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Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)

 RXRA_HUMAN              Reviewed;         462 AA.
P19793; B3KY83; Q2NL52; Q2V504;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
31-JUL-2019, entry version 228.
RecName: Full=Retinoic acid receptor RXR-alpha;
AltName: Full=Nuclear receptor subfamily 2 group B member 1;
AltName: Full=Retinoid X receptor alpha;
Name=RXRA; Synonyms=NR2B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=2159111; DOI=10.1038/345224a0;
Mangelsdorf D.J., Ong E.S., Dyck J.A., Evans R.M.;
"Nuclear receptor that identifies a novel retinoic acid response
pathway.";
Nature 345:224-229(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING.
PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
"DNA-binding profiling of human hormone nuclear receptors via
fluorescence correlation spectroscopy in a cell-free system.";
FEBS Lett. 582:2737-2744(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND TISSUE
SPECIFICITY.
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-462.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND IDENTIFICATION OF LIGAND.
PubMed=1310260; DOI=10.1016/0092-8674(92)90479-V;
Heyman R.A., Mangelsdorf D.J., Dyck J.A., Stein R.B., Eichele G.,
Evans R.M., Thaller C.;
"9-cis retinoic acid is a high affinity ligand for the retinoid X
receptor.";
Cell 68:397-406(1992).
[9]
FUNCTION, AND INTERACTION WITH NCOA3.
PubMed=9267036; DOI=10.1016/S0092-8674(00)80516-4;
Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L.,
Privalsky M.L., Nakatani Y., Evans R.M.;
"Nuclear receptor coactivator ACTR is a novel histone
acetyltransferase and forms a multimeric activation complex with P/CAF
and CBP/p300.";
Cell 90:569-580(1997).
[10]
INTERACTION WITH NCOA6.
PubMed=10567404; DOI=10.1074/jbc.274.48.34283;
Lee S.-K., Anzick S.L., Choi J.-E., Bubendorf L., Guan X.-Y.,
Jung Y.-K., Kallioniemi O.-P., Kononen J., Trent J.M., Azorsa D.,
Jhun B.-H., Cheong J.H., Lee Y.C., Meltzer P.S., Lee J.W.;
"A nuclear factor ASC-2, as a cancer-amplified transcriptional
coactivator essential for ligand-dependent transactivation by nuclear
receptors in vivo.";
J. Biol. Chem. 274:34283-34293(1999).
[11]
FUNCTION, AND HETERODIMERIZATION WITH PPARA.
PubMed=10195690; DOI=10.1016/S0303-7207(98)00217-2;
Gorla-Bajszczak A., Juge-Aubry C., Pernin A., Burger A.G., Meier C.A.;
"Conserved amino acids in the ligand-binding and tau(i) domains of the
peroxisome proliferator-activated receptor alpha are necessary for
heterodimerization with RXR.";
Mol. Cell. Endocrinol. 147:37-47(1999).
[12]
FUNCTION, PHOSPHORYLATION AT SER-27, AND MUTAGENESIS OF SER-27.
PubMed=11162439; DOI=10.1006/bbrc.2000.4043;
Harish S., Ashok M.S., Khanam T., Rangarajan P.N.;
"Serine 27, a human retinoid X receptor alpha residue, phosphorylated
by protein kinase A is essential for cyclicAMP-mediated downregulation
of RXRalpha function.";
Biochem. Biophys. Res. Commun. 279:853-857(2000).
[13]
INTERACTION WITH SFPQ.
PubMed=11259580; DOI=10.1128/MCB.21.7.2298-2311.2001;
Mathur M., Tucker P.W., Samuels H.H.;
"PSF is a novel corepressor that mediates its effect through Sin3A and
the DNA binding domain of nuclear hormone receptors.";
Mol. Cell. Biol. 21:2298-2311(2001).
[14]
INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION) AND PPARA,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11915042; DOI=10.1053/jhep.2002.32470;
Tsutsumi T., Suzuki T., Shimoike T., Suzuki R., Moriya K.,
Shintani Y., Fujie H., Matsuura Y., Koike K., Miyamura T.;
"Interaction of hepatitis C virus core protein with retinoid X
receptor alpha modulates its transcriptional activity.";
Hepatology 35:937-946(2002).
