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Hydroxycarboxylic acid receptor 3 (G-protein coupled receptor 109B) (G-protein coupled receptor HM74) (G-protein coupled receptor HM74B) (Niacin receptor 2) (Nicotinic acid receptor 2)

 HCAR3_HUMAN             Reviewed;         387 AA.
P49019; A8K4G5; B2R830; E9PI97; Q8NGE4;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 3.
25-OCT-2017, entry version 156.
RecName: Full=Hydroxycarboxylic acid receptor 3;
AltName: Full=G-protein coupled receptor 109B;
AltName: Full=G-protein coupled receptor HM74;
AltName: Full=G-protein coupled receptor HM74B;
AltName: Full=Niacin receptor 2;
AltName: Full=Nicotinic acid receptor 2;
Name=HCAR3; Synonyms=GPR109B, HCA3, HM74B, NIACR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-173; LEU-198; ARG-253;
MET-317 AND MET-346.
TISSUE=Monocyte;
PubMed=7505609; DOI=10.1093/intimm/5.10.1239;
Nomura H., Nielsen B.W., Matsushima K.;
"Molecular cloning of cDNAs encoding a LD78 receptor and putative
leukocyte chemotactic peptide receptors.";
Int. Immunol. 5:1239-1249(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-173; LEU-198;
ARG-253; MET-317 AND MET-346.
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-173; LEU-198;
ARG-253; MET-317 AND MET-346.
TISSUE=Neutrophil;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-173; LEU-198;
ARG-253; MET-317 AND MET-346.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
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).
[8]
FUNCTION, AND MUTAGENESIS OF ARG-111.
PubMed=19561068; DOI=10.1074/jbc.M109.019455;
Ahmed K., Tunaru S., Langhans C.-D., Hanson J., Michalski C.W.,
Koelker S., Jones P.M., Okun J.G., Offermanns S.;
"Deorphanization of GPR109B as a receptor for the beta-oxidation
intermediate 3-OH-octanoic acid and its role in the regulation of
lipolysis.";
J. Biol. Chem. 284:21928-21933(2009).
[9]
NOMENCLATURE.
PubMed=21454438; DOI=10.1124/pr.110.003301;
Offermanns S., Colletti S.L., Lovenberg T.W., Semple G., Wise A.,
Ijzerman A.P.;
"International union of basic and clinical pharmacology. LXXXII:
nomenclature and classification of hydroxy-carboxylic acid receptors
(GPR81, GPR109A, and GPR109B).";
Pharmacol. Rev. 63:269-290(2011).
-!- FUNCTION: Receptor for 3-OH-octanoid acid mediates a negative
feedback regulation of adipocyte lipolysis to counteract
prolipolytic influences under conditions of physiological or
pathological increases in beta-oxidation rates. Acts as a low
affinity receptor for nicotinic acid. This pharmacological effect
requires nicotinic acid doses that are much higher than those
provided by a normal diet. {ECO:0000269|PubMed:12522134,
ECO:0000269|PubMed:19561068}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expression largely restricted to adipose
tissue and spleen. {ECO:0000269|PubMed:12522134}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/gpr109b/";
-----------------------------------------------------------------------
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EMBL; D10923; BAA01721.1; -; mRNA.
EMBL; AB065865; BAC06083.1; -; Genomic_DNA.
EMBL; AK290930; BAF83619.1; -; mRNA.
EMBL; AK313212; BAG36027.1; -; mRNA.
EMBL; EU293604; ABX64359.1; -; Genomic_DNA.
EMBL; AC026333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC047891; AAH47891.1; -; mRNA.
CCDS; CCDS53842.1; -.
PIR; I69202; I69202.
RefSeq; NP_006009.2; NM_006018.2.
UniGene; Hs.458425; -.
ProteinModelPortal; P49019; -.
IntAct; P49019; 1.
STRING; 9606.ENSP00000436714; -.
BindingDB; P49019; -.
ChEMBL; CHEMBL4421; -.
DrugBank; DB00627; Niacin.
GuidetoPHARMACOLOGY; 313; -.
iPTMnet; P49019; -.
PhosphoSitePlus; P49019; -.
BioMuta; HCAR3; -.
DMDM; 519668680; -.
MaxQB; P49019; -.
PaxDb; P49019; -.
PeptideAtlas; P49019; -.
PRIDE; P49019; -.
DNASU; 8843; -.
