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Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)

 NR1H4_MOUSE             Reviewed;         488 AA.
Q60641; D3YTT2; E9QJW2; Q60642; Q60643;
27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 169.
RecName: Full=Bile acid receptor;
AltName: Full=Farnesoid X-activated receptor;
AltName: Full=Farnesol receptor HRR-1;
AltName: Full=Nuclear receptor subfamily 1 group H member 4;
AltName: Full=Retinoid X receptor-interacting protein 14;
Short=RXR-interacting protein 14;
Name=Nr1h4; Synonyms=Bar, Fxr, Rip14;
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 [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH
RXRA.
TISSUE=Liver;
PubMed=7760852; DOI=10.1210/mend.9.1.7760852;
Seol W., Choi H.S., Moore D.D.;
"Isolation of proteins that interact specifically with the retinoid X
receptor: two novel orphan receptors.";
Mol. Endocrinol. 9:72-85(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
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).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11030617; DOI=10.1016/S0092-8674(00)00062-3;
Sinal C.J., Tohkin M., Miyata M., Ward J.M., Lambert G.,
Gonzalez F.J.;
"Targeted disruption of the nuclear receptor FXR/BAR impairs bile acid
and lipid homeostasis.";
Cell 102:731-744(2000).
[5]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=11579204; DOI=10.1210/mend.15.10.0712;
Kast H.R., Nguyen C.M., Sinal C.J., Jones S.A., Laffitte B.A.,
Reue K., Gonzalez F.J., Willson T.M., Edwards P.A.;
"Farnesoid X-activated receptor induces apolipoprotein C-II
transcription: a molecular mechanism linking plasma triglyceride
levels to bile acids.";
Mol. Endocrinol. 15:1720-1728(2001).
[6]
FUNCTION, AND MUTAGENESIS OF LYS-370 AND VAL-388.
PubMed=12004058; DOI=10.1074/jbc.M200824200;
Cui J., Heard T.S., Yu J., Lo J.L., Huang L., Li Y., Schaeffer J.M.,
Wright S.D.;
"The amino acid residues asparagine 354 and isoleucine 372 of human
farnesoid X receptor confer the receptor with high sensitivity to
chenodeoxycholate.";
J. Biol. Chem. 277:25963-25969(2002).
[7]
FUNCTION.
PubMed=11706036; DOI=10.1074/jbc.M109326200;
Kast H.R., Goodwin B., Tarr P.T., Jones S.A., Anisfeld A.M.,
Stoltz C.M., Tontonoz P., Kliewer S., Willson T.M., Edwards P.A.;
"Regulation of multidrug resistance-associated protein 2 (ABCC2) by
the nuclear receptors pregnane X receptor, farnesoid X-activated
receptor, and constitutive androstane receptor.";
J. Biol. Chem. 277:2908-2915(2002).
[8]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12891557; DOI=10.1016/S0016-5085(03)00896-5;
Claudel T., Inoue Y., Barbier O., Duran-Sandoval D., Kosykh V.,
Fruchart J., Fruchart J.C., Gonzalez F.J., Staels B.;
"Farnesoid X receptor agonists suppress hepatic apolipoprotein CIII
expression.";
Gastroenterology 125:544-555(2003).
[9]
FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=12393883; DOI=10.1074/jbc.M209505200;
Zhang Y., Kast-Woelbern H.R., Edwards P.A.;
"Natural structural variants of the nuclear receptor farnesoid X
receptor affect transcriptional activation.";
J. Biol. Chem. 278:104-110(2003).
[10]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12421815; DOI=10.1074/jbc.M209525200;
Lambert G., Amar M.J., Guo G., Brewer H.B. Jr., Gonzalez F.J.,
Sinal C.J.;
"The farnesoid X-receptor is an essential regulator of cholesterol
homeostasis.";
J. Biol. Chem. 278:2563-2570(2003).
[11]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=12660231; DOI=10.1074/jbc.M302505200;
Anisfeld A.M., Kast-Woelbern H.R., Meyer M.E., Jones S.A., Zhang Y.,
Williams K.J., Willson T., Edwards P.A.;
"Syndecan-1 expression is regulated in an isoform-specific manner by
the farnesoid-X receptor.";
J. Biol. Chem. 278:20420-20428(2003).
[12]
INTERACTION WITH PPARGC1A.
PubMed=14729567; DOI=10.1101/gad.1138104;
Zhang Y., Castellani L.W., Sinal C.J., Gonzalez F.J., Edwards P.A.;
"Peroxisome proliferator-activated receptor-gamma coactivator 1alpha
(PGC-1alpha) regulates triglyceride metabolism by activation of the
nuclear receptor FXR.";
Genes Dev. 18:157-169(2004).
