NR1H2_HUMAN
ID NR1H2_HUMAN Reviewed; 460 AA.
AC P55055; A8K490; B4DNM6; E7EWA6; Q12970; Q5I0Y1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Oxysterols receptor LXR-beta;
DE AltName: Full=Liver X receptor beta;
DE AltName: Full=Nuclear receptor NER;
DE AltName: Full=Nuclear receptor subfamily 1 group H member 2;
DE AltName: Full=Ubiquitously-expressed nuclear receptor;
GN Name=NR1H2; Synonyms=LXRB, NER, UNR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Osteosarcoma, and Skin;
RX PubMed=7926814; DOI=10.1016/0378-1119(94)90080-9;
RA Shinar D.M., Endo N., Rutledge S.J., Vogel R., Rodan G.A., Schmidt A.;
RT "NER, a new member of the gene family encoding the human steroid hormone
RT nuclear receptor.";
RL Gene 147:273-276(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood, Brain, Placenta, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-460 (ISOFORM 1).
RA Song C., Konkontis J.M., Hiipakka R.A., Liao S.;
RT "Ubiquitous receptor: a novel receptor that modulates gene activation by
RT retinoic acid and thyroid hormone receptors.";
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INTERACTION WITH GPS2, SUMOYLATION AT LYS-409 AND LYS-447, AND
RP MUTAGENESIS OF LYS-409 AND LYS-447.
RX PubMed=20159957; DOI=10.1101/gad.545110;
RA Venteclef N., Jakobsson T., Ehrlund A., Damdimopoulos A., Mikkonen L.,
RA Ellis E., Nilsson L.M., Parini P., Jaenne O.A., Gustafsson J.A.,
RA Steffensen K.R., Treuter E.;
RT "GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory actions
RT of LRH-1 and LXRbeta in the hepatic acute phase response.";
RL Genes Dev. 24:381-395(2010).
RN [7]
RP INTERACTION WITH ABCA12 AND NR1H2.
RX PubMed=23931754; DOI=10.1016/j.cmet.2013.07.003;
RA Fu Y., Mukhamedova N., Ip S., D'Souza W., Henley K.J., DiTommaso T.,
RA Kesani R., Ditiatkovski M., Jones L., Lane R.M., Jennings G., Smyth I.M.,
RA Kile B.T., Sviridov D.;
RT "ABCA12 regulates ABCA1-dependent cholesterol efflux from macrophages and
RT the development of atherosclerosis.";
RL Cell Metab. 18:225-238(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH CCAR2.
RX PubMed=25661920; DOI=10.1016/j.jsbmb.2015.02.001;
RA Sakurabashi A., Wada-Hiraike O., Hirano M., Fu H., Isono W., Fukuda T.,
RA Morita Y., Tanikawa M., Miyamoto Y., Oda K., Kawana K., Osuga Y., Fujii T.;
RT "CCAR2 negatively regulates nuclear receptor LXRalpha by competing with
RT SIRT1 deacetylase.";
RL J. Steroid Biochem. Mol. Biol. 149:80-88(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 208-460 IN COMPLEX WITH SYNTHETIC
RP LIGANDS.
RX PubMed=12819202; DOI=10.1074/jbc.m304842200;
RA Farnegardh M., Bonn T., Sun S., Ljunggren J., Ahola H., Wilhelmsson A.,
RA Gustafsson J.-A., Carlquist M.;
RT "The three-dimensional structure of the liver X receptor beta reveals a
RT flexible ligand-binding pocket that can accommodate fundamentally different
RT ligands.";
RL J. Biol. Chem. 278:38821-38828(2003).
CC -!- FUNCTION: Nuclear receptor that exhibits a ligand-dependent
CC transcriptional activation activity (PubMed:25661920). Binds
CC preferentially to double-stranded oligonucleotide direct repeats having
CC the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4).
CC Regulates cholesterol uptake through MYLIP-dependent ubiquitination of
CC LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA
CC for the regulation of genes involved in liver metabolism (By
CC similarity). Induces LPCAT3-dependent phospholipid remodeling in
CC endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1
CC processing and lipogenesis (By similarity). Via LPCAT3, triggers the
CC incorporation of arachidonate into phosphatidylcholines of ER
CC membranes, increasing membrane dynamics and enabling triacylglycerols
CC transfer to nascent very low-density lipoprotein (VLDL) particles (By
CC similarity). Via LPCAT3 also counteracts lipid-induced ER stress
CC response and inflammation, likely by modulating SRC kinase membrane
CC compartmentalization and limiting the synthesis of lipid inflammatory
CC mediators (By similarity). Plays an anti-inflammatory role during the
CC hepatic acute phase response by acting as a corepressor: inhibits the
CC hepatic acute phase response by preventing dissociation of the N-Cor
CC corepressor complex (PubMed:20159957). {ECO:0000250|UniProtKB:Q60644,
CC ECO:0000269|PubMed:20159957, ECO:0000269|PubMed:25661920}.
CC -!- SUBUNIT: Forms a heterodimer with RXR. Interacts with CCAR2 (via N-
CC terminus) in a ligand-independent manner (PubMed:25661920). Interacts
CC (when sumoylated) with GPS2; interaction with GPS2 onto hepatic acute
CC phase protein promoters prevents N-Cor corepressor complex dissociation
CC (PubMed:20159957). Interacts with ABCA12 and ABCA1; this interaction is
CC required for ABCA1 localization to the cell surface and is necessary
CC for its normal activity and stability (PubMed:23931754).
CC {ECO:0000269|PubMed:12819202, ECO:0000269|PubMed:20159957,
CC ECO:0000269|PubMed:23931754, ECO:0000269|PubMed:25661920}.
CC -!- INTERACTION:
CC P55055; Q92828: CORO2A; NbExp=4; IntAct=EBI-745354, EBI-2835660;
CC P55055; Q99750: MDFI; NbExp=3; IntAct=EBI-745354, EBI-724076;
CC P55055; O75376: NCOR1; NbExp=6; IntAct=EBI-745354, EBI-347233;
CC P55055; P19793: RXRA; NbExp=3; IntAct=EBI-745354, EBI-78598;
CC P55055; P48443: RXRG; NbExp=5; IntAct=EBI-745354, EBI-712405;
CC P55055-1; Q07869-1: PPARA; NbExp=2; IntAct=EBI-21458417, EBI-21458428;
CC P55055-1; Q03181: PPARD; NbExp=2; IntAct=EBI-21458417, EBI-6426768;
CC P55055-1; P37231: PPARG; NbExp=2; IntAct=EBI-21458417, EBI-781384;
CC P55055-1; P19793: RXRA; NbExp=2; IntAct=EBI-21458417, EBI-78598;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55055-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55055-2; Sequence=VSP_053789;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Sumoylated by SUMO2 at Lys-409 and Lys-447 during the hepatic
CC acute phase response, leading to promote interaction with GPS2 and
CC prevent N-Cor corepressor complex dissociation.
CC {ECO:0000269|PubMed:20159957}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; U07132; AAA61783.1; -; mRNA.
DR EMBL; AK290855; BAF83544.1; -; mRNA.
DR EMBL; AK297978; BAG60288.1; -; mRNA.
DR EMBL; AC008655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007790; AAH07790.1; -; mRNA.
DR EMBL; BC033500; AAH33500.1; -; mRNA.
DR EMBL; BC047750; AAH47750.1; -; mRNA.
DR EMBL; BC074500; AAH74500.1; -; mRNA.
DR EMBL; U14534; AAA58594.1; -; mRNA.
DR CCDS; CCDS42593.1; -. [P55055-1]
DR CCDS; CCDS58673.1; -. [P55055-2]
DR PIR; JC4014; JC4014.
DR RefSeq; NP_001243576.1; NM_001256647.1. [P55055-2]
DR RefSeq; NP_009052.3; NM_007121.5. [P55055-1]
DR PDB; 1P8D; X-ray; 2.80 A; A/B=213-460.
DR PDB; 1PQ6; X-ray; 2.40 A; A/B/C/D=212-460.
DR PDB; 1PQ9; X-ray; 2.10 A; A/B/C/D=212-460.
DR PDB; 1PQC; X-ray; 2.80 A; A/B/C/D=212-460.
DR PDB; 1UPV; X-ray; 2.10 A; A=208-460.
DR PDB; 1UPW; X-ray; 2.40 A; A=208-460.
DR PDB; 3KFC; X-ray; 2.40 A; A/B/C/D=212-460.
DR PDB; 3L0E; X-ray; 2.30 A; A=212-460.
DR PDB; 4DK7; X-ray; 2.45 A; A/C=218-460.
DR PDB; 4DK8; X-ray; 2.75 A; A/C=218-460.
DR PDB; 4NQA; X-ray; 3.10 A; B/I=72-460.
DR PDB; 4RAK; X-ray; 2.04 A; A/B=213-460.
DR PDB; 5HJP; X-ray; 2.60 A; B/D=216-460.
DR PDB; 5I4V; X-ray; 2.61 A; A/E=210-460.
DR PDB; 5JY3; X-ray; 2.40 A; A/B/C/D=213-460.
DR PDB; 5KYA; X-ray; 2.60 A; A/E=210-460.
DR PDB; 5KYJ; X-ray; 2.80 A; A/E=210-460.
DR PDB; 6JIO; X-ray; 2.60 A; A/B/C/D=214-460.
DR PDB; 6K9G; X-ray; 2.80 A; A/B/C/D=214-460.
DR PDB; 6K9H; X-ray; 2.50 A; A/B=214-460.
DR PDB; 6K9M; X-ray; 2.90 A; A/B/C/D=214-460.
DR PDB; 6S4N; X-ray; 1.90 A; A/B/C/D=216-460.
DR PDB; 6S4T; X-ray; 2.00 A; A=216-460.
DR PDB; 6S4U; X-ray; 2.81 A; A/B/C=216-460.
DR PDB; 6S5K; X-ray; 1.60 A; A=216-460.
DR PDBsum; 1P8D; -.
DR PDBsum; 1PQ6; -.
DR PDBsum; 1PQ9; -.
DR PDBsum; 1PQC; -.
DR PDBsum; 1UPV; -.
DR PDBsum; 1UPW; -.
DR PDBsum; 3KFC; -.
DR PDBsum; 3L0E; -.
DR PDBsum; 4DK7; -.
DR PDBsum; 4DK8; -.
DR PDBsum; 4NQA; -.
DR PDBsum; 4RAK; -.
DR PDBsum; 5HJP; -.
DR PDBsum; 5I4V; -.
DR PDBsum; 5JY3; -.
DR PDBsum; 5KYA; -.
DR PDBsum; 5KYJ; -.
DR PDBsum; 6JIO; -.
DR PDBsum; 6K9G; -.
DR PDBsum; 6K9H; -.
DR PDBsum; 6K9M; -.
DR PDBsum; 6S4N; -.
DR PDBsum; 6S4T; -.
DR PDBsum; 6S4U; -.
DR PDBsum; 6S5K; -.
DR AlphaFoldDB; P55055; -.
DR SMR; P55055; -.
DR BioGRID; 113222; 64.
DR ComplexPortal; CPX-652; RXRbeta-LXRbeta nuclear hormone receptor complex.
DR ComplexPortal; CPX-678; RXRalpha-LXRbeta nuclear hormone receptor complex.
DR DIP; DIP-53004N; -.
DR IntAct; P55055; 42.
DR MINT; P55055; -.
DR STRING; 9606.ENSP00000253727; -.
DR BindingDB; P55055; -.
DR ChEMBL; CHEMBL4093; -.
