RXRA_HUMAN
ID RXRA_HUMAN Reviewed; 462 AA.
AC P19793; B3KY83; Q2NL52; Q2V504;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Retinoic acid receptor RXR-alpha;
DE AltName: Full=Nuclear receptor subfamily 2 group B member 1;
DE AltName: Full=Retinoid X receptor alpha;
GN Name=RXRA; Synonyms=NR2B1;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=2159111; DOI=10.1038/345224a0;
RA Mangelsdorf D.J., Ong E.S., Dyck J.A., Evans R.M.;
RT "Nuclear receptor that identifies a novel retinoic acid response pathway.";
RL Nature 345:224-229(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
RX PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
RA Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
RT "DNA-binding profiling of human hormone nuclear receptors via fluorescence
RT correlation spectroscopy in a cell-free system.";
RL FEBS Lett. 582:2737-2744(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Amygdala;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
RG NIEHS SNPs program;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND IDENTIFICATION OF LIGAND.
RX PubMed=1310260; DOI=10.1016/0092-8674(92)90479-v;
RA Heyman R.A., Mangelsdorf D.J., Dyck J.A., Stein R.B., Eichele G.,
RA Evans R.M., Thaller C.;
RT "9-cis retinoic acid is a high affinity ligand for the retinoid X
RT receptor.";
RL Cell 68:397-406(1992).
RN [9]
RP FUNCTION, AND INTERACTION WITH NCOA3.
RX PubMed=9267036; DOI=10.1016/s0092-8674(00)80516-4;
RA Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
RA Privalsky M.L., Nakatani Y., Evans R.M.;
RT "Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and
RT forms a multimeric activation complex with P/CAF and CBP/p300.";
RL Cell 90:569-580(1997).
RN [10]
RP INTERACTION WITH NCOA6.
RX PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
RA Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y., Jung Y.-K.,
RA Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D., Jhun B.-H.,
RA Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
RT "A nuclear factor ASC-2, as a cancer-amplified transcriptional coactivator
RT essential for ligand-dependent transactivation by nuclear receptors in
RT vivo.";
RL J. Biol. Chem. 274:34283-34293(1999).
RN [11]
RP FUNCTION, AND HETERODIMERIZATION WITH PPARA.
RX PubMed=10195690; DOI=10.1016/s0303-7207(98)00217-2;
RA Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.;
RT "Conserved amino acids in the ligand-binding and tau(i) domains of the
RT peroxisome proliferator-activated receptor alpha are necessary for
RT heterodimerization with RXR.";
RL Mol. Cell. Endocrinol. 147:37-47(1999).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT SER-27, AND MUTAGENESIS OF SER-27.
RX PubMed=11162439; DOI=10.1006/bbrc.2000.4043;
RA Harish S., Ashok M.S., Khanam T., Rangarajan P.N.;
RT "Serine 27, a human retinoid X receptor alpha residue, phosphorylated by
RT protein kinase A is essential for cyclicAMP-mediated downregulation of
RT RXRalpha function.";
RL Biochem. Biophys. Res. Commun. 279:853-857(2000).
RN [13]
RP INTERACTION WITH SFPQ.
RX PubMed=11259580; DOI=10.1128/mcb.21.7.2298-2311.2001;
RA Mathur M., Tucker P.W., Samuels H.H.;
RT "PSF is a novel corepressor that mediates its effect through Sin3A and the
RT DNA binding domain of nuclear hormone receptors.";
RL Mol. Cell. Biol. 21:2298-2311(2001).
RN [14]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION) AND PPARA,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11915042; DOI=10.1053/jhep.2002.32470;
RA Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K., Shintani Y.,
RA Fujie H., Matsuura Y., Koike K., Miyamura T.;
RT "Interaction of hepatitis C virus core protein with retinoid X receptor
RT alpha modulates its transcriptional activity.";
RL Hepatology 35:937-946(2002).
RN [15]
RP INTERACTION WITH PRMT2.
RX PubMed=12039952; DOI=10.1074/jbc.m201053200;
RA Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
RT "Identification of protein arginine methyltransferase 2 as a coactivator
RT for estrogen receptor alpha.";
RL J. Biol. Chem. 277:28624-28630(2002).
RN [16]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 158-PHE-PHE-159 AND
RP 160-LYS--LYS-165.
RX PubMed=12145331; DOI=10.1210/me.2001-0345;
RA Pruefer K., Barsony J.;
RT "Retinoid X receptor dominates the nuclear import and export of the
RT unliganded vitamin D receptor.";
RL Mol. Endocrinol. 16:1738-1751(2002).
RN [17]
RP INTERACTION WITH DNTTIP2.
RX PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
RA Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W., Rao S.M.,
RA Zhu Y.-J.;
RT "ERBP, a novel estrogen receptor binding protein enhancing the activity of
RT estrogen receptor.";
RL Biochem. Biophys. Res. Commun. 317:54-59(2004).
RN [18]
RP INTERACTION WITH RNF8.
RX PubMed=14981089; DOI=10.1074/jbc.m309148200;
RA Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T.,
RA Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L., Moriwaki H.,
RA Kojima S., Okano Y.;
RT "The RING finger protein, RNF8, interacts with retinoid X receptor alpha
RT and enhances its transcription-stimulating activity.";
RL J. Biol. Chem. 279:18926-18934(2004).
RN [19]
RP INTERACTION WITH RARA AND NR4A1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 357-MET--MET-360 AND 418-LEU--LEU-430.
RX PubMed=15509776; DOI=10.1128/mcb.24.22.9705-9725.2004;
RA Cao X., Liu W., Lin F., Li H., Kolluri S.K., Lin B., Han Y.H., Dawson M.I.,
RA Zhang X.K.;
RT "Retinoid X receptor regulates Nur77/TR3-dependent apoptosis [corrected] by
RT modulating its nuclear export and mitochondrial targeting.";
RL Mol. Cell. Biol. 24:9705-9725(2004).
RN [20]
RP INTERACTION WITH PELP1.
RX PubMed=16574651; DOI=10.1074/jbc.m601593200;
RA Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.;
RT "9-cis-retinoic acid up-regulates expression of transcriptional coregulator
RT PELP1, a novel coactivator of the retinoid X receptor alpha pathway.";
RL J. Biol. Chem. 281:15394-15404(2006).
RN [21]
RP SUMOYLATION AT LYS-108, AND INTERACTION WITH SENP6.
RX PubMed=16912044; DOI=10.1074/jbc.m604033200;
RA Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H.,
RA Baek S.H., Bang O.S., Chung C.H.;
RT "Negative modulation of RXRalpha transcriptional activity by small
RT ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-
RT specific protease SUSP1.";
RL J. Biol. Chem. 281:30669-30677(2006).