[15]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[16]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 158-PHE-PHE-159 AND
160-LYS--LYS-165.
PubMed=12145331; DOI=10.1210/me.2001-0345;
Pruefer K., Barsony J.;
"Retinoid X receptor dominates the nuclear import and export of the
unliganded vitamin D receptor.";
Mol. Endocrinol. 16:1738-1751(2002).
[17]
INTERACTION WITH DNTTIP2.
PubMed=15047147; DOI=10.1016/j.bbrc.2004.02.179;
Bu H., Kashireddy P., Chang J., Zhu Y.T., Zhang Z., Zheng W.,
Rao S.M., Zhu Y.-J.;
"ERBP, a novel estrogen receptor binding protein enhancing the
activity of estrogen receptor.";
Biochem. Biophys. Res. Commun. 317:54-59(2004).
[18]
INTERACTION WITH RNF8.
PubMed=14981089; DOI=10.1074/jbc.M309148200;
Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T.,
Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L.,
Moriwaki H., Kojima S., Okano Y.;
"The RING finger protein, RNF8, interacts with retinoid X receptor
alpha and enhances its transcription-stimulating activity.";
J. Biol. Chem. 279:18926-18934(2004).
[19]
INTERACTION WITH RARA AND NR4A1, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF 357-MET--MET-360 AND 418-LEU--LEU-430.
PubMed=15509776; DOI=10.1128/MCB.24.22.9705-9725.2004;
Cao X., Liu W., Lin F., Li H., Kolluri S.K., Lin B., Han Y.H.,
Dawson M.I., Zhang X.K.;
"Retinoid X receptor regulates Nur77/TR3-dependent apoptosis
[corrected] by modulating its nuclear export and mitochondrial
targeting.";
Mol. Cell. Biol. 24:9705-9725(2004).
[20]
INTERACTION WITH PELP1.
PubMed=16574651; DOI=10.1074/jbc.M601593200;
Singh R.R., Gururaj A.E., Vadlamudi R.K., Kumar R.;
"9-cis-retinoic acid up-regulates expression of transcriptional
coregulator PELP1, a novel coactivator of the retinoid X receptor
alpha pathway.";
J. Biol. Chem. 281:15394-15404(2006).
[21]
SUMOYLATION AT LYS-108, AND INTERACTION WITH SENP6.
PubMed=16912044; DOI=10.1074/jbc.M604033200;
Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S.,
Seol J.H., Baek S.H., Bang O.S., Chung C.H.;
"Negative modulation of RXRalpha transcriptional activity by small
ubiquitin-related modifier (SUMO) modification and its reversal by
SUMO-specific protease SUSP1.";
J. Biol. Chem. 281:30669-30677(2006).
[22]
SUBUNIT, INTERACTION WITH EP300 AND NR4A1, SUBCELLULAR LOCATION,
ACETYLATION AT LYS-145 BY EP300, AND MUTAGENESIS OF 133-HIS--LYS-156;
LYS-145; 206-GLN--ASN-216 AND 352-GLU--THR-462.
PubMed=17761950; DOI=10.1210/me.2007-0107;
Zhao W.X., Tian M., Zhao B.X., Li G.D., Liu B., Zhan Y.Y., Chen H.Z.,
Wu Q.;
"Orphan receptor TR3 attenuates the p300-induced acetylation of
retinoid X receptor-alpha.";
Mol. Endocrinol. 21:2877-2889(2007).
[23]
HETERODIMERIZATION WITH RARA.
PubMed=17205979; DOI=10.1074/mcp.M600223-MCP200;
Huq M.D., Tsai N.-P., Khan S.A., Wei L.-N.;
"Lysine trimethylation of retinoic acid receptor-alpha: a novel means
to regulate receptor function.";
Mol. Cell. Proteomics 6:677-688(2007).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
INTERACTION WITH BHLHE40/DEC1; BHLHE41/DEC2; NCOA1; MED1; NCOR1 AND
NCOR2.
