NR1H4_RAT
ID NR1H4_RAT Reviewed; 469 AA.
AC Q62735;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Bile acid receptor;
DE AltName: Full=Farnesoid X-activated receptor;
DE AltName: Full=Farnesol receptor HRR-1;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 4;
DE AltName: Full=Retinoid X receptor-interacting protein 14;
DE Short=RXR-interacting protein 14;
GN Name=Nr1h4; Synonyms=Bar, Fxr, Rip14;
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], INTERACTION WITH RXRA, AND INDUCTION.
RC STRAIN=Lewis; TISSUE=Liver;
RX PubMed=7774010; DOI=10.1016/0092-8674(95)90530-8;
RA Forman B.M., Goode E., Chen J., Oro A.E., Bradley D.J., Perlmann T.,
RA Noonan D.J., Burka L.T., McMorris T., Lamph W.W., Evans R.M.,
RA Weinberger C.;
RT "Identification of a nuclear receptor that is activated by farnesol
RT metabolites.";
RL Cell 81:687-693(1995).
RN [2]
RP DNA-BINDING.
RX PubMed=10744760; DOI=10.1074/jbc.275.14.10638;
RA Laffitte B.A., Kast H.R., Nguyen C.M., Zavacki A.M., Moore D.D.,
RA Edwards P.A.;
RT "Identification of the DNA binding specificity and potential target genes
RT for the farnesoid X-activated receptor.";
RL J. Biol. Chem. 275:10638-10647(2000).
RN [3]
RP INTERACTION WITH SMARCD1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [4]
RP FUNCTION IN GLUCOSE HOMEOSTASIS.
RX PubMed=20305288; DOI=10.1194/jlr.m004929;
RA Cao R., Cronk Z.X., Zha W., Sun L., Wang X., Fang Y., Studer E., Zhou H.,
RA Pandak W.M., Dent P., Gil G., Hylemon P.B.;
RT "Bile acids regulate hepatic gluconeogenic genes and farnesoid X receptor
RT via G(alpha)i-protein-coupled receptors and the AKT pathway.";
RL J. Lipid Res. 51:2234-2244(2010).
RN [5] {ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 241-469 IN COMPLEXES WITH
RP CHENODEOXYCHOLIC ACID ANALOGS AND NCOA2 COACTIVATOR PEPTIDE.
RX PubMed=12718893; DOI=10.1016/s1097-2765(03)00112-6;
RA Mi L.Z., Devarakonda S., Harp J.M., Han Q., Pellicciari R., Willson T.M.,
RA Khorasanizadeh S., Rastinejad F.;
RT "Structural basis for bile acid binding and activation of the nuclear
RT receptor FXR.";
RL Mol. Cell 11:1093-1100(2003).
CC -!- FUNCTION: Ligand-activated transcription factor. Receptor for bile
CC acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid,
CC deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential
CC role in BA homeostasis through the regulation of genes involved in BA
CC synthesis, conjugation and enterohepatic circulation. Also regulates
CC lipid and glucose homeostasis and is involved innate immune response.
CC The FXR-RXR heterodimer binds predominantly to farnesoid X receptor
CC response elements (FXREs) containing two inverted repeats of the
CC consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1
CC nucleotide (IR-1) but also to tandem repeat DR1 sites with lower
CC affinity, and can be activated by either FXR or RXR-specific ligands.
CC It is proposed that monomeric nuclear receptors such as NR5A2/LRH-1
CC bound to coregulatory nuclear responsive element (NRE) halfsites
CC located in close proximity to FXREs modulate transcriptional activity.
CC In the liver activates transcription of the corepressor NR0B2 thereby
CC indirectly inhibiting CYP7A1 and CYP8B1 (involved in BA synthesis)
CC implicating at least in part histone demethylase KDM1A resulting in
CC epigenomic repression, and SLC10A1/NTCP (involved in hepatic uptake of
CC conjugated BAs). Activates transcription of the repressor MAFG
CC (involved in regulation of BA synthesis). Activates transcription of
CC SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP
CC (involved in bile salt export) by directly recruiting histone
CC methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of
CC conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine
CC in the small intestine). Activates transcription of SLC27A5/BACS and
CC BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt
CC export) by directly recruiting histone methyltransferase CARM1, and
CC ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4
CC (involved in secretion of phosphatidylcholine in the small intestine).
CC In the intestine activates FGF19 expression and secretion leading to
CC hepatic CYP7A1 repression. The function also involves the coordinated
CC induction of hepatic KLB/beta-klotho expression. Regulates
CC transcription of liver UGT2B4 and SULT2A1 involved in BA
CC detoxification; binding to the UGT2B4 promoter seems to imply a
CC monomeric transactivation independent of RXRA. Modulates lipid
CC homeostasis by activating liver NR0B2/SHP-mediated repression of SREBF1
CC (involved in de novo lipogenesis), expression of PLTP (involved in HDL
CC formation), SCARB1 (involved in HDL hepatic uptake), APOE, APOC1,
CC APOC4, PPARA (involved in beta-oxidation of fatty acids), VLDLR and
CC SDC1 (involved in the hepatic uptake of LDL and IDL remnants), and
CC inhibiting expression of MTTP (involved in VLDL assembly). Increases
CC expression of APOC2 (promoting lipoprotein lipase activity implicated
CC in triglyceride clearance). Transrepresses APOA1 involving a monomeric
CC competition with NR2A1 for binding to a DR1 element. Also reduces
CC triglyceride clearance by inhibiting expression of ANGPTL3 and APOC3
CC (both involved in inhibition of lipoprotein lipase). Involved in
CC glucose homeostasis by modulating hepatic gluconeogenesis through
CC activation of NR0B2/SHP-mediated repression of respective genes.