RN [22]
RP SUBUNIT, INTERACTION WITH EP300 AND NR4A1, SUBCELLULAR LOCATION,
RP ACETYLATION AT LYS-145 BY EP300, AND MUTAGENESIS OF 133-HIS--LYS-156;
RP LYS-145; 206-GLN--ASN-216 AND 352-GLU--THR-462.
RX PubMed=17761950; DOI=10.1210/me.2007-0107;
RA Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z.,
RA Wu Q.;
RT "Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X
RT receptor-alpha.";
RL Mol. Endocrinol. 21:2877-2889(2007).
RN [23]
RP HETERODIMERIZATION WITH RARA.
RX PubMed=17205979; DOI=10.1074/mcp.m600223-mcp200;
RA Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
RT "Lysine trimethylation of retinoic acid receptor-alpha: a novel means to
RT regulate receptor function.";
RL Mol. Cell. Proteomics 6:677-688(2007).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [25]
RP INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND NCOR2.
RX PubMed=19786558; DOI=10.1124/mol.109.057000;
RA Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y.,
RA Makishima M.;
RT "The basic helix-loop-helix proteins differentiated embryo chondrocyte
RT (DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
RL Mol. Pharmacol. 76:1360-1369(2009).
RN [26]
RP INTERACTION WITH TACC1.
RX PubMed=20078863; DOI=10.1186/1471-2199-11-3;
RA Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
RT "The transforming acidic coiled coil (TACC1) protein modulates the
RT transcriptional activity of the nuclear receptors TR and RAR.";
RL BMC Mol. Biol. 11:3-3(2010).
RN [27]
RP FUNCTION, HETERODIMERIZATION WITH RARA, AND MUTAGENESIS OF SER-27.
RX PubMed=20215566; DOI=10.1210/en.2009-1338;
RA Santos N.C., Kim K.H.;
RT "Activity of retinoic acid receptor-alpha is directly regulated at its
RT protein kinase A sites in response to follicle-stimulating hormone
RT signaling.";
RL Endocrinology 151:2361-2372(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP FUNCTION.
RX PubMed=25417649; DOI=10.1038/ncomms6494;
RA Ma F., Liu S.Y., Razani B., Arora N., Li B., Kagechika H., Tontonoz P.,
RA Nunez V., Ricote M., Cheng G.;
RT "Retinoid X receptor alpha attenuates host antiviral response by
RT suppressing type I interferon.";
RL Nat. Commun. 5:5494-5494(2014).
RN [32]
RP FUNCTION, TISSUE SPECIFICITY, AND REPRESSION BY AGING.
RX PubMed=26463675; DOI=10.1093/brain/awv289;
RA Natrajan M.S., de la Fuente A.G., Crawford A.H., Linehan E., Nunez V.,
RA Johnson K.R., Wu T., Fitzgerald D.C., Ricote M., Bielekova B.,
RA Franklin R.J.;
RT "Retinoid X receptor activation reverses age-related deficiencies in myelin
RT debris phagocytosis and remyelination.";
RL Brain 138:3581-3597(2015).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP FUNCTION, INTERACTION WITH RARA, SUBCELLULAR LOCATION, AND INDUCTION BY
RP PULSATILE SHEAR STRESS.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
RN [35]
RP INTERACTION WITH VDR.
RX PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
RA Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
RA Kitanaka S.;
RT "Functional analyses of a novel missense and other mutations of the vitamin
RT D receptor in association with alopecia.";
RL Sci. Rep. 7:5102-5102(2017).
RN [36]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=30216632; DOI=10.1111/acel.12831;
RA Ma X., Warnier M., Raynard C., Ferrand M., Kirsh O., Defossez P.A.,
RA Martin N., Bernard D.;
RT "The nuclear receptor RXRA controls cellular senescence by regulating
RT calcium signaling.";
RL Aging Cell 17:E12831-E12831(2018).
RN [37]
RP STRUCTURE BY NMR OF 130-223.
RX PubMed=7925381; DOI=10.1111/j.1432-1033.1994.00639.x;
RA Lee M.S., Sem D.S., Kliewer S.A., Provencal J., Evans R.M., Wright P.E.;
RT "NMR assignments and secondary structure of the retinoid X receptor alpha
RT DNA-binding domain. Evidence for the novel C-terminal helix.";
RL Eur. J. Biochem. 224:639-650(1994).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
RX PubMed=7746322; DOI=10.1038/375203a0;
RA Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.;
RT "Structural determinants of nuclear receptor assembly on DNA direct
RT repeats.";
RL Nature 375:203-211(1995).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
RX PubMed=7760929; DOI=10.1038/375377a0;
RA Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D.;
RT "Crystal structure of the ligand-binding domain of the human nuclear
RT receptor RXR-alpha.";
RL Nature 375:377-382(1995).
RN [40]
RP STRUCTURE BY NMR OF 130-212.
RX PubMed=9698548; DOI=10.1006/jmbi.1998.1908;
RA Holmbeck S.M., Foster M.P., Casimiro D.R., Sem D.S., Dyson H.J.,
RA Wright P.E.;
RT "High-resolution solution structure of the retinoid X receptor DNA-binding
RT domain.";
RL J. Mol. Biol. 281:271-284(1998).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA AND
RP DNA.
RX PubMed=10698945; DOI=10.1093/emboj/19.5.1045;
RA Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.;
RT "Structure of the RXR-RAR DNA-binding complex on the retinoic acid response
RT element DR1.";
RL EMBO J. 19:1045-1054(2000).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO FORMS.
RX PubMed=10835357; DOI=10.1093/emboj/19.11.2592;
RA Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D.;
RT "Crystal structure of the human RXRalpha ligand-binding domain bound to its
RT natural ligand: 9-cis retinoic acid.";
RL EMBO J. 19:2592-2601(2000).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO FORMS.
RX PubMed=10970886; DOI=10.1101/gad.802300;
RA Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V.,
RA Xu H.E.;
RT "Structural basis for autorepression of retinoid X receptor by tetramer
RT formation and the AF-2 helix.";
RL Genes Dev. 14:2229-2241(2000).
RN [44] {ECO:0007744|PDB:1BY4}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-209 IN COMPLEX WITH ZINC AND
RP DNA, AND SUBUNIT.
RX PubMed=10669605; DOI=10.1006/jmbi.1999.3457;
RA Zhao Q., Chasse S.A., Devarakonda S., Sierk M.L., Ahvazi B., Rastinejad F.;
RT "Structural basis of RXR-DNA interactions.";
RL J. Mol. Biol. 296:509-520(2000).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARG;
RP COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC AGONISTS
RP ROSIGLITAZONE AND GI262570.