[13]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=15146238; DOI=10.1172/JCI21025;
Watanabe M., Houten S.M., Wang L., Moschetta A., Mangelsdorf D.J.,
Heyman R.A., Moore D.D., Auwerx J.;
"Bile acids lower triglyceride levels via a pathway involving FXR,
SHP, and SREBP-1c.";
J. Clin. Invest. 113:1408-1418(2004).
[14]
FUNCTION IN BA HOMEOSTASIS.
PubMed=16213224; DOI=10.1016/j.cmet.2005.09.001;
Inagaki T., Choi M., Moschetta A., Peng L., Cummins C.L.,
McDonald J.G., Luo G., Jones S.A., Goodwin B., Richardson J.A.,
Gerard R.D., Repa J.J., Mangelsdorf D.J., Kliewer S.A.;
"Fibroblast growth factor 15 functions as an enterohepatic signal to
regulate bile acid homeostasis.";
Cell Metab. 2:217-225(2005).
[15]
FUNCTION IN GLUCOSE HOMEOSTASIS.
PubMed=15564327; DOI=10.1210/en.2004-0965;
Stayrook K.R., Bramlett K.S., Savkur R.S., Ficorilli J., Cook T.,
Christe M.E., Michael L.F., Burris T.P.;
"Regulation of carbohydrate metabolism by the farnesoid X receptor.";
Endocrinology 146:984-991(2005).
[16]
FUNCTION BA HOMEOSTASIS.
PubMed=16946559; DOI=10.2133/dmpk.21.315;
Miyata M., Matsuda Y., Tsuchiya H., Kitada H., Akase T., Shimada M.,
Nagata K., Gonzalez F.J., Yamazoe Y.;
"Chenodeoxycholic acid-mediated activation of the farnesoid X receptor
negatively regulates hydroxysteroid sulfotransferase.";
Drug Metab. Pharmacokinet. 21:315-323(2006).
[17]
FUNCTION IN GLUCOSE HOMEOSTASIS.
PubMed=16446356; DOI=10.1074/jbc.M510258200;
Cariou B., van Harmelen K., Duran-Sandoval D., van Dijk T.H.,
Grefhorst A., Abdelkarim M., Caron S., Torpier G., Fruchart J.C.,
Gonzalez F.J., Kuipers F., Staels B.;
"The farnesoid X receptor modulates adiposity and peripheral insulin
sensitivity in mice.";
J. Biol. Chem. 281:11039-11049(2006).
[18]
FUNCTION IN GLUCOSE HOMEOSTASIS.
PubMed=16557297; DOI=10.1172/JCI25604;
Ma K., Saha P.K., Chan L., Moore D.D.;
"Farnesoid X receptor is essential for normal glucose homeostasis.";
J. Clin. Invest. 116:1102-1109(2006).
[19]
FUNCTION IN GLUCOSE HOMEOSTASIS.
PubMed=16410358; DOI=10.1073/pnas.0506982103;
Zhang Y., Lee F.Y., Barrera G., Lee H., Vales C., Gonzalez F.J.,
Willson T.M., Edwards P.A.;
"Activation of the nuclear receptor FXR improves hyperglycemia and
hyperlipidemia in diabetic mice.";
Proc. Natl. Acad. Sci. U.S.A. 103:1006-1011(2006).
[20]
FUNCTION IN ANTIBACTERIAL DEFENSE, AND TISSUE SPECIFICITY.
PubMed=16473946; DOI=10.1073/pnas.0509592103;
Inagaki T., Moschetta A., Lee Y.K., Peng L., Zhao G., Downes M.,
Yu R.T., Shelton J.M., Richardson J.A., Repa J.J., Mangelsdorf D.J.,
Kliewer S.A.;
"Regulation of antibacterial defense in the small intestine by the
nuclear bile acid receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:3920-3925(2006).
[21]
POSSIBLE FUNCTION IN TUMOR SUPPRESSION.
PubMed=19047134; DOI=10.1158/0008-5472.CAN-08-1791;
Modica S., Murzilli S., Salvatore L., Schmidt D.R., Moschetta A.;
"Nuclear bile acid receptor FXR protects against intestinal
tumorigenesis.";
Cancer Res. 68:9589-9594(2008).
[22]
INTERACTION WITH EP300, AND ACETYLATION.