PubMed=19786558; DOI=10.1124/mol.109.057000;
Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K.,
Kato Y., Makishima M.;
"The basic helix-loop-helix proteins differentiated embryo chondrocyte
(DEC) 1 and DEC2 function as corepressors of retinoid X receptors.";
Mol. Pharmacol. 76:1360-1369(2009).
[26]
INTERACTION WITH TACC1.
PubMed=20078863; DOI=10.1186/1471-2199-11-3;
Guyot R., Vincent S., Bertin J., Samarut J., Ravel-Chapuis P.;
"The transforming acidic coiled coil (TACC1) protein modulates the
transcriptional activity of the nuclear receptors TR and RAR.";
BMC Mol. Biol. 11:3-3(2010).
[27]
FUNCTION, HETERODIMERIZATION WITH RARA, AND MUTAGENESIS OF SER-27.
PubMed=20215566; DOI=10.1210/en.2009-1338;
Santos N.C., Kim K.H.;
"Activity of retinoic acid receptor-alpha is directly regulated at its
protein kinase A sites in response to follicle-stimulating hormone
signaling.";
Endocrinology 151:2361-2372(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
FUNCTION.
PubMed=25417649; DOI=10.1038/ncomms6494;
Ma F., Liu S.Y., Razani B., Arora N., Li B., Kagechika H.,
Tontonoz P., Nunez V., Ricote M., Cheng G.;
"Retinoid X receptor alpha attenuates host antiviral response by
suppressing type I interferon.";
Nat. Commun. 5:5494-5494(2014).
[32]
FUNCTION, TISSUE SPECIFICITY, AND REPRESSION BY AGING.
PubMed=26463675; DOI=10.1093/brain/awv289;
Natrajan M.S., de la Fuente A.G., Crawford A.H., Linehan E., Nunez V.,
Johnson K.R., Wu T., Fitzgerald D.C., Ricote M., Bielekova B.,
Franklin R.J.;
"Retinoid X receptor activation reverses age-related deficiencies in
myelin debris phagocytosis and remyelination.";
Brain 138:3581-3597(2015).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
FUNCTION, INTERACTION WITH RARA, SUBCELLULAR LOCATION, AND INDUCTION
BY PULSATILE SHEAR STRESS.
PubMed=28167758; DOI=10.1073/pnas.1621425114;
Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L.,
Shih Y.T., Chien S., Chiu J.J.;
"MicroRNA-10a is crucial for endothelial response to different flow
patterns via interaction of retinoid acid receptors and histone
deacetylases.";
Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
[35]
INTERACTION WITH VDR.
PubMed=28698609; DOI=10.1038/s41598-017-05081-x;
Tamura M., Ishizawa M., Isojima T., Oezen S., Oka A., Makishima M.,
Kitanaka S.;
"Functional analyses of a novel missense and other mutations of the
vitamin D receptor in association with alopecia.";
Sci. Rep. 7:5102-5102(2017).
[36]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=30216632; DOI=10.1111/acel.12831;
Ma X., Warnier M., Raynard C., Ferrand M., Kirsh O., Defossez P.A.,
Martin N., Bernard D.;
"The nuclear receptor RXRA controls cellular senescence by regulating
calcium signaling.";
Aging Cell 17:E12831-E12831(2018).
[37]
STRUCTURE BY NMR OF 130-223.
PubMed=7925381; DOI=10.1111/j.1432-1033.1994.00639.x;
Lee M.S., Sem D.S., Kliewer S.A., Provencal J., Evans R.M.,
Wright P.E.;
"NMR assignments and secondary structure of the retinoid X receptor
alpha DNA-binding domain. Evidence for the novel C-terminal helix.";
Eur. J. Biochem. 224:639-650(1994).
[38]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 130-209.
PubMed=7746322; DOI=10.1038/375203a0;
Rastinejad F., Perlmann T., Evans R.M., Sigler P.B.;
"Structural determinants of nuclear receptor assembly on DNA direct
repeats.";
Nature 375:203-211(1995).
[39]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 225-462.
PubMed=7760929; DOI=10.1038/375377a0;
Bourguet W., Ruff M., Chambon P., Gronemeyer H., Moras D.;
"Crystal structure of the ligand-binding domain of the human nuclear
receptor RXR-alpha.";
Nature 375:377-382(1995).