RX PubMed=10882139; DOI=10.1016/s1097-2765(00)80448-7;
RA Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K.,
RA Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.;
RT "Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the
RT molecular basis of heterodimerization among nuclear receptors.";
RL Mol. Cell 5:545-555(2000).
RN [46] {ECO:0007744|PDB:1K74}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA OR
RP PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC AGONIST
RP GW409544.
RX PubMed=11698662; DOI=10.1073/pnas.241410198;
RA Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B.,
RA Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.,
RA Moore J.T., Willson T.M.;
RT "Structural determinants of ligand binding selectivity between the
RT peroxisome proliferator-activated receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
RN [47]
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH
RP M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE CONTAMINANT
RP TCPOBOP.
RX PubMed=15610733; DOI=10.1016/j.molcel.2004.11.036;
RA Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J., Kliewer S.A.,
RA Xu H.E.;
RT "The nuclear xenobiotic receptor CAR: structural determinants of
RT constitutive activation and heterodimerization.";
RL Mol. Cell 16:893-905(2004).
RN [48] {ECO:0007744|PDB:2ACL}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 225-462 IN COMPLEX WITH ALL-TRANS
RP RETINOATE, AND FUNCTION.
RX PubMed=16107141; DOI=10.1021/jm050532w;
RA Jaye M.C., Krawiec J.A., Campobasso N., Smallwood A., Qiu C., Lu Q.,
RA Kerrigan J.J., De Los Frailes Alvaro M., Laffitte B., Liu W.S.,
RA Marino J.P. Jr., Meyer C.R., Nichols J.A., Parks D.J., Perez P.,
RA Sarov-Blat L., Seepersaud S.D., Steplewski K.M., Thompson S.K., Wang P.,
RA Watson M.A., Webb C.L., Haigh D., Caravella J.A., Macphee C.H.,
RA Willson T.M., Collins J.L.;
RT "Discovery of substituted maleimides as liver X receptor agonists and
RT determination of a ligand-bound crystal structure.";
RL J. Med. Chem. 48:5419-5422(2005).
RN [49] {ECO:0007744|PDB:3FAL}
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 225-462 IN COMPLEX WITH ALL-TRANS
RP RETINOATE, AND FUNCTION.
RX PubMed=18800767; DOI=10.1021/jm800612u;
RA Chao E.Y., Caravella J.A., Watson M.A., Campobasso N., Ghisletti S.,
RA Billin A.N., Galardi C., Wang P., Laffitte B.A., Iannone M.A.,
RA Goodwin B.J., Nichols J.A., Parks D.J., Stewart E., Wiethe R.W.,
RA Williams S.P., Smallwood A., Pearce K.H., Glass C.K., Willson T.M.,
RA Zuercher W.J., Collins J.L.;
RT "Structure-guided design of N-phenyl tertiary amines as transrepression-
RT selective liver X receptor modulators with anti-inflammatory activity.";
RL J. Med. Chem. 51:5758-5765(2008).
RN [50] {ECO:0007744|PDB:3FC6}
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 225-462 IN COMPLEX WITH ALL-TRANS
RP RETINOATE, AND FUNCTION.
RX PubMed=19167885; DOI=10.1016/j.bmcl.2009.01.004;
RA Washburn D.G., Hoang T.H., Campobasso N., Smallwood A., Parks D.J.,
RA Webb C.L., Frank K.A., Nord M., Duraiswami C., Evans C., Jaye M.,
RA Thompson S.K.;
RT "Synthesis and SAR of potent LXR agonists containing an indole
RT pharmacophore.";
RL Bioorg. Med. Chem. Lett. 19:1097-1100(2009).
RN [51] {ECO:0007744|PDB:5UAN}
RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 98-462 IN COMPLEX WITH RARB AND
RP DNA, AND FUNCTION.
RX PubMed=29021580; DOI=10.1038/s41467-017-00981-y;
RA Chandra V., Wu D., Li S., Potluri N., Kim Y., Rastinejad F.;
RT "The quaternary architecture of RARbeta-RXRalpha heterodimer facilitates
RT domain-domain signal transmission.";
RL Nat. Commun. 8:868-868(2017).
RN [52] {ECO:0007744|PDB:6A5Y}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 225-462 IN COMPLEX WITH NR1H4;
RP NCOA1 PEPTIDE AND 9-CIS RETINOATE, AND MUTAGENESIS OF GLU-434.
RX PubMed=30275017; DOI=10.1074/jbc.ra118.004652;
RA Wang N., Zou Q., Xu J., Zhang J., Liu J.;
RT "Ligand binding and heterodimerization with retinoid X receptor alpha
RT (RXRalpha) induce farnesoid X receptor (FXR) conformational changes
RT affecting coactivator binding.";
RL J. Biol. Chem. 293:18180-18191(2018).
CC -!- FUNCTION: Receptor for retinoic acid that acts as a transcription
CC factor (PubMed:11162439, PubMed:11915042). Forms homo- or heterodimers
CC with retinoic acid receptors (RARs) and binds to target response
CC elements in response to their ligands, all-trans or 9-cis retinoic
CC acid, to regulate gene expression in various biological processes
CC (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:28167758,
CC PubMed:17761950, PubMed:16107141, PubMed:18800767, PubMed:19167885).
CC The RAR/RXR heterodimers bind to the retinoic acid response elements
CC (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to
CC regulate transcription (PubMed:10195690, PubMed:11162439,
CC PubMed:11915042, PubMed:17761950, PubMed:28167758). The high affinity
CC ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid
CC (PubMed:1310260). In the absence of ligand, the RXR-RAR heterodimers
CC associate with a multiprotein complex containing transcription
CC corepressors that induce histone deacetylation, chromatin condensation
CC and transcriptional suppression (PubMed:20215566). On ligand binding,
CC the corepressors dissociate from the receptors and coactivators are
CC recruited leading to transcriptional activation (PubMed:20215566,
CC PubMed:9267036). Serves as a common heterodimeric partner for a number
CC of nuclear receptors, such as RARA, RARB and PPARA (PubMed:10195690,
CC PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB
CC heterodimer can act as a transcriptional repressor or transcriptional
CC activator, depending on the RARE DNA element context (PubMed:29021580).