PubMed=18842595; DOI=10.1074/jbc.M803531200;
Fang S., Tsang S., Jones R., Ponugoti B., Yoon H., Wu S.Y.,
Chiang C.M., Willson T.M., Kemper J.K.;
"The p300 acetylase is critical for ligand-activated farnesoid X
receptor (FXR) induction of SHP.";
J. Biol. Chem. 283:35086-35095(2008).
[23]
FUNCTION IN INFLAMMATORY RESPONSE.
PubMed=18972444; DOI=10.1002/hep.22519;
Wang Y.D., Chen W.D., Wang M., Yu D., Forman B.M., Huang W.;
"Farnesoid X receptor antagonizes nuclear factor kappaB in hepatic
inflammatory response.";
Hepatology 48:1632-1643(2008).
[24]
TISSUE SPECIFICITY.
PubMed=19393742; DOI=10.1016/j.bbadis.2009.04.004;
Renga B., Migliorati M., Mencarelli A., Fiorucci S.;
"Reciprocal regulation of the bile acid-activated receptor FXR and the
interferon-gamma-STAT-1 pathway in macrophages.";
Biochim. Biophys. Acta 1792:564-573(2009).
[25]
ACETYLATION.
PubMed=19883617; DOI=10.1016/j.cmet.2009.09.009;
Kemper J.K., Xiao Z., Ponugoti B., Miao J., Fang S., Kanamaluru D.,
Tsang S., Wu S.Y., Chiang C.M., Veenstra T.D.;
"FXR acetylation is normally dynamically regulated by p300 and SIRT1
but constitutively elevated in metabolic disease states.";
Cell Metab. 10:392-404(2009).
[26]
FUNCTION IN INTESTINAL INNATE IMMUNITY, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=19864602; DOI=10.4049/jimmunol.0803978;
Vavassori P., Mencarelli A., Renga B., Distrutti E., Fiorucci S.;
"The bile acid receptor FXR is a modulator of intestinal innate
immunity.";
J. Immunol. 183:6251-6261(2009).
[27]
INTERACTION WITH SMARCA4.
PubMed=19805516; DOI=10.1128/MCB.00825-09;
Miao J., Fang S., Lee J., Comstock C., Knudsen K.E., Kemper J.K.;
"Functional specificities of Brm and Brg-1 Swi/Snf ATPases in the
feedback regulation of hepatic bile acid biosynthesis.";
Mol. Cell. Biol. 29:6170-6181(2009).
[28]
FUNCTION IN GLUCOSE HOMEOSTASIS, AND TISSUE SPECIFICITY.
PubMed=20447400; DOI=10.1016/j.febslet.2010.04.068;
Popescu I.R., Helleboid-Chapman A., Lucas A., Vandewalle B.,
Dumont J., Bouchaert E., Derudas B., Kerr-Conte J., Caron S.,
Pattou F., Staels B.;
"The nuclear receptor FXR is expressed in pancreatic beta-cells and
protects human islets from lipotoxicity.";
FEBS Lett. 584:2845-2851(2010).
[29]
DNA-BINDING.
PubMed=20091679; DOI=10.1002/hep.23450;
Thomas A.M., Hart S.N., Kong B., Fang J., Zhong X.B., Guo G.L.;
"Genome-wide tissue-specific farnesoid X receptor binding in mouse
liver and intestine.";
Hepatology 51:1410-1419(2010).
[30]
DNA-BINDING, AND INTERACTION WITH NR5A2.
PubMed=20483916; DOI=10.1093/nar/gkq397;
Chong H.K., Infante A.M., Seo Y.K., Jeon T.I., Zhang Y., Edwards P.A.,
Xie X., Osborne T.F.;
"Genome-wide interrogation of hepatic FXR reveals an asymmetric IR-1
motif and synergy with LRH-1.";
Nucleic Acids Res. 38:6007-6017(2010).
[31]
REVIEW.
PubMed=21383957; DOI=10.1621/nrs.08005;
Modica S., Gadaleta R.M., Moschetta A.;
"Deciphering the nuclear bile acid receptor FXR paradigm.";
Nucl. Recept. Signal. 8:E005-E005(2010).
[32]
FUNCTION IN INTESTINAL INFLAMMATION.
PubMed=21242261; DOI=10.1136/gut.2010.212159;
Gadaleta R.M., van Erpecum K.J., Oldenburg B., Willemsen E.C.,
Renooij W., Murzilli S., Klomp L.W., Siersema P.D., Schipper M.E.,
Danese S., Penna G., Laverny G., Adorini L., Moschetta A.,
van Mil S.W.;
"Farnesoid X receptor activation inhibits inflammation and preserves
the intestinal barrier in inflammatory bowel disease.";
Gut 60:463-472(2011).
