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Hydroxycarboxylic acid receptor 2 (G-protein coupled receptor 109) (G-protein coupled receptor 109A) (G-protein coupled receptor HM74) (Niacin receptor 1) (Nicotinic acid receptor) (Protein PUMA-G)

 HCAR2_RAT               Reviewed;         360 AA.
Q80Z39;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
07-JUN-2017, entry version 100.
RecName: Full=Hydroxycarboxylic acid receptor 2;
AltName: Full=G-protein coupled receptor 109;
AltName: Full=G-protein coupled receptor 109A;
AltName: Full=G-protein coupled receptor HM74;
AltName: Full=Niacin receptor 1;
AltName: Full=Nicotinic acid receptor;
AltName: Full=Protein PUMA-G;
Name=Hcar2; Synonyms=Gpr109, Gpr109a, Gpr109b, Niacr1, Pumag;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12646212; DOI=10.1016/S0006-291X(03)00342-5;
Soga T., Kamohara M., Takasaki J., Matsumoto S., Saito T., Ohishi T.,
Hiyama H., Matsuo A., Matsushime H., Furuichi K.;
"Molecular identification of nicotinic acid receptor.";
Biochem. Biophys. Res. Commun. 303:364-369(2003).
[2]
FUNCTION, TISSUE SPECIFICITY, AND CHARACTERIZATION.
PubMed=12522134; DOI=10.1074/jbc.M210695200;
Wise A., Foord S.M., Fraser N.J., Barnes A.A., Elshourbagy N.,
Eilert M., Ignar D.M., Murdock P.R., Steplewski K., Green A.,
Brown A.J., Dowell S.J., Szekeres P.G., Hassall D.G., Marshall F.H.,
Wilson S., Pike N.B.;
"Molecular identification of high and low affinity receptors for
nicotinic acid.";
J. Biol. Chem. 278:9869-9874(2003).
[3]
FUNCTION.
PubMed=19141678; DOI=10.1152/ajpendo.91004.2008;
Plaisance E.P., Lukasova M., Offermanns S., Zhang Y., Cao G.,
Judd R.L.;
"Niacin stimulates adiponectin secretion through the GPR109A
receptor.";
Am. J. Physiol. 296:E549-E558(2009).
-!- FUNCTION: Acts as a high affinity receptor for both nicotinic acid
(also known as niacin) and (D)-beta-hydroxybutyrate and mediates
increased adiponectin secretion and decreased lipolysis through
G(i)-protein-mediated inhibition of adenylyl cyclase. This
pharmacological effect requires nicotinic acid doses that are much
higher than those provided by a normal diet. Mediates nicotinic
acid-induced apoptosis in mature neutrophils. Receptor activation
by nicotinic acid results in reduced cAMP levels which may affect
activity of cAMP-dependent protein kinase A and phosphorylation of
target proteins, leading to neutrophil apoptosis. The rank order
of potency for the displacement of nicotinic acid binding is 5-
methyl pyrazole-3-carboxylic acid = pyridine-3-acetic acid >
acifran > 5-methyl nicotinic acid = acipimox >> nicotinuric acid =
nicotinamide. {ECO:0000269|PubMed:12522134,
ECO:0000269|PubMed:12646212, ECO:0000269|PubMed:19141678}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed in adipose tissue, lung and spleen.
{ECO:0000269|PubMed:12522134, ECO:0000269|PubMed:12646212}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AB103062; BAC58009.1; -; mRNA.
RefSeq; NP_852141.1; NM_181476.1.
UniGene; Rn.214478; -.
ProteinModelPortal; Q80Z39; -.
STRING; 10116.ENSRNOP00000036057; -.
BindingDB; Q80Z39; -.
ChEMBL; CHEMBL4731; -.
GuidetoPHARMACOLOGY; 312; -.
iPTMnet; Q80Z39; -.
PhosphoSitePlus; Q80Z39; -.
PaxDb; Q80Z39; -.
PRIDE; Q80Z39; -.
Ensembl; ENSRNOT00000032249; ENSRNOP00000036057; ENSRNOG00000026653.
GeneID; 353250; -.
KEGG; rno:353250; -.
UCSC; RGD:727952; rat.
CTD; 353250; -.
RGD; 727952; Hcar2.
eggNOG; ENOG410IKI5; Eukaryota.
eggNOG; ENOG4110VUM; LUCA.
GeneTree; ENSGT00510000046798; -.
InParanoid; Q80Z39; -.
KO; K08402; -.
OMA; KWDWKFG; -.
OrthoDB; EOG091G0AN6; -.
PhylomeDB; Q80Z39; -.
TreeFam; TF330775; -.
Reactome; R-RNO-3296197; Hydroxycarboxylic acid-binding receptors.
Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-RNO-418594; G alpha (i) signalling events.
PRO; PR:Q80Z39; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000026653; -.
Genevisible; Q80Z39; RN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:Ensembl.
GO; GO:0070553; F:nicotinic acid receptor activity; IDA:UniProtKB.
GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:UniProtKB.
GO; GO:0070165; P:positive regulation of adiponectin secretion; IDA:UniProtKB.
GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; ISS:UniProtKB.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR028017; HCAR2/3_rcpt.
PANTHER; PTHR24231:SF49; PTHR24231:SF49; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Apoptosis; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Membrane; Phosphoprotein; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 360 Hydroxycarboxylic acid receptor 2.
/FTId=PRO_0000069606.
TOPO_DOM 1 30 Extracellular. {ECO:0000255}.
TRANSMEM 31 51 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 52 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 82 98 Extracellular. {ECO:0000255}.
TRANSMEM 99 119 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 120 140 Cytoplasmic. {ECO:0000255}.
TRANSMEM 141 161 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 162 189 Extracellular. {ECO:0000255}.
TRANSMEM 190 210 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 211 226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 227 247 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 248 270 Extracellular. {ECO:0000255}.
TRANSMEM 271 291 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 292 360 Cytoplasmic. {ECO:0000255}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EP66}.
DISULFID 97 174 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 360 AA; 41459 MW; 975BDEBCA448A6C5 CRC64;
MSKQNHFLVI NGKNCCVFRD ENIAKVLPPV LGLEFVFGLL GNGLALWIFC FHLKSWKSSR
IFLFNLAVAD FLLIICLPFL TDNYVQNWDW RFGSIPCRVM LFMLAMNRQG SIIFLTVVAV
DRYFRVVHPH HFLNKISNRT AAIISCFLWG ITIGLTVHLL YTDMMTRNGD ANLCSSFSIC
YTFRWHDAMF LLEFFLPLGI ILFCSGRIIW SLRQRQMDRH VKIKRAINFI MVVAIVFVIC
FLPSVAVRIR IFWLLYKHNV RNCDIYSSVD LAFFTTLSFT YMNSMLDPVV YYFSSPSFPN
FFSTCINRCL RRKTLGEPDN NRSTSVELTG DPSTIRSIPG ALMTDPSEPG SPPYLASTSR


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