CC The RXRA/PPARA heterodimer is required for PPARA transcriptional
CC activity on fatty acid oxidation genes such as ACOX1 and the P450
CC system genes (PubMed:10195690). Together with RARA, positively
CC regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1
CC signaling response to pulsatile shear stress in vascular endothelial
CC cells (PubMed:28167758). Acts as an enhancer of RARA binding to RARE
CC DNA element (PubMed:28167758). May facilitate the nuclear import of
CC heterodimerization partners such as VDR and NR4A1 (PubMed:12145331,
CC PubMed:15509776). Promotes myelin debris phagocytosis and remyelination
CC by macrophages (PubMed:26463675). Plays a role in the attenuation of
CC the innate immune system in response to viral infections, possibly by
CC negatively regulating the transcription of antiviral genes such as type
CC I IFN genes (PubMed:25417649). Involved in the regulation of calcium
CC signaling by repressing ITPR2 gene expression, thereby controlling
CC cellular senescence (PubMed:30216632). {ECO:0000269|PubMed:10195690,
CC ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:11915042,
CC ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:1310260,
CC ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16107141,
CC ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18800767,
CC ECO:0000269|PubMed:19167885, ECO:0000269|PubMed:20215566,
CC ECO:0000269|PubMed:25417649, ECO:0000269|PubMed:26463675,
CC ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:29021580,
CC ECO:0000269|PubMed:30216632, ECO:0000269|PubMed:9267036}.
CC -!- SUBUNIT: Homodimer (PubMed:10669605, PubMed:17761950). Heterodimer (via
CC C-terminus) with RARA; required for ligand-dependent retinoic acid
CC receptor transcriptional activity; association with RARA is enhanced by
CC pulsatile shear stress (PubMed:28167758, PubMed:10698945,
CC PubMed:15509776). Heterodimer with PPARA (via the leucine-like zipper
CC in the LBD); the interaction is required for PPARA transcriptional
CC activity (PubMed:10195690, PubMed:11915042, PubMed:11698662).
CC Heterodimerizes with PPARG (PubMed:10882139, PubMed:11698662).
CC Heterodimerizes (via NR LBD) with RARB (PubMed:29021580).
CC Heterodimerizes with NR1H4; the heterodimerization enhances the binding
CC affinity for LXXLL motifs from coactivators (PubMed:30275017).
CC Interacts with NCOA3 and NCOA6 coactivators (PubMed:9267036,
CC PubMed:10567404). Interacts with coactivator FAM120B (By similarity).
CC Interacts with coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8
CC (PubMed:16574651, PubMed:16912044, PubMed:11259580, PubMed:15047147,
CC PubMed:14981089). Interacts with PRMT2 (PubMed:12039952). Interacts
CC with ASXL1 (By similarity). Interacts with BHLHE40/DEC1, BHLHE41/DEC2,
CC NCOR1 and NCOR2 (PubMed:19786558). Interacts in a ligand-dependent
CC fashion with MED1 and NCOA1 (PubMed:19786558, PubMed:10882139,
CC PubMed:11698662). Interacts with VDR (PubMed:28698609). Interacts with
CC EP300; the interaction is decreased by 9-cis retinoic acid
CC (PubMed:17761950). Heterodimer (via C-terminus) with NR4A1 (via DNA-
CC binding domain); DNA-binding of the heterodimer is enhanced by 9-cis
CC retinoic acid (PubMed:17761950, PubMed:15509776). NR4A1 competes with
CC EP300 for interaction with RXRA and thereby attenuates EP300 mediated
CC acetylation of RXRA (PubMed:17761950). In the absence of hormonal
CC ligand, interacts with TACC1 (PubMed:20078863).
CC {ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:10195690,
CC ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10669605,
CC ECO:0000269|PubMed:10698945, ECO:0000269|PubMed:10882139,
CC ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11698662,
CC ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12039952,
CC ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:15047147,
CC ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16574651,
CC ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17761950,
CC ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:20078863,
CC ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:28698609,
CC ECO:0000269|PubMed:29021580, ECO:0000269|PubMed:30275017,
CC ECO:0000269|PubMed:9267036}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via the DNA binding domain)
CC with HCV core protein; the interaction enhances the transcriptional
CC activities of the RXRA/RARA and the RXRA/PPARA heterodimers.
CC {ECO:0000269|PubMed:11915042}.
CC -!- INTERACTION:
CC P19793; O14503: BHLHE40; NbExp=4; IntAct=EBI-78598, EBI-711810;
CC P19793; P35637: FUS; NbExp=3; IntAct=EBI-78598, EBI-400434;
CC P19793; Q15648: MED1; NbExp=6; IntAct=EBI-78598, EBI-394459;
CC P19793; Q71SY5: MED25; NbExp=4; IntAct=EBI-78598, EBI-394558;
CC P19793; Q15788: NCOA1; NbExp=14; IntAct=EBI-78598, EBI-455189;
CC P19793; Q15596: NCOA2; NbExp=5; IntAct=EBI-78598, EBI-81236;
CC P19793; P55055: NR1H2; NbExp=3; IntAct=EBI-78598, EBI-745354;
CC P19793; P55055-1: NR1H2; NbExp=2; IntAct=EBI-78598, EBI-21458417;
CC P19793; Q13133: NR1H3; NbExp=8; IntAct=EBI-78598, EBI-781356;
CC P19793; P27986: PIK3R1; NbExp=8; IntAct=EBI-78598, EBI-79464;
CC P19793; P37231: PPARG; NbExp=3; IntAct=EBI-78598, EBI-781384;
CC P19793; P37231-1: PPARG; NbExp=6; IntAct=EBI-78598, EBI-15664691;
CC P19793; P10276: RARA; NbExp=14; IntAct=EBI-78598, EBI-413374;
CC P19793; P42224: STAT1; NbExp=2; IntAct=EBI-78598, EBI-1057697;
CC P19793; P11473: VDR; NbExp=6; IntAct=EBI-78598, EBI-286357;
CC P19793; P97792-1: Cxadr; Xeno; NbExp=2; IntAct=EBI-78598, EBI-15903843;
CC P19793; Q9JLI4: Ncoa6; Xeno; NbExp=2; IntAct=EBI-78598, EBI-286271;
CC P19793; P04625: THRA; Xeno; NbExp=4; IntAct=EBI-78598, EBI-286261;
CC P19793; PRO_0000278730 [Q03463]; Xeno; NbExp=3; IntAct=EBI-78598, EBI-9159704;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12145331,
CC ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950,
CC ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:12145331,
CC ECO:0000269|PubMed:15509776}. Mitochondrion
CC {ECO:0000269|PubMed:17761950}. Note=Localization to the nucleus is
CC enhanced by vitamin D3 (PubMed:15509776). Nuclear localization may be
CC enhanced by the interaction with heterodimerization partner VDR
CC (PubMed:12145331). Translocation to the mitochondrion upon interaction
CC with NR4A1 (PubMed:17761950, PubMed:15509776). Increased nuclear
CC localization upon pulsatile shear stress (PubMed:28167758).