[33]
FUNCTION IN LIPID HOMEOSTASIS.
PubMed=21804189; DOI=10.1172/JCI45277;
Chennamsetty I., Claudel T., Kostner K.M., Baghdasaryan A., Kratky D.,
Levak-Frank S., Frank S., Gonzalez F.J., Trauner M., Kostner G.M.;
"Farnesoid X receptor represses hepatic human APOA gene expression.";
J. Clin. Invest. 121:3724-3734(2011).
[34]
REVIEW.
PubMed=22820415; DOI=10.1016/j.bbalip.2012.07.004;
Hollman D.A., Milona A., van Erpecum K.J., van Mil S.W.;
"Anti-inflammatory and metabolic actions of FXR: insights into
molecular mechanisms.";
Biochim. Biophys. Acta 1821:1443-1452(2012).
[35]
POSSIBLE FUNCTION IN PROTECTION AGAINST CHOLESTASIS.
PubMed=22057115; DOI=10.1053/j.gastro.2011.10.028;
Modica S., Petruzzelli M., Bellafante E., Murzilli S., Salvatore L.,
Celli N., Di Tullio G., Palasciano G., Moustafa T., Halilbasic E.,
Trauner M., Moschetta A.;
"Selective activation of nuclear bile acid receptor FXR in the
intestine protects mice against cholestasis.";
Gastroenterology 142:355-365(2012).
[36]
FUNCTION IN INFLAMMATORY RESPONSE.
PubMed=23372731; DOI=10.1371/journal.pone.0054472;
Renga B., Mencarelli A., Cipriani S., D'Amore C., Carino A., Bruno A.,
Francisci D., Zampella A., Distrutti E., Fiorucci S.;
"The bile acid sensor FXR is required for immune-regulatory activities
of TLR-9 in intestinal inflammation.";
PLoS ONE 8:E54472-E54472(2013).
[37]
FUNCTION IN BA HOMEOSTASIS.
PubMed=25651182; DOI=10.1016/j.cmet.2015.01.007;
de Aguiar Vallim T.Q., Tarling E.J., Ahn H., Hagey L.R.,
Romanoski C.E., Lee R.G., Graham M.J., Motohashi H., Yamamoto M.,
Edwards P.A.;
"MAFG is a transcriptional repressor of bile acid synthesis and
metabolism.";
Cell Metab. 21:298-310(2015).
[38]
FUNCTION IN BA HOMEOSTASIS***INTACT.
PubMed=25545350; DOI=10.1002/hep.27677;
Kim Y.C., Fang S., Byun S., Seok S., Kemper B., Kemper J.K.;
"Farnesoid X receptor-induced lysine-specific histone demethylase
reduces hepatic bile acid levels and protects the liver against bile
acid toxicity.";
Hepatology 62:220-231(2015).
[39]
FUNCTION IN BA HOMEOSTASIS.
PubMed=26505219; DOI=10.1210/me.2015-1226;
Fu T., Kim Y.C., Byun S., Kim D.H., Seok S., Suino-Powell K., Xu H.E.,
Kemper B., Kemper J.K.;
"FXR primes the liver for intestinal FGF15 signaling by transient
induction of beta-Klotho.";
Mol. Endocrinol. 30:92-103(2016).
