SUCR1_RAT
ID SUCR1_RAT Reviewed; 317 AA.
AC Q6IYF9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Succinate receptor 1;
DE AltName: Full=G-protein coupled receptor 91;
GN Name=Sucnr1; Synonyms=Gpr91;
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 FUNCTION.
RC STRAIN=Sprague-Dawley;
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY612851; AAT10590.1; -; mRNA.
DR RefSeq; NP_001001518.1; NM_001001518.1.
DR PDB; 6IBB; X-ray; 2.12 A; A/C=2-317.
DR PDB; 6RNK; X-ray; 1.94 A; A=2-317.
DR PDB; 6Z10; X-ray; 2.27 A; A=2-317.
DR PDBsum; 6IBB; -.
DR PDBsum; 6RNK; -.
DR PDBsum; 6Z10; -.
DR AlphaFoldDB; Q6IYF9; -.
DR SMR; Q6IYF9; -.
DR STRING; 10116.ENSRNOP00000018767; -.
DR BindingDB; Q6IYF9; -.
DR ChEMBL; CHEMBL2150839; -.
DR GuidetoPHARMACOLOGY; 166; -.
DR GlyGen; Q6IYF9; 1 site.
DR PhosphoSitePlus; Q6IYF9; -.
DR PaxDb; Q6IYF9; -.
DR ABCD; Q6IYF9; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000018767; ENSRNOP00000018767; ENSRNOG00000014039.
DR GeneID; 408199; -.
DR KEGG; rno:408199; -.
DR UCSC; RGD:1303193; rat.
DR CTD; 56670; -.
DR RGD; 1303193; Sucnr1.
DR eggNOG; ENOG502QVWP; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR InParanoid; Q6IYF9; -.
DR OrthoDB; 1133445at2759; -.
DR PhylomeDB; Q6IYF9; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q6IYF9; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0002281; P:macrophage activation involved in immune response; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0060177; P:regulation of angiotensin metabolic process; ISO:RGD.
DR GO; GO:0002001; P:renin secretion into blood stream; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Succinate receptor 1"
FT /id="PRO_0000383594"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..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..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..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 HELIX 8..19
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 21..47
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 53..81
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 88..121
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 132..159
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6RNK"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 193..213
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 225..253
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 263..285
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:6RNK"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6RNK"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6RNK"
SQ SEQUENCE 317 AA; 36679 MW; 5971EFB7ABF6113B CRC64;
MAQNLSCENW LALENILKKY YLSAFYGIEF IVGMLGNFTV VFGYLFCMKN WNSSNVYLFN
LSISDLAFLC TLPMLIRSYA TGNWTYGDVL CISNRYVLHA NLYTSILFLT FISIDRYLLM
KFPFREHILQ KKEFAILISL AVWVLVTLEV LPMLTFITST PIEKGDSCVD YASSGNPKYS
LIYSLCLTLL GFLIPLSVMC FFYYKMVVFL KKRSQQQATV LSLNKPLRLV VLAVVIFSVL
FTPYHIMRNV RIASRLDSWP QGCSQKAIKC LYILTRPLAF LNSAVNPIFY FLVGDHFRDM
LFSKLRQYFK SLTSFRL