CC {ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776,
CC ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:28167758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P19793-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19793-2; Sequence=VSP_056565;
CC -!- TISSUE SPECIFICITY: Expressed in lung fibroblasts (at protein level)
CC (PubMed:30216632). Expressed in monocytes (PubMed:26463675). Highly
CC expressed in liver, also found in kidney and brain (PubMed:24275569,
CC PubMed:2159111, PubMed:14702039). {ECO:0000269|PubMed:14702039,
CC ECO:0000269|PubMed:2159111, ECO:0000269|PubMed:24275569,
CC ECO:0000269|PubMed:26463675, ECO:0000269|PubMed:30216632}.
CC -!- INDUCTION: Down-regulated by aging (PubMed:26463675). Induced by
CC pulsatile shear stress (PubMed:28167758). {ECO:0000269|PubMed:26463675,
CC ECO:0000269|PubMed:28167758}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain (AF1
CC domain), a DNA-binding domain and a C-terminal ligand-binding domain
CC (AF2 domain).
CC -!- PTM: Acetylated by EP300; acetylation enhances DNA binding and
CC transcriptional activity. {ECO:0000269|PubMed:17761950}.
CC -!- PTM: Phosphorylated on serine and threonine residues mainly in the N-
CC terminal modulating domain (By similarity). Constitutively
CC phosphorylated on Ser-21 in the presence or absence of ligand (By
CC similarity). Under stress conditions, hyperphosphorylated by activated
CC JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By similarity).
CC Phosphorylated on Ser-27, in vitro, by PKA (PubMed:11162439). This
CC phosphorylation is required for repression of cAMP-mediated
CC transcriptional activity of RARA (PubMed:11162439).
CC {ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:11162439}.
CC -!- PTM: Sumoylation negatively regulates transcriptional activity.
CC Desumoylated specifically by SENP6. {ECO:0000269|PubMed:16912044}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/rxra/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Retinoid X receptor entry;
CC URL="https://en.wikipedia.org/wiki/Retinoid_X_receptor";
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DR EMBL; X52773; CAA36982.1; -; mRNA.
DR EMBL; AB307705; BAH02296.1; -; mRNA.
DR EMBL; AK131192; BAG54745.1; -; mRNA.
DR EMBL; AC156789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL683798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88123.1; -; Genomic_DNA.
DR EMBL; BC110998; AAI10999.1; -; mRNA.
DR EMBL; DQ303444; ABB96254.1; -; Genomic_DNA.
DR CCDS; CCDS35172.1; -. [P19793-1]
DR PIR; S09592; S09592.
DR RefSeq; NP_001278850.1; NM_001291921.1. [P19793-2]
DR RefSeq; NP_002948.1; NM_002957.5. [P19793-1]
DR PDB; 1BY4; X-ray; 2.10 A; A/B/C/D=129-209.
DR PDB; 1DSZ; X-ray; 1.70 A; B=129-212.
DR PDB; 1FBY; X-ray; 2.25 A; A/B=224-462.
DR PDB; 1FM6; X-ray; 2.10 A; A/U=225-462.
DR PDB; 1FM9; X-ray; 2.10 A; A=225-462.
DR PDB; 1G1U; X-ray; 2.50 A; A/B/C/D=225-462.
DR PDB; 1G5Y; X-ray; 2.00 A; A/B/C/D=225-462.
DR PDB; 1K74; X-ray; 2.30 A; A=225-462.
DR PDB; 1MV9; X-ray; 1.90 A; A=223-462.
DR PDB; 1MVC; X-ray; 1.90 A; A=223-462.
DR PDB; 1MZN; X-ray; 1.90 A; A/C/E/G=223-462.
DR PDB; 1R0N; X-ray; 2.60 A; A=130-206.
DR PDB; 1RDT; X-ray; 2.40 A; A=225-462.
DR PDB; 1RXR; NMR; -; A=130-212.
DR PDB; 1XLS; X-ray; 2.96 A; A/B/C/D=227-458.
DR PDB; 1XV9; X-ray; 2.70 A; A/C=227-462.
DR PDB; 1XVP; X-ray; 2.60 A; A/C=227-462.
DR PDB; 1YNW; X-ray; 3.00 A; B=130-228.
DR PDB; 2ACL; X-ray; 2.80 A; A/C/E/G=225-462.
DR PDB; 2NLL; X-ray; 1.90 A; A=135-200.
DR PDB; 2P1T; X-ray; 1.80 A; A=223-462.
DR PDB; 2P1U; X-ray; 2.20 A; A=223-462.
DR PDB; 2P1V; X-ray; 2.20 A; A=223-462.
DR PDB; 2ZXZ; X-ray; 3.00 A; A=223-462.
DR PDB; 2ZY0; X-ray; 2.90 A; A/C=223-462.
DR PDB; 3DZU; X-ray; 3.20 A; A=11-462.
DR PDB; 3DZY; X-ray; 3.10 A; A=11-462.
DR PDB; 3E00; X-ray; 3.10 A; A=11-462.
DR PDB; 3E94; X-ray; 1.90 A; A=223-462.
DR PDB; 3FAL; X-ray; 2.36 A; A/C=225-462.
DR PDB; 3FC6; X-ray; 2.06 A; A/C=225-462.
DR PDB; 3FUG; X-ray; 2.00 A; A=223-462.
DR PDB; 3H0A; X-ray; 2.10 A; A=228-455.
DR PDB; 3KWY; X-ray; 2.30 A; A=223-462.
DR PDB; 3NSP; X-ray; 2.90 A; A/B=223-462.
DR PDB; 3NSQ; X-ray; 2.60 A; A/B=223-462.
DR PDB; 3OAP; X-ray; 2.05 A; A=228-458.
DR PDB; 3OZJ; X-ray; 2.10 A; A/C=225-462.
DR PDB; 3PCU; X-ray; 2.00 A; A=229-458.
DR PDB; 3R29; X-ray; 2.90 A; A/B=223-462.
DR PDB; 3R2A; X-ray; 3.00 A; A/B/C/D=223-462.
DR PDB; 3R5M; X-ray; 2.80 A; A/C=223-462.
DR PDB; 3UVV; X-ray; 2.95 A; B=225-462.
DR PDB; 4CN2; X-ray; 2.07 A; C/D=130-212.