[40]
STRUCTURE BY NMR OF 130-212.
PubMed=9698548; DOI=10.1006/jmbi.1998.1908;
Holmbeck S.M., Foster M.P., Casimiro D.R., Sem D.S., Dyson H.J.,
Wright P.E.;
"High-resolution solution structure of the retinoid X receptor DNA-
binding domain.";
J. Mol. Biol. 281:271-284(1998).
[41]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 129-209 IN COMPLEX WITH RARA
AND DNA.
PubMed=10698945; DOI=10.1093/emboj/19.5.1045;
Rastinejad F., Wagner T., Zhao Q., Khorasanizadeh S.;
"Structure of the RXR-RAR DNA-binding complex on the retinoic acid
response element DR1.";
EMBO J. 19:1045-1054(2000).
[42]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 224-462 OF APO AND HOLO
FORMS.
PubMed=10835357; DOI=10.1093/emboj/19.11.2592;
Egea P.F., Mitschler A., Rochel N., Ruff M., Chambon P., Moras D.;
"Crystal structure of the human RXRalpha ligand-binding domain bound
to its natural ligand: 9-cis retinoic acid.";
EMBO J. 19:2592-2601(2000).
[43]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 225-462 OF APO AND HOLO
FORMS.
PubMed=10970886; DOI=10.1101/gad.802300;
Gampe R.T. Jr., Montana V.G., Lambert M.H., Wisely G.B., Milburn M.V.,
Xu H.E.;
"Structural basis for autorepression of retinoid X receptor by
tetramer formation and the AF-2 helix.";
Genes Dev. 14:2229-2241(2000).
[44] {ECO:0000244|PDB:1BY4}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-209 IN COMPLEX WITH ZINC
AND DNA, AND SUBUNIT.
PubMed=10669605; DOI=10.1006/jmbi.1999.3457;
Zhao Q., Chasse S.A., Devarakonda S., Sierk M.L., Ahvazi B.,
Rastinejad F.;
"Structural basis of RXR-DNA interactions.";
J. Mol. Biol. 296:509-520(2000).
[45]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-462 IN COMPLEX WITH
PPARG; COACTIVATOR NCOA1; RETINOIC ACID AND SYNTHETIC ANTIDIABETIC
AGONISTS ROSIGLITAZONE AND GI262570.
PubMed=10882139; DOI=10.1016/S1097-2765(00)80448-7;
Gampe R.T. Jr., Montana V.G., Lambert M.H., Miller A.B., Bledsoe R.K.,
Milburn M.V., Kliewer S.A., Willson T.M., Xu H.E.;
"Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the
molecular basis of heterodimerization among nuclear receptors.";
Mol. Cell 5:545-555(2000).
[46]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 225-462 IN COMPLEX WITH PPARA
OR PPARG; 9-CIS RETINOIC ACID; COACTIVATOR NCOA1 AND PPAR SYNTHETIC
AGONIST GW409544.
PubMed=11698662; DOI=10.1073/pnas.241410198;
Xu H.E., Lambert M.H., Montana V.G., Plunket K.D., Moore L.B.,
Collins J.L., Oplinger J.A., Kliewer S.A., Gampe R.T. Jr., McKee D.D.,
Moore J.T., Willson T.M.;
"Structural determinants of ligand binding selectivity between the
peroxisome proliferator-activated receptors.";
Proc. Natl. Acad. Sci. U.S.A. 98:13919-13924(2001).
[47]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 227-458 IN COMPLEX WITH
M.MUSCULUS NR1I13; R.NORVEGICUS NCOA2 AND AGONIST INSECTICIDE
CONTAMINANT TCPOBOP.
PubMed=15610733; DOI=10.1016/S1097-2765(04)00727-0;
Suino K., Peng L., Reynolds R., Li Y., Cha J.Y., Repa J.J.,
Kliewer S.A., Xu H.E.;
"The nuclear xenobiotic receptor CAR: structural determinants of
constitutive activation and heterodimerization.";
Mol. Cell 16:893-905(2004).
[48] {ECO:0000244|PDB:2ACL}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 225-462 IN COMPLEX WITH
9-CIS RETINOIC ACID, AND FUNCTION.
