; -.
DR PharmGKB; PA32372; -.
DR VEuPathDB; HostDB:ENSG00000167332; -.
DR eggNOG; ENOG502QVRN; Eukaryota.
DR GeneTree; ENSGT01050000244899; -.
DR HOGENOM; CLU_012526_0_0_1; -.
DR InParanoid; Q9H255; -.
DR OMA; MNLACAN; -.
DR OrthoDB; 1159837at2759; -.
DR PhylomeDB; Q9H255; -.
DR TreeFam; TF342735; -.
DR PathwayCommons; Q9H255; -.
DR Reactome; R-HSA-381753; Olfactory Signaling Pathway.
DR Reactome; R-HSA-9752946; Expression and translocation of olfactory receptors.
DR SignaLink; Q9H255; -.
DR BioGRID-ORCS; 81285; 12 hits in 676 CRISPR screens.
DR ChiTaRS; OR51E2; human.
DR GeneWiki; OR51E2; -.
DR GenomeRNAi; 81285; -.
DR Pharos; Q9H255; Tchem.
DR PRO; PR:Q9H255; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H255; protein.
DR Bgee; ENSG00000167332; Expressed in pigmented layer of retina and 80 other tissues.
DR ExpressionAtlas; Q9H255; baseline and differential.
DR Genevisible; Q9H255; HS.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0004984; F:olfactory receptor activity; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; ISS:UniProtKB.
DR GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
DR GO; GO:0097325; P:melanocyte proliferation; IMP:UniProtKB.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:UniProtKB.
DR GO; GO:1900135; P:positive regulation of renin secretion into blood stream; ISS:UniProtKB.
DR GO; GO:0043401; P:steroid hormone mediated signaling pathway; IDA: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 1: Evidence at protein 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_0000150751"
FT TOPO_DOM 1..24
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..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..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..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; 35493 MW; 03582CC2AAB6E2C6 CRC64;
MSSCNFTHAT FVLIGIPGLE KAHFWVGFPL LSMYVVAMFG NCIVVFIVRT ERSLHAPMYL
FLCMLAAIDL ALSTSTMPKI LALFWFDSRE ISFEACLTQM FFIHALSAIE STILLAMAFD
RYVAICHPLR HAAVLNNTVT AQIGIVAVVR GSLFFFPLPL LIKRLAFCHS NVLSHSYCVH
QDVMKLAYAD TLPNVVYGLT AILLVMGVDV MFISLSYFLI IRTVLQLPSK SERAKAFGTC
VSHIGVVLAF YVPLIGLSVV HRFGNSLHPI VRVVMGDIYL LLPPVINPII YGAKTKQIRT
RVLAMFKISC DKDLQAVGGK