-!- FUNCTION: Ligand-activated transcription factor. Receptor for bile
acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic
acid, deoxycholic acid (DCA) and allocholic acid (ACA). Plays a
essential role in BA homeostasis through the regulation of genes
involved in BA synthesis, conjugation and enterohepatic
circulation. Also regulates lipid and glucose homeostasis and is
involved in innate immune response (PubMed:11030617,
PubMed:21383957, PubMed:22820415). The FXR-RXR heterodimer binds
predominantly to farnesoid X receptor response elements (FXREs)
containing two inverted repeats of the consensus sequence 5'-
AGGTCA-3' in which the monomers are spaced by 1 nucleotide (IR-1)
but also to tandem repeat DR1 sites with lower affinity, and can
be activated by either FXR or RXR-specific ligands. It is proposed
that monomeric nuclear receptors such as NR5A2/LRH-1 bound to
coregulatory nuclear responsive element (NRE) halfsites located in
close proximity to FXREs modulate transcriptional activity
(PubMed:20091679, PubMed:20483916). In the liver activates
transcription of the corepressor NR0B2 thereby indirectly
inhibiting CYP7A1 and CYP8B1 (involved in BA synthesis)
implicating at least in part histone demethylase KDM1A resulting
in epigenomic repression, and SLC10A1/NTCP (involved in hepatic
uptake of conjugated BAs). Activates transcription of the
repressor MAFG (involved in regulation of BA synthesis)
(PubMed:21383957, PubMed:25651182, PubMed:25545350). Activates
transcription of SLC27A5/BACS and BAAT (involved in BA
conjugation), ABCB11/BSEP (involved in bile salt export) by
directly recruiting histone methyltransferase CARM1, and
ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4
(involved in secretion of phosphatidylcholine in the small
intestine) (PubMed:21383957). In ileal enterocytes activates
FABP6/IBABP (involved in cytosolic transport), SLC51A/OSTA and
SLC51B/OSTB (involved in secretion of conjugated BAs to the portal
blood), and repressor NR0B2/SHP thereby indirectly inhibiting
SLC10A2/ASBT (involved in BA uptake) (By similarity). In the
intestine activates FGF15 expression and secretion leading to
hepatic CYP7A1 repression; the function also involves the
coordinated induction of hepatic KLB/beta-klotho expression
(PubMed:16213224, PubMed:26505219). Transcriptional activation of
FABP6/IBAP and SCD1 but not of ABCB11 is isoform-specific
(PubMed:12393883). Regulates transcription of liver UGT2B4 and
SULT2A1 involved in BA detoxification; binding to the UGT2B4
promoter seems to imply a monomeric transactivation independent of
RXRA (By similarity). Modulates lipid homeostasis by activating
liver NR0B2/SHP-mediated repression of SREBF1 isoform SREBP-1C
(involved in de novo lipogenesis), expression of PLTP (involved in
HDL formation), SCARB1 (involved in HDL hepatic uptake), APOE,
APOC1, APOC4, VLDLR and SDC1 (involved in the hepatic uptake of
LDL and IDL remnants), and inhibiting expression of MTTP (involved
in VLDL assembly) (PubMed:12421815, PubMed:15146238). Increases
expression of APOC2 (promoting lipoprotein lipase activity
implicated in triglyceride clearance) (PubMed:11579204).
Transrepresses APOA1 probably involving a monomeric competition
with NR2A1 for binding to a DR1 element (PubMed:21804189). Also
reduces triglyceride clearance by inhibiting expression of ANGPTL3
and APOC3 (both involved in inhibition of lipoprotein lipase)
(PubMed:12891557, PubMed:15146238). Involved in glucose
homeostasis by modulating hepatic gluconeogenesis through
activation of NR0B2/SHP-mediated repression of respective genes.
Modulates glycogen synthesis (inducing phosphorylation of glycogen
synthase kinase-3). Modulates glucose-stimulated insulin secretion
and is involved in insulin resistance (PubMed:15564327,
PubMed:16446356, PubMed:16557297, PubMed:16410358,
PubMed:20447400). Involved in intestinal innate immunity. Plays a
role in protecting the distal small intestine against bacterial
overgrowth and preservation of the epithelial barrier
(PubMed:16473946, PubMed:21242261). Down-regulates inflammatory
cytokine expression in several types of immune cells including
macrophages and mononuclear cells (PubMed:19864602). Mediates
transrepression of TLR4-induced cytokine expression; the function
seems to require its sumoylation and prevents N-CoR nuclear
receptor corepressor clearance from target genes such as IL1B and
NOS2 (By similarity). Involved in the TLR9-mediated protective
mechanism in intestinal inflammation (PubMed:23372731). Plays a
anti-inflammatory role in liver inflammation; proposed to inhibit
proinflammatory (but not antiapoptotic) NF-kappa-B signaling
(PubMed:18972444). {ECO:0000250|UniProtKB:Q62735,
ECO:0000250|UniProtKB:Q96RI1, ECO:0000269|PubMed:11030617,
ECO:0000269|PubMed:11579204, ECO:0000269|PubMed:11706036,
ECO:0000269|PubMed:12004058, ECO:0000269|PubMed:12393883,
ECO:0000269|PubMed:12421815, ECO:0000269|PubMed:12660231,
ECO:0000269|PubMed:12891557, ECO:0000269|PubMed:15146238,
ECO:0000269|PubMed:15564327, ECO:0000269|PubMed:16213224,
ECO:0000269|PubMed:16410358, ECO:0000269|PubMed:16446356,
ECO:0000269|PubMed:16473946, ECO:0000269|PubMed:16557297,
ECO:0000269|PubMed:16946559, ECO:0000269|PubMed:18972444,
ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:20091679,
ECO:0000269|PubMed:20447400, ECO:0000269|PubMed:20483916,
ECO:0000269|PubMed:21242261, ECO:0000269|PubMed:21804189,
ECO:0000269|PubMed:23372731, ECO:0000269|PubMed:25545350,
ECO:0000269|PubMed:25651182, ECO:0000269|PubMed:26505219,
ECO:0000305|PubMed:21383957, ECO:0000305|PubMed:22820415}.