PubMed=16107141; DOI=10.1021/jm050532w;
Jaye M.C., Krawiec J.A., Campobasso N., Smallwood A., Qiu C., Lu Q.,
Kerrigan J.J., De Los Frailes Alvaro M., Laffitte B., Liu W.S.,
Marino J.P. Jr., Meyer C.R., Nichols J.A., Parks D.J., Perez P.,
Sarov-Blat L., Seepersaud S.D., Steplewski K.M., Thompson S.K.,
Wang P., Watson M.A., Webb C.L., Haigh D., Caravella J.A.,
Macphee C.H., Willson T.M., Collins J.L.;
"Discovery of substituted maleimides as liver X receptor agonists and
determination of a ligand-bound crystal structure.";
J. Med. Chem. 48:5419-5422(2005).
[49] {ECO:0000244|PDB:3FAL}
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 225-462 IN COMPLEX WITH
9-CIS RETINOIC ACID, AND FUNCTION.
PubMed=18800767; DOI=10.1021/jm800612u;
Chao E.Y., Caravella J.A., Watson M.A., Campobasso N., Ghisletti S.,
Billin A.N., Galardi C., Wang P., Laffitte B.A., Iannone M.A.,
Goodwin B.J., Nichols J.A., Parks D.J., Stewart E., Wiethe R.W.,
Williams S.P., Smallwood A., Pearce K.H., Glass C.K., Willson T.M.,
Zuercher W.J., Collins J.L.;
"Structure-guided design of N-phenyl tertiary amines as
transrepression-selective liver X receptor modulators with anti-
inflammatory activity.";
J. Med. Chem. 51:5758-5765(2008).
[50] {ECO:0000244|PDB:3FC6}
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 225-462 IN COMPLEX WITH
9-CIS RETINOIC ACID, AND FUNCTION.
PubMed=19167885; DOI=10.1016/j.bmcl.2009.01.004;
Washburn D.G., Hoang T.H., Campobasso N., Smallwood A., Parks D.J.,
Webb C.L., Frank K.A., Nord M., Duraiswami C., Evans C., Jaye M.,
Thompson S.K.;
"Synthesis and SAR of potent LXR agonists containing an indole
pharmacophore.";
Bioorg. Med. Chem. Lett. 19:1097-1100(2009).
[51] {ECO:0000244|PDB:5UAN}
X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) OF 98-462 IN COMPLEX WITH RARB
AND DNA, AND FUNCTION.
PubMed=29021580; DOI=10.1038/s41467-017-00981-y;
Chandra V., Wu D., Li S., Potluri N., Kim Y., Rastinejad F.;
"The quaternary architecture of RARbeta-RXRalpha heterodimer
facilitates domain-domain signal transmission.";
Nat. Commun. 8:868-868(2017).
[52] {ECO:0000244|PDB:6A5Y}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 225-462 IN COMPLEX WITH
NR1H4; NCOA1 PEPTIDE AND 9-CIS-RETINOIC ACID, AND MUTAGENESIS OF
GLU-434.
PubMed=30275017; DOI=10.1074/jbc.RA118.004652;
Wang N., Zou Q., Xu J., Zhang J., Liu J.;
"Ligand binding and heterodimerization with retinoid X receptor alpha
(RXRalpha) induce farnesoid X receptor (FXR) conformational changes
affecting coactivator binding.";
J. Biol. Chem. 293:18180-18191(2018).
-!- FUNCTION: Receptor for retinoic acid that acts as a transcription
factor (PubMed:11162439, PubMed:11915042). Forms homo- or
heterodimers with retinoic acid receptors (RARs) and binds to
target response elements in response to their ligands, all-trans
or 9-cis retinoic acid, to regulate gene expression in various
biological processes (PubMed:10195690, PubMed:11162439,
PubMed:11915042, PubMed:28167758, PubMed:17761950,
PubMed:16107141, PubMed:18800767, PubMed:19167885). The RAR/RXR
heterodimers bind to the retinoic acid response elements (RARE)
composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate
transcription (PubMed:10195690, PubMed:11162439, PubMed:11915042,
PubMed:17761950, PubMed:28167758). The high affinity ligand for
retinoid X receptors (RXRs) is 9-cis retinoic acid
(PubMed:1310260). In the absence of ligand, the RXR-RAR
heterodimers associate with a multiprotein complex containing
transcription corepressors that induce histone deacetylation,
chromatin condensation and transcriptional suppression
(PubMed:20215566). On ligand binding, the corepressors dissociate
from the receptors and coactivators are recruited leading to
transcriptional activation (PubMed:20215566, PubMed:9267036).