CC Modulates glycogen synthesis (inducing phosphorylation of glycogen
CC synthase kinase-3). Modulates glucose-stimulated insulin secretion and
CC is involved in insulin resistance. Involved in intestinal innate
CC immunity. Plays a role in protecting the distal small intestine against
CC bacterial overgrowth and preservation of the epithelial barrier. Down-
CC regulates inflammatory cytokine expression in several types of immune
CC cells including macrophages and mononuclear cells. Mediates trans-
CC repression of TLR4-induced cytokine expression; the function seems to
CC require its sumoylation and prevents N-CoR nuclear receptor corepressor
CC clearance from target genes such as IL1B and NOS2. Involved in the
CC TLR9-mediated protective mechanism in intestinal inflammation. Plays an
CC anti-inflammatory role in liver inflammation; proposed to inhibit pro-
CC inflammatory (but not antiapoptotic) NF-kappa-B signaling.
CC {ECO:0000250|UniProtKB:Q60641, ECO:0000250|UniProtKB:Q96RI1,
CC ECO:0000269|PubMed:10744760, ECO:0000269|PubMed:20305288}.
CC -!- SUBUNIT: Heterodimer with RXRA; the heterodimerization enhances the
CC binding affinity for LXXLL motifs from coactivators (By similarity).
CC Binds DNA predominantly as a heterodimer with RXRA. After activation by
CC agonist binding interacts with coactivators. Interacts with NCOA1,
CC NCOA2, PPARGC1A, CARM1, SETD7, PRMT1, GPS2, SMARCA4 and MED1, EP300 and
CC SMARCD1. Interacts with XRCC5 and XRCC6; decreasing NR1H4/FXR
CC transactivation activity towards ABCB11/BSEP. Interacts with PAGR1 AND
CC NCOA6; indicative for an association with an MLL2/MLL3 complex (ASCOM).
CC {ECO:0000250|UniProtKB:Q60641, ECO:0000250|UniProtKB:Q96RI1,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:7774010}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60641,
CC ECO:0000250|UniProtKB:Q96RI1, ECO:0000305}.
CC -!- INDUCTION: Heterodimer of NR1H4 and RXR activated by farnesol.
CC {ECO:0000269|PubMed:7774010}.
CC -!- PTM: Acetylated by EP300. Lys-210 as is the major acetylation site for
CC EP300; the dynamicly regulated acetylation inhibits heterodimerization
CC with RXRA and transactivation activity. Deacetylated by SIRT1.
CC {ECO:0000250|UniProtKB:Q96RI1}.
CC -!- PTM: Methylation may increase transactivation of target genes.
CC {ECO:0000250|UniProtKB:Q96RI1}.
CC -!- PTM: Phosphorylation by PKC/PRKCA increases transactivation activity by
CC promoting association with PPARGC1A. {ECO:0000250|UniProtKB:Q96RI1}.
CC -!- PTM: Sumoylated upon ligand binding. {ECO:0000250|UniProtKB:Q96RI1}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; U18374; AAC52205.1; -; mRNA.
DR PIR; A56918; A56918.
DR RefSeq; NP_068513.1; NM_021745.1.
DR PDB; 1OSV; X-ray; 2.50 A; A/B=241-469.
DR PDB; 1OT7; X-ray; 2.90 A; A/B=240-468.
DR PDBsum; 1OSV; -.
DR PDBsum; 1OT7; -.
DR AlphaFoldDB; Q62735; -.
DR SMR; Q62735; -.
DR IntAct; Q62735; 1.
DR STRING; 10116.ENSRNOP00000009910; -.
DR ChEMBL; CHEMBL4105917; -.
DR PhosphoSitePlus; Q62735; -.
DR PaxDb; Q62735; -.
DR GeneID; 60351; -.
DR KEGG; rno:60351; -.
DR UCSC; RGD:628831; rat.
DR CTD; 9971; -.
DR RGD; 628831; Nr1h4.
DR VEuPathDB; HostDB:ENSRNOG00000007197; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_12_3_1; -.
DR InParanoid; Q62735; -.
DR OrthoDB; 1137281at2759; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-RNO-211976; Endogenous sterols.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-4090294; SUMOylation of intracellular receptors.
DR EvolutionaryTrace; Q62735; -.
DR PRO; PR:Q62735; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007197; Expressed in liver and 10 other tissues.
DR ExpressionAtlas; Q62735; baseline and differential.
DR Genevisible; Q62735; RN.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0032052; F:bile acid binding; IDA:RGD.
