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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_MOUSE             Reviewed;         360 AA.
Q9EP66;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
07-JUN-2017, entry version 122.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, AND TISSUE
SPECIFICITY.
STRAIN=129/SvJ, and C57BL/6J;
PubMed=11745392;
DOI=10.1002/1521-4141(200112)31:12<3714::AID-IMMU3714>3.0.CO;2-1;
Schaub A., Fuetterer A., Pfeffer K.;
"PUMA-G, an IFN-gamma-inducible gene in macrophages is a novel member
of the seven transmembrane spanning receptor superfamily.";
Eur. J. Immunol. 31:3714-3725(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
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).
[4]
FUNCTION.
PubMed=15929991; DOI=10.1074/jbc.C500213200;
Taggart A.K.P., Kero J., Gan X., Cai T.-Q., Cheng K., Ippolito M.,
Ren N., Kaplan R., Wu K., Wu T.-J., Jin L., Liaw C., Chen R.,
Richman J., Connolly D., Offermanns S., Wright S.D., Waters M.G.;
"(D)-beta-hydroxybutyrate inhibits adipocyte lipolysis via the
nicotinic acid receptor PUMA-G.";
J. Biol. Chem. 280:26649-26652(2005).
[5]
DISRUPTION PHENOTYPE.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
{ECO:0000269|PubMed:15929991}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed in lungs, spleen, heart, skeletal
muscle and adipose tissue. {ECO:0000269|PubMed:11745392,
ECO:0000269|PubMed:12646212}.
-!- INDUCTION: By interferon-gamma in macrophages.
{ECO:0000269|PubMed:11745392}.
-!- DISRUPTION PHENOTYPE: Niacin administration has no effect on serum
adiponectin levels in contrast to wild-type mice where levels are
decreased. {ECO:0000269|PubMed:19141678}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ300198; CAC17790.1; -; mRNA.
EMBL; AJ300199; CAC17791.1; -; Genomic_DNA.
EMBL; AK150795; BAE29858.1; -; mRNA.
CCDS; CCDS19668.1; -.
RefSeq; NP_109626.1; NM_030701.3.
UniGene; Mm.440567; -.
UniGene; Mm.486809; -.
ProteinModelPortal; Q9EP66; -.
STRING; 10090.ENSMUSP00000054104; -.
BindingDB; Q9EP66; -.
ChEMBL; CHEMBL4420; -.
GuidetoPHARMACOLOGY; 312; -.
iPTMnet; Q9EP66; -.
PhosphoSitePlus; Q9EP66; -.
PaxDb; Q9EP66; -.
PRIDE; Q9EP66; -.
Ensembl; ENSMUST00000057145; ENSMUSP00000054104; ENSMUSG00000045502.
GeneID; 80885; -.
KEGG; mmu:80885; -.
UCSC; uc008zop.3; mouse.
CTD; 338442; -.
MGI; MGI:1933383; Hcar2.
eggNOG; ENOG410IKI5; Eukaryota.
eggNOG; ENOG4110VUM; LUCA.
GeneTree; ENSGT00510000046798; -.
InParanoid; Q9EP66; -.
KO; K08402; -.
OMA; KWDWKFG; -.
OrthoDB; EOG091G0AN6; -.
PhylomeDB; Q9EP66; -.
TreeFam; TF330775; -.
Reactome; R-MMU-3296197; Hydroxycarboxylic acid-binding receptors.
Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-MMU-418594; G alpha (i) signalling events.
PRO; PR:Q9EP66; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000045502; -.
CleanEx; MM_GPR109A; -.
ExpressionAtlas; Q9EP66; baseline and differential.
Genevisible; Q9EP66; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IDA:MGI.
GO; GO:0070553; F:nicotinic acid receptor activity; ISS:UniProtKB.
GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:MGI.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
GO; GO:0001781; P:neutrophil apoptotic process; ISO:MGI.
GO; GO:0070165; P:positive regulation of adiponectin secretion; ISS: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_0000069605.
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:0000244|PubMed:21183079}.
DISULFID 97 174 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 360 AA; 41401 MW; CCCE52A2475777FC CRC64;
MSKSDHFLVI NGKNCCVFRD ENIAKVLPPV LGLEFVFGLL GNGLALWIFC FHLKSWKSSR
IFLFNLAVAD FLLIICLPFL TDNYVHNWDW RFGGIPCRVM LFMLAMNRQG SIIFLTVVAV
DRYFRVVHPH HFLNKISNRT AAIISCFLWG LTIGLTVHLL YTNMMTKNGE AYLCSSFSIC
YNFRWHDAMF LLEFFLPLAI ILFCSGRIIW SLRQRQMDRH AKIKRAINFI MVVAIVFIIC
FLPSVAVRIR IFWLLYKYNV RNCDIYSSVD LAFFTTLSFT YMNSMLDPVV YYFSSPSFPN
FFSTCINRCL RKKTLGEPDN NRSTSVELTG DPSTTRSIPG ALMADPSEPG SPPYLASTSR


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