Serves as a common heterodimeric partner for a number of nuclear
receptors, such as RARA, RARB and PPARA (PubMed:10195690,
PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB
heterodimer can act as a transcriptional repressor or
transcriptional activator, depending on the RARE DNA element
context (PubMed:29021580). The RXRA/PPARA heterodimer is required
for PPARA transcriptional activity on fatty acid oxidation genes
such as ACOX1 and the P450 system genes (PubMed:10195690).
Together with RARA, positively regulates microRNA-10a expression,
thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile
shear stress in vascular endothelial cells (PubMed:28167758). Acts
as an enhancer of RARA binding to RARE DNA element
(PubMed:28167758). May facilitate the nuclear import of
heterodimerization partners such as VDR and NR4A1
(PubMed:12145331, PubMed:15509776). Promotes myelin debris
phagocytosis and remyelination by macrophages (PubMed:26463675).
Plays a role in the attenuation of the innate immune system in
response to viral infections, possibly by negatively regulating
the transcription of antiviral genes such as type I IFN genes
(PubMed:25417649). Involved in the regulation of calcium signaling
by repressing ITPR2 gene expression, thereby controlling cellular
senescence (PubMed:30216632). {ECO:0000269|PubMed:10195690,
ECO:0000269|PubMed:11162439, ECO:0000269|PubMed:11915042,
ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:1310260,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18800767,
ECO:0000269|PubMed:19167885, ECO:0000269|PubMed:20215566,
ECO:0000269|PubMed:25417649, ECO:0000269|PubMed:26463675,
ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:29021580,
ECO:0000269|PubMed:30216632, ECO:0000269|PubMed:9267036}.
-!- SUBUNIT: Homodimer (PubMed:10669605, PubMed:17761950). Heterodimer
(via C-terminus) with RARA; required for ligand-dependent retinoic
acid receptor transcriptional activity; association with RARA is
enhanced by pulsatile shear stress (PubMed:28167758,
PubMed:10698945, PubMed:15509776). Heterodimer with PPARA (via the
leucine-like zipper in the LBD); the interaction is required for
PPARA transcriptional activity (PubMed:10195690, PubMed:11915042,
PubMed:11698662). Heterodimerizes with PPARG (PubMed:10882139,
PubMed:11698662). Heterodimerizes (via NR LBD) with RARB
(PubMed:29021580). Heterodimerizes with NR1H4; the
heterodimerization enhances the binding affinity for LXXLL motifs
from coactivators (PubMed:30275017). Interacts with NCOA3 and
NCOA6 coactivators (PubMed:9267036, PubMed:10567404). Interacts
with coactivator FAM120B (By similarity). Interacts with
coactivator PELP1, SENP6, SFPQ, DNTTIP2 and RNF8 (PubMed:16574651,
PubMed:16912044, PubMed:11259580, PubMed:15047147,
PubMed:14981089). Interacts with PRMT2 (PubMed:12039952).
Interacts with ASXL1 (By similarity). Interacts with BHLHE40/DEC1,
BHLHE41/DEC2, NCOR1 and NCOR2 (PubMed:19786558). Interacts in a
ligand-dependent fashion with MED1 and NCOA1 (PubMed:19786558,
PubMed:10882139, PubMed:11698662). Interacts with VDR
(PubMed:28698609). Interacts with EP300; the interaction is
decreased by 9-cis retinoic acid (PubMed:17761950). Heterodimer
(via C-terminus) with NR4A1 (via DNA-binding domain); DNA-binding
of the heterodimer is enhanced by 9-cis retinoic acid
(PubMed:17761950, PubMed:15509776). NR4A1 competes with EP300 for
interaction with RXRA and thereby attenuates EP300 mediated
acetylation of RXRA (PubMed:17761950). In the absence of hormonal
ligand, interacts with TACC1 (PubMed:20078863).