-!- FUNCTION: Isoform 2: Activates transcription of IBAP and SDC1.
{ECO:0000269|PubMed:12393883}.
-!- FUNCTION: Isoform 4: Activates transcription of IBAP and SDC1.
{ECO:0000269|PubMed:12393883}.
-!- SUBUNIT: Binds DNA predominantly as a heterodimer with RXRA
(PubMed:7760852). After activation by agonist binding interacts
with coactivators. Interacts with PPARGC1A, SMARCA4 and EP300
(PubMed:14729567, PubMed:18842595, PubMed:19805516). Interacts
with NCOA1, NCOA2, CARM1, SETD7, PRMT1, GPS2, SMARCA4 and MED1.
Interacts with XRCC5 and XRCC6; decreasing NR1H4/FXR
transactivation activity towards ABCB11/BSEP. Interacts with PAGR1
AND NCOA6; indicative for an association with an MLL2/MLL3 complex
(ASCOM) (By similarity). Interacts with NR5A2 (PubMed:20483916).
{ECO:0000250|UniProtKB:Q62735, ECO:0000250|UniProtKB:Q96RI1,
ECO:0000269|PubMed:14729567, ECO:0000269|PubMed:18842595,
ECO:0000269|PubMed:19805516, ECO:0000269|PubMed:20483916,
ECO:0000269|PubMed:7760852}.
-!- INTERACTION:
O70343-1:Ppargc1a; NbExp=3; IntAct=EBI-11659377, EBI-11359934;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19864602,
ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=FXRbeta1, FXRalpha3, FXRalpha2(+);
IsoId=Q60641-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=FXRbeta2, FXFRalpha4, FXRalpha2(-);
IsoId=Q60641-2; Sequence=VSP_003666;
Note=Produced by alternative splicing of isoform 1.;
Name=3; Synonyms=FXRalpha1, FXRalpha1(+);
IsoId=Q60641-3; Sequence=VSP_058157;
Note=Produced by alternative promoter usage.;
Name=4; Synonyms=FXRalpha2, FXRalpha1(-);
IsoId=Q60641-4; Sequence=VSP_058157, VSP_003666;
Note=Produced by alternative splicing of isoform 3.;
-!- TISSUE SPECIFICITY: Expressed in liver and kidney. Expressed in
pancreatic beta cells and macrophages. Expressed in the villus
epithelium in adult ileum, with highest expression in the
intervillus regions. Expression in colon is reduced by
inflammation. {ECO:0000269|PubMed:16473946,
ECO:0000269|PubMed:19393742, ECO:0000269|PubMed:19864602,
ECO:0000269|PubMed:20447400}.
-!- PTM: Acetylated by EP300 (PubMed:18842595). Lys-228 as is the
major acetylation site for EP300; the dynamicly regulated
acetylation inhibits heterodimerization with RXRA and
transactivation activity. Deacetylated by SIRT1 (By similarity).
Elevated acetylation levels are found in metabolic disease states
(mouse models of obesity and type II diabetes) (PubMed:19883617).
{ECO:0000250|UniProtKB:Q96RI1, ECO:0000269|PubMed:18842595,
ECO:0000269|PubMed:19883617}.
-!- PTM: Methylation may increase transactivation of target genes.
{ECO:0000250|UniProtKB:Q96RI1}.
-!- PTM: Phosphorylation by PKC/PRKCA increases transactivation
activity by promoting association with PPARGC1A.
{ECO:0000250|UniProtKB:Q96RI1}.
-!- PTM: Sumoylated upon ligand binding.
{ECO:0000250|UniProtKB:Q96RI1}.
-!- DISEASE: Note=Activation protects mice against cholestasis,
development of chronical intestinal inflammation and fibrosis. May
suppress intestinal tumorigenesis. {ECO:0000269|PubMed:19047134,
ECO:0000269|PubMed:19864602, ECO:0000269|PubMed:22057115}.
