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OXGR1_MOUSE
ID   OXGR1_MOUSE             Reviewed;         337 AA.
AC   Q6IYF8; Q0VEK6; Q3UQE9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=2-oxoglutarate receptor 1;
DE   AltName: Full=Alpha-ketoglutarate receptor 1;
DE   AltName: Full=G-protein coupled receptor 99;
GN   Name=Oxgr1; Synonyms=Gpr99;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC   STRAIN=BALB/cJ;
RX   PubMed=15141213; DOI=10.1038/nature02488;
RA   He W., Miao F.J.-P., Lin D.C.-H., Schwandner R.T., Wang Z., Gao J.,
RA   Chen J.-L., Tian H., Ling L.;
RT   "Citric acid cycle intermediates as ligands for orphan G-protein-coupled
RT   receptors.";
RL   Nature 429:188-193(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [3]
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).
CC   -!- FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively
CC       through a G(q)-mediated pathway. {ECO:0000269|PubMed:15141213}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the kidney with limited
CC       expression in the testis and the smooth muscle.
CC       {ECO:0000269|PubMed:15141213}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE25093.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY612852; AAT10591.1; -; mRNA.
DR   EMBL; AK142510; BAE25093.1; ALT_FRAME; mRNA.
DR   EMBL; BC119196; AAI19197.1; -; mRNA.
DR   EMBL; BC119200; AAI19201.1; -; mRNA.
DR   CCDS; CCDS27340.1; -.
DR   RefSeq; NP_001001490.1; NM_001001490.3.
DR   AlphaFoldDB; Q6IYF8; -.
DR   SMR; Q6IYF8; -.
DR   STRING; 10090.ENSMUSP00000055137; -.
DR   GuidetoPHARMACOLOGY; 162; -.
DR   GlyGen; Q6IYF8; 1 site.
DR   PhosphoSitePlus; Q6IYF8; -.
DR   PaxDb; Q6IYF8; -.
DR   PeptideAtlas; Q6IYF8; -.
DR   PRIDE; Q6IYF8; -.
DR   Antibodypedia; 10650; 122 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000058213; ENSMUSP00000055137; ENSMUSG00000044819.
DR   GeneID; 239283; -.
DR   KEGG; mmu:239283; -.
DR   UCSC; uc007uzo.1; mouse.
DR   CTD; 27199; -.
DR   MGI; MGI:2685145; Oxgr1.
DR   VEuPathDB; HostDB:ENSMUSG00000044819; -.
DR   eggNOG; ENOG502QYYG; Eukaryota.
DR   GeneTree; ENSGT01030000234621; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q6IYF8; -.
DR   OMA; FVIIHPM; -.
DR   OrthoDB; 933668at2759; -.
DR   PhylomeDB; Q6IYF8; -.
DR   TreeFam; TF330775; -.
DR   Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 239283; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q6IYF8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q6IYF8; protein.
DR   Bgee; ENSMUSG00000044819; Expressed in right kidney and 19 other tissues.
DR   Genevisible; Q6IYF8; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0016208; F:AMP binding; ISO:MGI.
DR   GO; GO:0001609; F:G protein-coupled adenosine receptor activity; ISO:MGI.
DR   GO; GO:0001883; F:purine nucleoside binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
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_0000069995"
FT   TOPO_DOM        1..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..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;  38230 MW;  079A603551112277 CRC64;
     MIEPLDSPAS DSDFLDYPSA LGNCTDEQIS FKMQYLPVIY SIIFLVGFPG NTVAISIYIF
     KMRPWRGSTV IMLNLALTDL LYLTSLPFLI HYYASGENWI FGDFMCKFIR FGFHFNLYSS
     ILFLTCFSLF RYVVIIHPMS CFSIQKTRWA VVACAGVWVI SLVAVMPMTF LITSTTRTNR
     SACLDLTSSD DLTTIKWYNL ILTATTFCLP LVIVTLCYTT IISTLTHGPR THSCFKQKAR
     RLTILLLLVF YICFLPFHIL RVIRIESRLL SISCSIESHI HEAYIVSRPL AALNTFGNLL
     LYVVVSNNFQ QAFCSIVRCK ASGDLEQGKK DSCSNNP
 
 
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