DR PDB; 4CN3; X-ray; 2.35 A; A/B/C=130-212, D=130-173, D=175-212.
DR PDB; 4CN5; X-ray; 2.00 A; A/B=130-212.
DR PDB; 4CN7; X-ray; 2.34 A; A/B/E/F=130-212.
DR PDB; 4J5W; X-ray; 2.80 A; C/D=227-462.
DR PDB; 4J5X; X-ray; 2.80 A; C/D=227-462.
DR PDB; 4K4J; X-ray; 2.00 A; A=228-458.
DR PDB; 4K6I; X-ray; 2.10 A; A=228-458.
DR PDB; 4M8E; X-ray; 2.40 A; A=228-458.
DR PDB; 4M8H; X-ray; 2.20 A; A=228-458.
DR PDB; 4N5G; X-ray; 2.11 A; A/B/C/D=223-462.
DR PDB; 4N8R; X-ray; 2.03 A; A/B/C/D=223-462.
DR PDB; 4NQA; X-ray; 3.10 A; A/H=98-462.
DR PDB; 4OC7; X-ray; 2.50 A; A=223-462.
DR PDB; 4POH; X-ray; 2.30 A; A=228-458.
DR PDB; 4POJ; X-ray; 2.00 A; A=228-458.
DR PDB; 4PP3; X-ray; 2.00 A; A=228-458.
DR PDB; 4PP5; X-ray; 2.00 A; A=228-458.
DR PDB; 4RFW; X-ray; 2.40 A; A=228-458.
DR PDB; 4RMC; X-ray; 2.70 A; A=228-458.
DR PDB; 4RMD; X-ray; 1.90 A; A=228-462.
DR PDB; 4RME; X-ray; 2.30 A; A=228-462.
DR PDB; 4ZO1; X-ray; 3.22 A; B=231-455.
DR PDB; 4ZSH; X-ray; 1.80 A; A=223-462.
DR PDB; 5EC9; X-ray; 2.30 A; A=229-456.
DR PDB; 5JI0; X-ray; 1.98 A; A=223-462.
DR PDB; 5LYQ; X-ray; 2.17 A; A=223-462.
DR PDB; 5MJ5; X-ray; 1.90 A; A=229-457.
DR PDB; 5MK4; X-ray; 2.00 A; A/C=229-457.
DR PDB; 5MKJ; X-ray; 2.50 A; A=229-458.
DR PDB; 5MKU; X-ray; 1.78 A; A=229-456.
DR PDB; 5MMW; X-ray; 2.70 A; A=229-457.
DR PDB; 5TBP; X-ray; 2.60 A; A/B/C/D=223-462.
DR PDB; 5UAN; X-ray; 3.51 A; A=98-462.
DR PDB; 5Z12; X-ray; 2.75 A; B/C=228-458.
DR PDB; 5ZQU; X-ray; 2.60 A; A/B/C/D=224-462.
DR PDB; 6A5Y; X-ray; 2.10 A; D=225-462.
DR PDB; 6A5Z; X-ray; 2.95 A; D/L=225-462.
DR PDB; 6A60; X-ray; 3.05 A; D=225-462.
DR PDB; 6FBQ; X-ray; 1.60 A; A/B=130-212.
DR PDB; 6FBR; X-ray; 2.10 A; A/B=130-212.
DR PDB; 6HN6; X-ray; 2.71 A; A=201-462.
DR PDB; 6JNO; X-ray; 2.65 A; A/B/C/D=224-462.
DR PDB; 6JNR; X-ray; 2.30 A; A/B=224-462.
DR PDB; 6L6K; X-ray; 1.80 A; A=224-462.
DR PDB; 6LB4; X-ray; 1.50 A; A=224-462.
DR PDB; 6LB5; X-ray; 2.40 A; A/C=224-462.
DR PDB; 6LB6; X-ray; 2.40 A; A=224-462.
DR PDB; 6SJM; X-ray; 2.52 A; A=229-456.
DR PDB; 6STI; X-ray; 1.89 A; A=223-462.
DR PDB; 6XWG; X-ray; 2.40 A; C=130-212.
DR PDB; 6XWH; X-ray; 2.10 A; C/D=130-212.
DR PDB; 7A77; X-ray; 1.50 A; A=223-462.
DR PDB; 7B88; X-ray; 2.38 A; A=229-456.
DR PDB; 7B9O; X-ray; 2.05 A; A=229-456.
DR PDB; 7BK4; X-ray; 2.80 A; A/C=223-462.
DR PDB; 7CFO; X-ray; 2.15 A; A/B/C/D=224-462.
DR PDB; 7NKE; X-ray; 2.35 A; A/C=223-462.
DR PDBsum; 1BY4; -.
DR PDBsum; 1DSZ; -.
DR PDBsum; 1FBY; -.
DR PDBsum; 1FM6; -.
DR PDBsum; 1FM9; -.
DR PDBsum; 1G1U; -.
DR PDBsum; 1G5Y; -.
DR PDBsum; 1K74; -.
DR PDBsum; 1MV9; -.
DR PDBsum; 1MVC; -.
DR PDBsum; 1MZN; -.
DR PDBsum; 1R0N; -.
DR PDBsum; 1RDT; -.
DR PDBsum; 1RXR; -.
DR PDBsum; 1XLS; -.
DR PDBsum; 1XV9; -.
DR PDBsum; 1XVP; -.
DR PDBsum; 1YNW; -.
DR PDBsum; 2ACL; -.
DR PDBsum; 2NLL; -.
DR PDBsum; 2P1T; -.
DR PDBsum; 2P1U; -.
DR PDBsum; 2P1V; -.
DR PDBsum; 2ZXZ; -.
DR PDBsum; 2ZY0; -.
DR PDBsum; 3DZU; -.
DR PDBsum; 3DZY; -.
DR PDBsum; 3E00; -.
DR PDBsum; 3E94; -.
DR PDBsum; 3FAL; -.
DR PDBsum; 3FC6; -.
DR PDBsum; 3FUG; -.
DR PDBsum; 3H0A; -.
DR PDBsum; 3KWY; -.
DR PDBsum; 3NSP; -.
DR PDBsum; 3NSQ; -.
DR PDBsum; 3OAP; -.
DR PDBsum; 3OZJ; -.
DR PDBsum; 3PCU; -.
DR PDBsum; 3R29; -.
DR PDBsum; 3R2A; -.
DR PDBsum; 3R5M; -.
DR PDBsum; 3UVV; -.
DR PDBsum; 4CN2; -.
DR PDBsum; 4CN3; -.
DR PDBsum; 4CN5; -.
DR PDBsum; 4CN7; -.