-!- DISRUPTION PHENOTYPE: Elevated serum bile acid, cholesterol, and
triglycerides, increased hepatic cholesterol and triglycerides,
and a proatherogenic serum lipoprotein profile. Reduced bile acid
pools and reduced fecal bile acid excretion.
{ECO:0000269|PubMed:11030617}.
-!- MISCELLANEOUS: Mouse Nr1h4/FXR is less responsive to CDCA and more
responsive to cholic acid (CA) than human FXR.
{ECO:0000305|PubMed:12004058, ECO:0000305|PubMed:21383957}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U09416; AAC53066.1; -; mRNA.
EMBL; U09417; AAC53065.1; -; mRNA.
EMBL; U09418; AAC52978.1; -; mRNA.
EMBL; AC152417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015261; AAH15261.1; -; mRNA.
CCDS; CCDS24116.1; -. [Q60641-2]
CCDS; CCDS48668.1; -. [Q60641-1]
CCDS; CCDS48669.1; -. [Q60641-3]
PIR; I49018; I49018.
PIR; I49019; I49019.
PIR; I49020; I49020.
RefSeq; NP_001156976.1; NM_001163504.1. [Q60641-3]
RefSeq; NP_001157172.1; NM_001163700.1. [Q60641-1]
RefSeq; XP_006513454.1; XM_006513391.3. [Q60641-3]
RefSeq; XP_006513456.1; XM_006513393.3. [Q60641-4]
UniGene; Mm.3095; -.
ProteinModelPortal; Q60641; -.
SMR; Q60641; -.
BioGrid; 203043; 7.
DIP; DIP-443N; -.
IntAct; Q60641; 1.
STRING; 10090.ENSMUSP00000100933; -.
BindingDB; Q60641; -.
ChEMBL; CHEMBL5343; -.
iPTMnet; Q60641; -.
PhosphoSitePlus; Q60641; -.
PaxDb; Q60641; -.
PRIDE; Q60641; -.
Ensembl; ENSMUST00000058126; ENSMUSP00000053092; ENSMUSG00000047638. [Q60641-2]
Ensembl; ENSMUST00000105296; ENSMUSP00000100933; ENSMUSG00000047638. [Q60641-1]
Ensembl; ENSMUST00000105297; ENSMUSP00000100934; ENSMUSG00000047638. [Q60641-3]
GeneID; 20186; -.
KEGG; mmu:20186; -.
UCSC; uc007gsg.2; mouse. [Q60641-1]
UCSC; uc007gsh.2; mouse.
CTD; 9971; -.
MGI; MGI:1352464; Nr1h4.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136372; -.
HOGENOM; HOG000220843; -.
HOVERGEN; HBG108655; -.
InParanoid; Q60641; -.
KO; K08537; -.
OMA; MPQEITN; -.
OrthoDB; EOG091G0I4P; -.
TreeFam; TF316304; -.
Reactome; R-MMU-159418; Recycling of bile acids and salts.
Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-211976; Endogenous sterols.
Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
PRO; PR:Q60641; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000047638; -.
CleanEx; MM_NR1H4; -.
ExpressionAtlas; Q60641; baseline and differential.
Genevisible; Q60641; MM.
GO; GO:0005719; C:nuclear euchromatin; ISO:MGI.
GO; GO:0032052; F:bile acid binding; IMP:BHF-UCL.
GO; GO:0038181; F:bile acid receptor activity; ISO:MGI.
GO; GO:1902122; F:chenodeoxycholic acid binding; ISO:MGI.
GO; GO:0004879; F:nuclear receptor activity; IMP:BHF-UCL.
GO; GO:0046965; F:retinoid X receptor binding; IDA:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0004887; F:thyroid hormone receptor activity; IEA:InterPro.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IGI:MGI.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0008206; P:bile acid metabolic process; IMP:MGI.
GO; GO:0038183; P:bile acid signaling pathway; IMP:BHF-UCL.
GO; GO:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0071417; P:cellular response to organonitrogen compound; IMP:BHF-UCL.
GO; GO:0035356; P:cellular triglyceride homeostasis; ISO:MGI.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
GO; GO:0034971; P:histone H3-R17 methylation; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0072615; P:interleukin-17 secretion; ISO:MGI.
GO; GO:0038185; P:intracellular bile acid receptor signaling pathway; ISO:MGI.
GO; GO:0030522; P:intracellular receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; ISO:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; ISO:MGI.
GO; GO:0032692; P:negative regulation of interleukin-1 production; IMP:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; ISO:MGI.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IC:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:UniProtKB.
GO; GO:2001250; P:positive regulation of ammonia assimilation cycle; IMP:BHF-UCL.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IDA:UniProtKB.
