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O51E2_RAT
ID   O51E2_RAT               Reviewed;         320 AA.
AC   O88628;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Olfactory receptor 51E2;
DE   AltName: Full=G-protein coupled receptor RA1c {ECO:0000303|PubMed:9932290};
DE   AltName: Full=Olfactory receptor 59;
GN   Name=Or51e2; Synonyms=Olr59, Psgr {ECO:0000303|PubMed:11707321};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9932290;
RA   Raming K., Konzelmann S., Breer H.;
RT   "Identification of a novel G-protein coupled receptor expressed in distinct
RT   brain regions and a defined olfactory zone.";
RL   Recept. Channels 6:141-151(1998).
RN   [2]
RP   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).
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. Activated
CC       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 (By similarity). May also be activated by steroid
CC       hormones and regulate cell proliferation (By similarity). Activated by
CC       L-lactate in glomus cells (By similarity).
CC       {ECO:0000250|UniProtKB:Q8VBV9, ECO:0000250|UniProtKB:Q9H255}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H255};
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: Expressed in brain and liver. Expressed only in
CC       some areas of the brain and in the olfactory epithelium.
CC       {ECO:0000269|PubMed:11707321}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF079864; AAD12761.1; -; mRNA.
DR   RefSeq; NP_775415.1; NM_173293.1.
DR   AlphaFoldDB; O88628; -.
DR   SMR; O88628; -.
DR   STRING; 10116.ENSRNOP00000025097; -.
DR   GlyGen; O88628; 1 site.
DR   PaxDb; O88628; -.
DR   GeneID; 170816; -.
DR   KEGG; rno:170816; -.
DR   UCSC; RGD:628858; rat.
DR   CTD; 170816; -.
DR   RGD; 628858; Olr59.
DR   eggNOG; ENOG502QVRN; Eukaryota.
DR   InParanoid; O88628; -.
DR   OrthoDB; 1159837at2759; -.
DR   PhylomeDB; O88628; -.
DR   Reactome; R-RNO-381753; Olfactory Signaling Pathway.
DR   PRO; PR:O88628; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043229; C:intracellular organelle; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0071398; P:cellular response to fatty acid; ISS:UniProtKB.
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; ISS: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; ISS:UniProtKB.
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_0000150752"
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;  35505 MW;  E7FF78F5FFD5BF94 CRC64;
     MSSCNFTHAT FMLIGIPGLE EAHFWFGFPL LSMYAVALFG NCIVVFIVRT ERSLHAPMYL
     FLCMLAAIDL ALSTSTMPKI LALFWFDSRE ITFDACLAQM FFIHALSAIE STILLAMAFD
     RYVAICHPLR HAAVLNNTVT VQIGMVALVR GSLFFFPLPL LIKRLAFCHS NVLSHSYCVH
     QDVMKLAYTD TLPNVVYGLT AILLVMGVDV MFISLSYFLI IRAVLQLPSK SERAKAFGTC
     VSHIGVVLAF YVPLIGLSVV HRFGNSLDPI VHVLMGDVYL LLPPVINPII YGAKTKQIRT
     RVLAMFKISC DKDIEAGGNT
 
 
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