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SUCR1_MOUSE
ID   SUCR1_MOUSE             Reviewed;         317 AA.
AC   Q99MT6; Q4V9V9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Succinate receptor 1;
DE   AltName: Full=G-protein coupled receptor 91;
GN   Name=Sucnr1; Synonyms=Gpr91;
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=C57BL/6J;
RX   PubMed=11273702; DOI=10.1006/jmbi.2001.4520;
RA   Wittenberger T., Schaller H.C., Hellebrand S.;
RT   "An expressed sequence tag (EST) data mining strategy succeeding in the
RT   discovery of new G-protein coupled receptors.";
RL   J. Mol. Biol. 307:799-813(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Receptor for succinate. {ECO:0000269|PubMed:15141213}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the kidney (proximal and
CC       distal tubules and the juxtaglomerular apparatus). Weakly expressed in
CC       liver, spleen and small intestine. {ECO:0000269|PubMed:11273702,
CC       ECO:0000269|PubMed:15141213}.
CC   -!- DISRUPTION PHENOTYPE: Abolition of succinate-induced hypertension.
CC       {ECO:0000269|PubMed:15141213}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AF295367; AAK01867.1; -; mRNA.
DR   EMBL; BC096665; AAH96665.1; -; mRNA.
DR   CCDS; CCDS38442.1; -.
DR   RefSeq; NP_115776.2; NM_032400.2.
DR   AlphaFoldDB; Q99MT6; -.
DR   SMR; Q99MT6; -.
DR   STRING; 10090.ENSMUSP00000029326; -.
DR   ChEMBL; CHEMBL4739861; -.
DR   GlyGen; Q99MT6; 1 site.
DR   iPTMnet; Q99MT6; -.
DR   PhosphoSitePlus; Q99MT6; -.
DR   PaxDb; Q99MT6; -.
DR   PRIDE; Q99MT6; -.
DR   ProteomicsDB; 257373; -.
DR   Antibodypedia; 18315; 266 antibodies from 28 providers.
DR   DNASU; 84112; -.
DR   Ensembl; ENSMUST00000029326; ENSMUSP00000029326; ENSMUSG00000027762.
DR   GeneID; 84112; -.
DR   KEGG; mmu:84112; -.
DR   UCSC; uc008pja.2; mouse.
DR   CTD; 56670; -.
DR   MGI; MGI:1934135; Sucnr1.
DR   VEuPathDB; HostDB:ENSMUSG00000027762; -.
DR   eggNOG; ENOG502QVWP; Eukaryota.
DR   GeneTree; ENSGT01030000234621; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q99MT6; -.
DR   OMA; VMCFFYY; -.
DR   OrthoDB; 1133445at2759; -.
DR   PhylomeDB; Q99MT6; -.
DR   TreeFam; TF350009; -.
DR   Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 84112; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q99MT6; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q99MT6; protein.
DR   Bgee; ENSMUSG00000027762; Expressed in white adipose tissue and 49 other tissues.
DR   Genevisible; Q99MT6; MM.
DR   GO; GO:0009986; C:cell surface; TAS:MGI.
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; IDA:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; IMP:MGI.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; IMP:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0060177; P:regulation of angiotensin metabolic process; IMP:MGI.
DR   GO; GO:0002001; P:renin secretion into blood stream; IMP:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IMP:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..317
FT                   /note="Succinate receptor 1"
FT                   /id="PRO_0000070135"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..47
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..119
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..157
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..204
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..246
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..277
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..294
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..317
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        106
FT                   /note="I -> M (in Ref. 1; AAK01867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="F -> L (in Ref. 1; AAK01867)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="F -> V (in Ref. 1; AAK01867)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  36765 MW;  378C0738E108B3A5 CRC64;
     MAQNLSCENW LATEAILNKY YLSAFYAIEF IFGLLGNVTV VFGYLFCMKN WNSSNVYLFN
     LSISDFAFLC TLPILIKSYA NDKGTYGDVL CISNRYVLHT NLYTSILFLT FISMDRYLLM
     KYPFREHFLQ KKEFAILISL AVWALVTLEV LPMLTFINSV PKEEGSNCID YASSGNPEHN
     LIYSLCLTLL GFLIPLSVMC FFYYKMVVFL KRRSQQQATA LPLDKPQRLV VLAVVIFSIL
     FTPYHIMRNL RIASRLDSWP QGCTQKAIKS IYTLTRPLAF LNSAINPIFY FLMGDHYREM
     LISKFRQYFK SLTSFRT
 
 
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