GO; GO:2000213; P:positive regulation of glutamate metabolic process; IMP:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:1905695; P:positive regulation of phosphatidic acid biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:2000188; P:regulation of cholesterol homeostasis; IMP:UniProtKB.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; ISO:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0034255; P:regulation of urea metabolic process; IMP:BHF-UCL.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:MGI.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IMP:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; IDA:UniProtKB.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001728; ThyrH_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
PRINTS; PR00546; THYROIDHORMR.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative promoter usage;
Alternative splicing; Complete proteome; DNA-binding; Immunity;
Inflammatory response; Innate immunity; Metal-binding; Methylation;
Nucleus; Phosphoprotein; Receptor; Reference proteome; Repressor;
Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 488 Bile acid receptor.
/FTId=PRO_0000053539.
DNA_BIND 135 210 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 138 158 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 174 198 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 258 476 Ligand-binding. {ECO:0000250}.
REGION 344 352 Agonist binding.
{ECO:0000250|UniProtKB:Q62735}.
BINDING 377 377 Agonist. {ECO:0000250|UniProtKB:Q62735}.
BINDING 385 385 Agonist. {ECO:0000250|UniProtKB:Q62735}.
BINDING 463 463 Agonist. {ECO:0000250|UniProtKB:Q62735}.
BINDING 485 485 Agonist. {ECO:0000250|UniProtKB:Q62735}.
MOD_RES 146 146 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:Q96RI1}.
MOD_RES 165 165 Phosphoserine; by PKC/PRKCA.
{ECO:0000250|UniProtKB:Q96RI1}.
MOD_RES 168 168 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:Q96RI1}.
MOD_RES 221 221 N6-methyllysine; by SETD7.
{ECO:0000250|UniProtKB:Q96RI1}.
MOD_RES 228 228 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:Q96RI1}.
MOD_RES 458 458 Phosphothreonine; by PKC/PRKCZ.
{ECO:0000250|UniProtKB:Q96RI1}.
VAR_SEQ 1 36 MVMQFQGLENPIQISLHHSHRLSGFVPEGMSVKPAK -> M
NLIGHSHLQATDEFSLSESLF (in isoform 3 and
isoform 4).
{ECO:0000303|PubMed:12393883}.
/FTId=VSP_058157.
VAR_SEQ 208 211 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:12393883,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7760852}.
/FTId=VSP_003666.
MUTAGEN 370 370 K->N: Increases affinity to CDCA and
transcriptional activity in response to
CDCA; when associated with I-388.
{ECO:0000269|PubMed:12004058}.
MUTAGEN 388 388 V->I: Increases affinity to CDCA and
transcriptional activity in response to
CDCA; when associated with N-370.
{ECO:0000269|PubMed:12004058}.
CONFLICT 28 28 E -> D (in Ref. 1; AAC53066 and 3;
AAH15261). {ECO:0000305}.
CONFLICT 199 199 K -> R (in Ref. 1; AAC53065/AAC53066/
AAC52978 and 3; AAH15261). {ECO:0000305}.
CONFLICT 235 235 A -> V (in Ref. 1; AAC53065/AAC53066/
AAC52978 and 3; AAH15261). {ECO:0000305}.
SEQUENCE 488 AA; 55994 MW; 3E59B7146F8ECC86 CRC64;
MVMQFQGLEN PIQISLHHSH RLSGFVPEGM SVKPAKGMLT EHAAGPLGQN LDLESYSPYN
NVPFPQVQPQ ISSSSYYSNL GFYPQQPEDW YSPGIYELRR MPAETGYQGE TEVSEMPVTK
KPRMAAASAG RIKGDELCVV CGDRASGYHY NALTCEGCKG FFRRSITKNA VYKCKNGGNC
VMDMYMRRKC QECRLRKCKE MGMLAECMYT GLLTEIQCKS KRLRKNVKQH ADQTANEDDS
EGRDLRQVTS TTKFCREKTE LTADQQTLLD YIMDSYNKQR MPQEITNKIL KEEFSAEENF
LILTEMATSH VQILVEFTKK LPGFQTLDHE DQIALLKGSA VEAMFLRSAE IFNKKLPAGH
ADLLEERIRK SGISDEYITP MFSFYKSVGE LKMTQEEYAL LTAIVILSPD RQYIKDREAV
EKLQEPLLDV LQKLCKMYQP ENPQHFACLL GRLTELRTFN HHHAEMLMSW RVNDHKFTPL
LCEIWDVQ


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