DR PDBsum; 4J5W; -.
DR PDBsum; 4J5X; -.
DR PDBsum; 4K4J; -.
DR PDBsum; 4K6I; -.
DR PDBsum; 4M8E; -.
DR PDBsum; 4M8H; -.
DR PDBsum; 4N5G; -.
DR PDBsum; 4N8R; -.
DR PDBsum; 4NQA; -.
DR PDBsum; 4OC7; -.
DR PDBsum; 4POH; -.
DR PDBsum; 4POJ; -.
DR PDBsum; 4PP3; -.
DR PDBsum; 4PP5; -.
DR PDBsum; 4RFW; -.
DR PDBsum; 4RMC; -.
DR PDBsum; 4RMD; -.
DR PDBsum; 4RME; -.
DR PDBsum; 4ZO1; -.
DR PDBsum; 4ZSH; -.
DR PDBsum; 5EC9; -.
DR PDBsum; 5JI0; -.
DR PDBsum; 5LYQ; -.
DR PDBsum; 5MJ5; -.
DR PDBsum; 5MK4; -.
DR PDBsum; 5MKJ; -.
DR PDBsum; 5MKU; -.
DR PDBsum; 5MMW; -.
DR PDBsum; 5TBP; -.
DR PDBsum; 5UAN; -.
DR PDBsum; 5Z12; -.
DR PDBsum; 5ZQU; -.
DR PDBsum; 6A5Y; -.
DR PDBsum; 6A5Z; -.
DR PDBsum; 6A60; -.
DR PDBsum; 6FBQ; -.
DR PDBsum; 6FBR; -.
DR PDBsum; 6HN6; -.
DR PDBsum; 6JNO; -.
DR PDBsum; 6JNR; -.
DR PDBsum; 6L6K; -.
DR PDBsum; 6LB4; -.
DR PDBsum; 6LB5; -.
DR PDBsum; 6LB6; -.
DR PDBsum; 6SJM; -.
DR PDBsum; 6STI; -.
DR PDBsum; 6XWG; -.
DR PDBsum; 6XWH; -.
DR PDBsum; 7A77; -.
DR PDBsum; 7B88; -.
DR PDBsum; 7B9O; -.
DR PDBsum; 7BK4; -.
DR PDBsum; 7CFO; -.
DR PDBsum; 7NKE; -.
DR AlphaFoldDB; P19793; -.
DR BMRB; P19793; -.
DR SASBDB; P19793; -.
DR SMR; P19793; -.
DR BioGRID; 112168; 144.
DR ComplexPortal; CPX-496; RXRalpha-PXR nuclear receptor complex.
DR ComplexPortal; CPX-508; RXRalpha-RARalpha retinoic acid receptor complex.
DR ComplexPortal; CPX-513; RXRalpha-NCOA2 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-5342; RXRalpha-NCOA1 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-631; RXRalpha-VDR nuclear hormone receptor complex.
DR ComplexPortal; CPX-632; RXRalpha-LXRalpha nuclear hormone receptor complex.
DR ComplexPortal; CPX-654; RXRalpha-TRbeta nuclear hormone receptor complex.
DR ComplexPortal; CPX-662; RXRalpha-TRalpha nuclear hormone receptor complex.
DR ComplexPortal; CPX-664; RXRalpha-RXRalpha retinoic acid receptor complex.
DR ComplexPortal; CPX-678; RXRalpha-LXRbeta nuclear hormone receptor complex.
DR ComplexPortal; CPX-816; RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex.
DR CORUM; P19793; -.
DR DIP; DIP-641N; -.
DR ELM; P19793; -.
DR IntAct; P19793; 53.
DR MINT; P19793; -.
DR STRING; 9606.ENSP00000419692; -.
DR BindingDB; P19793; -.
DR ChEMBL; CHEMBL2061; -.
DR DrugBank; DB08063; 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE.
DR DrugBank; DB08402; 2-[(2,4-DICHLOROBENZOYL)AMINO]-5-(PYRIMIDIN-2-YLOXY)BENZOIC ACID.
DR DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DR DrugBank; DB07557; 3,20-Pregnanedione.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00210; Adapalene.
DR DrugBank; DB01436; Alfacalcidol.
DR DrugBank; DB00523; Alitretinoin.
DR DrugBank; DB00132; alpha-Linolenic acid.
DR DrugBank; DB04557; Arachidonic Acid.
DR DrugBank; DB00307; Bexarotene.
DR DrugBank; DB01393; Bezafibrate.
DR DrugBank; DB03756; Doconexent.
DR DrugBank; DB00749; Etodolac.
DR DrugBank; DB00926; Etretinate.
DR DrugBank; DB05956; EVT-101.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB02746; Phthalic Acid.
DR DrugBank; DB00412; Rosiglitazone.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB08601; Tributyltin.
DR DrugCentral; P19793; -.
DR GuidetoPHARMACOLOGY; 610; -.
DR SwissLipids; SLP:000001552; -.
DR MoonDB; P19793; Predicted.
DR GlyGen; P19793; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19793; -.
DR PhosphoSitePlus; P19793; -.
DR BioMuta; RXRA; -.
DR DMDM; 133701; -.
DR EPD; P19793; -.
DR jPOST; P19793; -.
DR MassIVE; P19793; -.
DR MaxQB; P19793; -.
DR PaxDb; P19793; -.
DR PeptideAtlas; P19793; -.
DR PRIDE; P19793; -.
DR ProteomicsDB; 3832; -.
DR ProteomicsDB; 53687; -. [P19793-1]
DR Antibodypedia; 3881; 430 antibodies from 41 providers.
DR DNASU; 6256; -.
DR Ensembl; ENST00000481739.2; ENSP00000419692.1; ENSG00000186350.12. [P19793-1]
DR GeneID; 6256; -.
DR KEGG; hsa:6256; -.
DR MANE-Select; ENST00000481739.2; ENSP00000419692.1; NM_002957.6; NP_002948.1.
DR UCSC; uc004cfb.3; human. [P19793-1]
DR CTD; 6256; -.
DR DisGeNET; 6256; -.
DR GeneCards; RXRA; -.
DR HGNC; HGNC:10477; RXRA.
DR HPA; ENSG00000186350; Tissue enhanced (skeletal).
DR MIM; 180245; gene.
DR neXtProt; NX_P19793; -.
DR OpenTargets; ENSG00000186350; -.
DR PharmGKB; PA34890; -.
DR VEuPathDB; HostDB:ENSG00000186350; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000159789; -.
DR HOGENOM; CLU_007368_5_4_1; -.
DR InParanoid; P19793; -.