DR DrugBank; DB07082; 1,1,1,3,3,3-HEXAFLUORO-2-{4-[(2,2,2-TRIFLUOROETHYL)AMINO]PHENYL}PROPAN-2-OL.
DR DrugBank; DB03848; Benzenesulfinic acid.
DR DrugBank; DB11994; Diacerein.
DR DrugBank; DB03791; GW-3965.
DR DrugBank; DB13174; Rhein.
DR DrugBank; DB07080; TO-901317.
DR GuidetoPHARMACOLOGY; 601; -.
DR SwissLipids; SLP:000001551; -.
DR MoonDB; P55055; Predicted.
DR GlyGen; P55055; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55055; -.
DR PhosphoSitePlus; P55055; -.
DR BioMuta; NR1H2; -.
DR DMDM; 296439251; -.
DR EPD; P55055; -.
DR jPOST; P55055; -.
DR MassIVE; P55055; -.
DR MaxQB; P55055; -.
DR PaxDb; P55055; -.
DR PeptideAtlas; P55055; -.
DR PRIDE; P55055; -.
DR ProteomicsDB; 18810; -.
DR ProteomicsDB; 56767; -. [P55055-1]
DR Antibodypedia; 9326; 406 antibodies from 42 providers.
DR DNASU; 7376; -.
DR Ensembl; ENST00000253727.10; ENSP00000253727.4; ENSG00000131408.15. [P55055-1]
DR Ensembl; ENST00000411902.6; ENSP00000396151.2; ENSG00000131408.15. [P55055-2]
DR Ensembl; ENST00000593926.5; ENSP00000471194.1; ENSG00000131408.15. [P55055-1]
DR Ensembl; ENST00000652203.1; ENSP00000499121.1; ENSG00000131408.15. [P55055-1]
DR GeneID; 7376; -.
DR KEGG; hsa:7376; -.
DR MANE-Select; ENST00000253727.10; ENSP00000253727.4; NM_007121.7; NP_009052.4.
DR UCSC; uc002psa.6; human. [P55055-1]
DR CTD; 7376; -.
DR DisGeNET; 7376; -.
DR GeneCards; NR1H2; -.
DR HGNC; HGNC:7965; NR1H2.
DR HPA; ENSG00000131408; Low tissue specificity.
DR MIM; 600380; gene.
DR neXtProt; NX_P55055; -.
DR OpenTargets; ENSG00000131408; -.
DR PharmGKB; PA31750; -.
DR VEuPathDB; HostDB:ENSG00000131408; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000161465; -.
DR HOGENOM; CLU_007368_12_4_1; -.
DR InParanoid; P55055; -.
DR OMA; GMREQCE; -.
DR OrthoDB; 1137281at2759; -.
DR PhylomeDB; P55055; -.
DR TreeFam; TF352167; -.
DR PathwayCommons; P55055; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-9031525; NR1H2 & NR1H3 regulate gene expression to limit cholesterol uptake.
DR Reactome; R-HSA-9031528; NR1H2 & NR1H3 regulate gene expression linked to triglyceride lipolysis in adipose.
DR Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR SignaLink; P55055; -.
DR SIGNOR; P55055; -.
DR BioGRID-ORCS; 7376; 21 hits in 1112 CRISPR screens.
DR ChiTaRS; NR1H2; human.
DR EvolutionaryTrace; P55055; -.
DR GeneWiki; Liver_X_receptor_beta; -.
DR GenomeRNAi; 7376; -.
DR Pharos; P55055; Tchem.
DR PRO; PR:P55055; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P55055; protein.
DR Bgee; ENSG00000131408; Expressed in popliteal artery and 172 other tissues.
DR ExpressionAtlas; P55055; baseline and differential.
DR Genevisible; P55055; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IMP:BHF-UCL.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060336; P:negative regulation of interferon-gamma-mediated signaling pathway; NAS:BHF-UCL.
DR GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IMP:BHF-UCL.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0032376; P:positive regulation of cholesterol transport; IDA:BHF-UCL.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IMP:BHF-UCL.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0090187; P:positive regulation of pancreatic juice secretion; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:BHF-UCL.
DR GO; GO:0090340; P:positive regulation of secretion of lysosomal enzymes; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00373; -.
DR InterPro; IPR023257; Liver_X_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_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; PR02034; LIVERXRECPTR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
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; Activator; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..460
FT /note="Oxysterols receptor LXR-beta"
FT /id="PRO_0000053532"
FT DOMAIN 222..460
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 84..161
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 87..107
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 125..149
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..85
FT /note="Transactivation AF-1; required for ligand-
FT independent transactivation function"
FT /evidence="ECO:0000269|PubMed:25661920"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..460
FT /note="Transactivation AF-2; required for ligand-dependent
FT transactivation function; mediates interaction with CCAR2"
FT /evidence="ECO:0000269|PubMed:25661920"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 409
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000269|PubMed:20159957"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000269|PubMed:20159957"
FT VAR_SEQ 61..158
FT /note="VIPDPEEEPERKRKKGPAPKMLGHELCRVCGDKASGFHYNVLSCEGCKGFFR
FT RSVVRGGARRYACRGGGTCQMDAFMRRKCQQCRLRKCKEAGMREQC -> G (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053789"
FT VARIANT 2
FT /note="S -> F (in dbSNP:rs41379547)"
FT /id="VAR_050579"
FT MUTAGEN 409
FT /note="K->R: Impaired ability to act as an anti-
FT inflammatory role during the hepatic acute phase response;
FT when associated with R-447."
FT /evidence="ECO:0000269|PubMed:20159957"
FT MUTAGEN 447
FT /note="K->R: Impaired ability to act as an anti-
FT inflammatory role during the hepatic acute phase response;
FT when associated with R-409."
FT /evidence="ECO:0000269|PubMed:20159957"
FT CONFLICT 175
FT /note="Q -> QQ (in Ref. 1; AAA61783, 2; BAF83544/BAG60288,
FT 4; AAH07790/AAH33500/AAH47750/AAH74500 and 5; AAA58594)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="D -> G (in Ref. 2; BAG60288)"
FT /evidence="ECO:0000305"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4NQA"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4NQA"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:4NQA"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4NQA"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4NQA"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4NQA"
FT HELIX 221..242
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6S4N"
FT HELIX 263..286
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 296..317
FT /evidence="ECO:0007829|PDB:6S5K"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4NQA"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:6S5K"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:6S5K"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6S4N"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 388..409
FT /evidence="ECO:0007829|PDB:6S5K"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:4RAK"
FT HELIX 416..440
FT /evidence="ECO:0007829|PDB:6S5K"
FT TURN 441..445
FT /evidence="ECO:0007829|PDB:6S5K"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:6S5K"
SQ SEQUENCE 460 AA; 50974 MW; 9465A6FFB7FCFD2F CRC64;
MSSPTTSSLD TPLPGNGPPQ PGAPSSSPTV KEEGPEPWPG GPDPDVPGTD EASSACSTDW
VIPDPEEEPE RKRKKGPAPK MLGHELCRVC GDKASGFHYN VLSCEGCKGF FRRSVVRGGA
RRYACRGGGT CQMDAFMRRK CQQCRLRKCK EAGMREQCVL SEEQIRKKKI RKQQQESQSQ
SQSPVGPQGS SSSASGPGAS PGGSEAGSQG SGEGEGVQLT AAQELMIQQL VAAQLQCNKR
SFSDQPKVTP WPLGADPQSR DARQQRFAHF TELAIISVQE IVDFAKQVPG FLQLGREDQI
ALLKASTIEI MLLETARRYN HETECITFLK DFTYSKDDFH RAGLQVEFIN PIFEFSRAMR
RLGLDDAEYA LLIAINIFSA DRPNVQEPGR VEALQQPYVE ALLSYTRIKR PQDQLRFPRM
LMKLVSLRTL SSVHSEQVFA LRLQDKKLPP LLSEIWDVHE