DR GO; GO:0038181; F:bile acid receptor activity; IDA:UniProtKB.
DR GO; GO:1902122; F:chenodeoxycholic acid binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:RGD.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:RGD.
DR GO; GO:0038183; P:bile acid signaling pathway; IDA:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; ISO:RGD.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISO:RGD.
DR GO; GO:1903413; P:cellular response to bile acid; IDA:UniProtKB.
DR GO; GO:0071398; P:cellular response to fatty acid; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0035356; P:cellular triglyceride homeostasis; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0055089; P:fatty acid homeostasis; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; IEP:RGD.
DR GO; GO:0072574; P:hepatocyte proliferation; IEP:RGD.
DR GO; GO:0034971; P:histone H3-R17 methylation; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0038185; P:intracellular bile acid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:RGD.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEP:RGD.
DR GO; GO:0010876; P:lipid localization; IEP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:RGD.
DR GO; GO:0032692; P:negative regulation of interleukin-1 production; ISO:RGD.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISO:RGD.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0010868; P:negative regulation of triglyceride biosynthetic process; IMP:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; ISO:RGD.
DR GO; GO:2001250; P:positive regulation of ammonia assimilation cycle; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:2000213; P:positive regulation of glutamate metabolic process; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:RGD.
DR GO; GO:1905695; P:positive regulation of phosphatidic acid biosynthetic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0120188; P:regulation of bile acid secretion; IEP:RGD.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0010883; P:regulation of lipid storage; IEP:RGD.
DR GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0034255; P:regulation of urea metabolic process; ISO:RGD.
DR GO; GO:1904486; P:response to 17alpha-ethynylestradiol; IEP:RGD.
DR GO; GO:0070723; P:response to cholesterol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:1901557; P:response to fenofibrate; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071873; P:response to norepinephrine; IMP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:RGD.
DR CDD; cd06936; NR_LBD_Fxr; 1.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR044114; NR_LBD_NR1H4.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00546; THYROIDHORMR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; DNA-binding; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..469
FT /note="Bile acid receptor"
FT /id="PRO_0000053540"
FT DOMAIN 245..469
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 121..196
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 124..144
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 160..184
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT BINDING 328
FT /ligand="3beta,7beta-dihydroxy-5beta-cholan-24-oate"
FT /ligand_id="ChEBI:CHEBI:78602"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:12718893,
FT ECO:0007744|PDB:1OT7"
FT BINDING 328
FT /ligand="chenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36234"
FT /ligand_note="agonist"
FT /evidence="ECO:0000305|PubMed:12718893,
FT ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7"
FT BINDING 358
FT /ligand="chenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36234"
FT /ligand_note="agonist"
FT /evidence="ECO:0000305|PubMed:12718893,
FT ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7"
FT BINDING 366
FT /ligand="3beta,7beta-dihydroxy-5beta-cholan-24-oate"
FT /ligand_id="ChEBI:CHEBI:78602"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:12718893,
FT ECO:0007744|PDB:1OT7"
FT BINDING 366
FT /ligand="chenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36234"
FT /ligand_note="agonist"
FT /evidence="ECO:0000305|PubMed:12718893,
FT ECO:0007744|PDB:1OSV, ECO:0007744|PDB:1OT7"
FT BINDING 444
FT /ligand="chenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36234"
FT /ligand_note="agonist"
FT /evidence="ECO:0000305|PubMed:12718893,
FT ECO:0007744|PDB:1OSV"
FT MOD_RES 132
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT MOD_RES 151
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT MOD_RES 154
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT MOD_RES 203
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT MOD_RES 210
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT MOD_RES 439
FT /note="Phosphothreonine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q96RI1"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:1OSV"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 277..300
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 310..333
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:1OSV"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 356..371
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 398..419
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 426..448
FT /evidence="ECO:0007829|PDB:1OSV"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:1OSV"
SQ SEQUENCE 469 AA; 53935 MW; 2BEAF5847D9E403C CRC64;
MNLIGPSHLQ ATDEFALSEN LFGVLTEHAA GPLGQNLDLE SYSPYNNVQF PQVQPQISSS
SYYSNLGFYP QQPEDWYSPG LYELRRMPTE SVYQGETEVS EMPVTKKPRM AASSAGRIKG
DELCVVCGDR ASGYHYNALT CEGCKGFFRR SITKNAVYKC KNGGNCVMDM YMRRKCQDCR
LRKCREMGML AECLLTEIQC KSKRLRKNVK QHADQTVNED SEGRDLRQVT STTKLCREKT
ELTVDQQTLL DYIMDSYSKQ RMPQEITNKI LKEEFSAEEN FLILTEMATS HVQILVEFTK
RLPGFQTLDH EDQIALLKGS AVEAMFLRSA EIFNKKLPAG HADLLEERIR KSGISDEYIT
PMFSFYKSVG ELKMTQEEYA LLTAIVILSP DRQYIKDREA VEKLQEPLLD VLQKLCKIYQ
PENPQHFACL LGRLTELRTF NHHHAEMLMS WRVNDHKFTP LLCEIWDVQ