DR OMA; NAVSHIC; -.
DR PhylomeDB; P19793; -.
DR TreeFam; TF352097; -.
DR PathwayCommons; P19793; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
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-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-HSA-9632974; NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; P19793; -.
DR SIGNOR; P19793; -.
DR BioGRID-ORCS; 6256; 52 hits in 1110 CRISPR screens.
DR ChiTaRS; RXRA; human.
DR EvolutionaryTrace; P19793; -.
DR GeneWiki; Retinoid_X_receptor_alpha; -.
DR GenomeRNAi; 6256; -.
DR Pharos; P19793; Tclin.
DR PRO; PR:P19793; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P19793; protein.
DR Bgee; ENSG00000186350; Expressed in skin of hip and 203 other tissues.
DR ExpressionAtlas; P19793; baseline and differential.
DR Genevisible; P19793; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0050692; F:DNA binding domain binding; IDA:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:GO_Central.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:CAFA.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IPI:BHF-UCL.
DR GO; GO:0042277; F:peptide binding; IDA:CAFA.
DR GO; GO:0001972; F:retinoic acid binding; IDA:CAFA.
DR GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IC:ComplexPortal.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; TAS:BHF-UCL.
DR GO; GO:0002157; P:positive regulation of thyroid hormone mediated signaling pathway; IDA:ComplexPortal.
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:GO_Central.
DR GO; GO:0032411; P:positive regulation of transporter activity; TAS:BHF-UCL.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IMP:BHF-UCL.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:ComplexPortal.
DR DisProt; DP00062; -.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR IDEAL; IID00031; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR021780; Nuc_recep-AF1.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF11825; Nuc_recep-AF1; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00545; RETINOIDXR.
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; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
KW Host-virus interaction; Isopeptide bond; Metal-binding; Mitochondrion;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..462
FT /note="Retinoic acid receptor RXR-alpha"
FT /id="PRO_0000053566"
FT DOMAIN 227..458
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 135..200
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 135..155
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 171..195
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..134
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..165
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12145331"
FT REGION 201..224
FT /note="Hinge"
FT REGION 206..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..368
FT /note="Required for nuclear export"
FT /evidence="ECO:0000269|PubMed:15509776"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10669605,
FT ECO:0007744|PDB:1BY4"
FT BINDING 316
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000269|PubMed:30275017,
FT ECO:0007744|PDB:6A5Y"
FT BINDING 316
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000269|PubMed:16107141,
FT ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885,
FT ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL,
FT ECO:0007744|PDB:3FC6"
FT BINDING 327
FT /ligand="9-cis-retinoate"
FT /ligand_id="ChEBI:CHEBI:78630"
FT /evidence="ECO:0000269|PubMed:30275017,
FT ECO:0007744|PDB:6A5Y"
FT BINDING 327
FT /ligand="all-trans-retinoate"
FT /ligand_id="ChEBI:CHEBI:35291"
FT /evidence="ECO:0000269|PubMed:16107141,
FT ECO:0000269|PubMed:18800767, ECO:0000269|PubMed:19167885,
FT ECO:0007744|PDB:2ACL, ECO:0007744|PDB:3FAL,
FT ECO:0007744|PDB:3FC6"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11162439"
FT MOD_RES 56
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 70
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 82
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000269|PubMed:17761950"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 260
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P28700"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:16912044"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056565"
FT VARIANT 261
FT /note="P -> L (in dbSNP:rs2234960)"
FT /id="VAR_014620"
FT VARIANT 327
FT /note="A -> S (in dbSNP:rs1805345)"
FT /id="VAR_050582"
FT VARIANT 336
FT /note="S -> I (in dbSNP:rs1805345)"
FT /id="VAR_014621"
FT VARIANT 398
FT /note="A -> V (in dbSNP:rs11542209)"
FT /id="VAR_050583"
FT MUTAGEN 27
FT /note="S->A: Abolishes phosphorylation. No change in
FT increase of RARA-mediated transcriptional activity."
FT /evidence="ECO:0000269|PubMed:11162439,
FT ECO:0000269|PubMed:20215566"
FT MUTAGEN 27
FT /note="S->A: Increase in RARA-mediated transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:11162439,
FT ECO:0000269|PubMed:20215566"
FT MUTAGEN 133..156
FT /note="Missing: Abolishes acetylation by EP300."
FT /evidence="ECO:0000269|PubMed:17761950"
FT MUTAGEN 145
FT /note="K->R: Abolishes acetylation by EP300, DNA binding
FT and transcriptional activity. Impairs interaction with
FT EP300."
FT /evidence="ECO:0000269|PubMed:17761950"
FT MUTAGEN 158..159
FT /note="FF->AA: Abolishes nuclear export."
FT /evidence="ECO:0000269|PubMed:12145331"
FT MUTAGEN 160..165
FT /note="KRTVRK->QGTVGQ: Abolishes nuclear localization and
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:12145331"
FT MUTAGEN 206..216
FT /note="Missing: No impact on acetylation by EP300."
FT /evidence="ECO:0000269|PubMed:17761950"
FT MUTAGEN 352..462
FT /note="Missing: No impact on acetylation by EP300."
FT /evidence="ECO:0000269|PubMed:17761950"
FT MUTAGEN 357..360
FT /note="MRDM->ARDA: Abolishes nuclear export."
FT /evidence="ECO:0000269|PubMed:15509776"
FT MUTAGEN 418..430
FT /note="LLLRLPALRSIGL->ALARLPALRSIGA: Abolishes nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:15509776"
FT MUTAGEN 434
FT /note="E->N,Q,K,A: As a heterodimer with NR1H4, impairs
FT interaction with coactivator NCOA1. Impairs transcriptional
FT activity."
FT /evidence="ECO:0000269|PubMed:30275017"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4CN5"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6FBQ"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6FBQ"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6FBQ"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:6FBQ"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2NLL"
FT TURN 181..185
FT /evidence="ECO:0007829|PDB:6FBQ"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:6FBQ"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6FBQ"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:7A77"
FT HELIX 232..242
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:1MZN"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1FM9"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1XVP"
FT HELIX 264..284
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 294..316
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:6LB4"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6LB4"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:6LB4"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3UVV"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:6LB4"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3DZU"
FT HELIX 386..407
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 414..419
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 422..442
FT /evidence="ECO:0007829|PDB:6LB4"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:4ZO1"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:6LB4"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3NSQ"
SQ SEQUENCE 462 AA; 50811 MW; 7F952B580AD84C42 CRC64;
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING
MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP
AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID
KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL
AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL
LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM
QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL
RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT
