OXGR1_RAT
ID OXGR1_RAT Reviewed; 337 AA.
AC Q6Y1R5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=2-oxoglutarate receptor 1;
DE AltName: Full=Alpha-ketoglutarate receptor 1;
DE AltName: Full=G-protein coupled receptor 80;
DE AltName: Full=P2Y purinoceptor 15;
DE Short=P2Y15;
GN Name=Oxgr1; Synonyms=Gpr80, P2y15;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15001573; DOI=10.1074/jbc.m400360200;
RA Inbe H., Watanabe S., Miyawaki M., Tanabe E., Encinas J.A.;
RT "Identification and characterization of a cell-surface receptor, P2Y15, for
RT AMP and adenosine.";
RL J. Biol. Chem. 279:19790-19799(2004).
CC -!- FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively
CC through a G(q)-mediated pathway (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in mast cells and is found
CC predominantly in the tissues of the respiratory tract and kidneys.
CC {ECO:0000269|PubMed:15001573}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be a P2Y receptor.
CC {ECO:0000305|PubMed:15001573}.
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DR EMBL; AY191367; AAP32736.1; -; mRNA.
DR RefSeq; NP_997471.1; NM_207588.1.
DR RefSeq; XP_006252533.1; XM_006252471.3.
DR AlphaFoldDB; Q6Y1R5; -.
DR SMR; Q6Y1R5; -.
DR STRING; 10116.ENSRNOP00000054374; -.
DR BindingDB; Q6Y1R5; -.
DR ChEMBL; CHEMBL2325; -.
DR GlyGen; Q6Y1R5; 1 site.
DR PhosphoSitePlus; Q6Y1R5; -.
DR PaxDb; Q6Y1R5; -.
DR PRIDE; Q6Y1R5; -.
DR Ensembl; ENSRNOT00000057564; ENSRNOP00000054374; ENSRNOG00000037884.
DR GeneID; 290493; -.
DR KEGG; rno:290493; -.
DR CTD; 27199; -.
DR RGD; 1303155; Oxgr1.
DR eggNOG; ENOG502QYYG; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q6Y1R5; -.
DR OMA; FVIIHPM; -.
DR OrthoDB; 933668at2759; -.
DR PhylomeDB; Q6Y1R5; -.
DR TreeFam; TF330775; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q6Y1R5; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000037884; Expressed in kidney and 1 other tissue.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor 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 PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="2-oxoglutarate receptor 1"
FT /id="PRO_0000069996"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..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..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 337 AA; 38377 MW; 9899E80DE0531CB9 CRC64;
MIETLDSPAN DSDFLDYITA LENCTDEQIS FKMQYLPVIY SIIFLVGFPG NTVAISIYVF
KMRPWKSSTI IMLNLALTDL LYLTSLPFLI HYYASGENWI FGDFMCKFIR FGFHFNLYSS
ILFLTCFSLF RYIVIIHPMS CFSIQKTRWA VVACAGVWVI SLVAVMPMTF LITSTTRTNR
SACLDLTSSD DLTTIKWYNL ILTATTFCLP LLIVTLCYTT IISTLTHGPR THSCFKQKAR
RLTILLLLVF YVCFLPFHIL RVIRIESRLL SISCSIESHI HEAYIVSRPL AALNTFGNLL
LYVVVSNNFQ QAFCSAVRCK AIGDLEQAKK DSCSNNP