Ensembl; ENST00000528880; ENSP00000436714; ENSG00000255398.
GeneID; 8843; -.
KEGG; hsa:8843; -.
UCSC; uc001ucy.4; human.
CTD; 8843; -.
DisGeNET; 8843; -.
EuPathDB; HostDB:ENSG00000255398.2; -.
GeneCards; HCAR3; -.
H-InvDB; HIX0036803; -.
HGNC; HGNC:16824; HCAR3.
HPA; HPA028660; -.
MIM; 606039; gene.
neXtProt; NX_P49019; -.
OpenTargets; ENSG00000255398; -.
PharmGKB; PA165512827; -.
eggNOG; ENOG410IKI5; Eukaryota.
eggNOG; ENOG4110VUM; LUCA.
GeneTree; ENSGT00510000046798; -.
HOVERGEN; HBG051680; -.
InParanoid; P49019; -.
KO; K08402; -.
OMA; KWDWKFG; -.
OrthoDB; EOG091G0AN6; -.
PhylomeDB; P49019; -.
TreeFam; TF330775; -.
Reactome; R-HSA-3296197; Hydroxycarboxylic acid-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
GenomeRNAi; 8843; -.
PRO; PR:P49019; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000255398; -.
CleanEx; HS_GPR109B; -.
Genevisible; P49019; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR028017; HCAR2/3_rcpt.
PANTHER; PTHR24231:SF0; PTHR24231:SF0; 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;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Membrane; Polymorphism; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 387 Hydroxycarboxylic acid receptor 3.
/FTId=PRO_0000069604.
TOPO_DOM 1 28 Extracellular. {ECO:0000255}.
TRANSMEM 29 50 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 51 63 Cytoplasmic. {ECO:0000255}.
TRANSMEM 64 85 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 86 102 Extracellular. {ECO:0000255}.
TRANSMEM 103 123 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 124 142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 143 163 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 164 194 Extracellular. {ECO:0000255}.
TRANSMEM 195 209 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 210 236 Cytoplasmic. {ECO:0000255}.
TRANSMEM 237 256 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 257 273 Extracellular. {ECO:0000255}.
TRANSMEM 274 298 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 299 387 Cytoplasmic. {ECO:0000255}.
DISULFID 100 177 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 173 173 T -> P (in dbSNP:rs1798192).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505609,
ECO:0000269|Ref.2}.
/FTId=VAR_038715.
VARIANT 198 198 F -> L (in dbSNP:rs17884481).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505609,
ECO:0000269|Ref.2}.
/FTId=VAR_038716.
VARIANT 253 253 H -> R (in dbSNP:rs118091133).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505609,
ECO:0000269|Ref.2}.
/FTId=VAR_038717.
VARIANT 317 317 I -> M (in dbSNP:rs116821988).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505609,
ECO:0000269|Ref.2}.
/FTId=VAR_038718.
VARIANT 346 346 I -> M (in dbSNP:rs56308926).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7505609,
ECO:0000269|Ref.2}.
/FTId=VAR_038719.
VARIANT 350 350 G -> S (in dbSNP:rs201835480).
/FTId=VAR_038720.
MUTAGEN 111 111 R->A: Abrogates completely the activation
by OH-octanoid acid.
{ECO:0000269|PubMed:19561068}.
CONFLICT 94 94 K -> N (in Ref. 1; BAA01721).
{ECO:0000305}.
SEQUENCE 387 AA; 44478 MW; 887BA427B6134A3F CRC64;
MNRHHLQDHF LEIDKKNCCV FRDDFIAKVL PPVLGLEFIF GLLGNGLALW IFCFHLKSWK
SSRIFLFNLA VADFLLIICL PFVMDYYVRR SDWKFGDIPC RLVLFMFAMN RQGSIIFLTV
VAVDRYFRVV HPHHALNKIS NWTAAIISCL LWGITVGLTV HLLKKKLLIQ NGTANVCISF
SICHTFRWHE AMFLLEFFLP LGIILFCSAR IIWSLRQRQM DRHAKIKRAI TFIMVVAIVF
VICFLPSVVV RIHIFWLLHT SGTQNCEVYR SVDLAFFITL SFTYMNSMLD PVVYYFSSPS
FPNFFSTLIN RCLQRKITGE PDNNRSTSVE LTGDPNKTRG APEALIANSG EPWSPSYLGP
TSNNHSKKGH CHQEPASLEK QLGCCIE


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