{ECO:0000250|UniProtKB:P28700, ECO:0000269|PubMed:10195690,
ECO:0000269|PubMed:10567404, ECO:0000269|PubMed:10669605,
ECO:0000269|PubMed:10698945, ECO:0000269|PubMed:10882139,
ECO:0000269|PubMed:11259580, ECO:0000269|PubMed:11698662,
ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:12039952,
ECO:0000269|PubMed:14981089, ECO:0000269|PubMed:15047147,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:16574651,
ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17761950,
ECO:0000269|PubMed:19786558, ECO:0000269|PubMed:20078863,
ECO:0000269|PubMed:28167758, ECO:0000269|PubMed:28698609,
ECO:0000269|PubMed:29021580, ECO:0000269|PubMed:30275017,
ECO:0000269|PubMed:9267036}.
-!- SUBUNIT: (Microbial infection) Interacts (via the DNA binding
domain) with HCV core protein; the interaction enhances the
transcriptional activities of the RXRA/RARA and the RXRA/PPARA
heterodimers. {ECO:0000269|PubMed:11915042}.
-!- INTERACTION:
Q03463:- (xeno); NbExp=3; IntAct=EBI-78598, EBI-9159704;
O14503:BHLHE40; NbExp=4; IntAct=EBI-78598, EBI-711810;
P97792-1:Cxadr (xeno); NbExp=2; IntAct=EBI-78598, EBI-15903843;
Q15648:MED1; NbExp=6; IntAct=EBI-78598, EBI-394459;
Q71SY5:MED25; NbExp=4; IntAct=EBI-78598, EBI-394558;
Q15788:NCOA1; NbExp=14; IntAct=EBI-78598, EBI-455189;
Q15596:NCOA2; NbExp=5; IntAct=EBI-78598, EBI-81236;
Q9JLI4:Ncoa6 (xeno); NbExp=2; IntAct=EBI-78598, EBI-286271;
P27986:PIK3R1; NbExp=8; IntAct=EBI-78598, EBI-79464;
P37231-1:PPARG; NbExp=6; IntAct=EBI-78598, EBI-15664691;
P10276:RARA; NbExp=14; IntAct=EBI-78598, EBI-413374;
P42224:STAT1; NbExp=2; IntAct=EBI-78598, EBI-1057697;
P04625:THRA (xeno); NbExp=4; IntAct=EBI-78598, EBI-286261;
P11473:VDR; NbExp=6; IntAct=EBI-78598, EBI-286357;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:11915042,
ECO:0000269|PubMed:12145331, ECO:0000269|PubMed:15509776,
ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:28167758}.
Cytoplasm {ECO:0000269|PubMed:12145331,
ECO:0000269|PubMed:15509776}. Mitochondrion
{ECO:0000269|PubMed:17761950}. Note=Localization to the nucleus is
enhanced by vitamin D3 (PubMed:15509776). Nuclear localization may
be enhanced by the interaction with heterodimerization partner VDR
(PubMed:12145331). Translocation to the mitochondrion upon
interaction with NR4A1 (PubMed:17761950, PubMed:15509776).
Increased nuclear localization upon pulsatile shear stress
(PubMed:28167758). {ECO:0000269|PubMed:12145331,
ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950,
ECO:0000269|PubMed:28167758}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19793-1; Sequence=Displayed;
Name=2;
IsoId=P19793-2; Sequence=VSP_056565;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lung fibroblasts (at protein
level) (PubMed:30216632). Expressed in monocytes
(PubMed:26463675). Highly expressed in liver, also found in kidney
and brain (PubMed:24275569, PubMed:2159111, PubMed:14702039).
{ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:2159111,
ECO:0000269|PubMed:24275569, ECO:0000269|PubMed:26463675,
ECO:0000269|PubMed:30216632}.
-!- INDUCTION: Down-regulated by aging (PubMed:26463675). Induced by
pulsatile shear stress (PubMed:28167758).
{ECO:0000269|PubMed:26463675, ECO:0000269|PubMed:28167758}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain
(AF1 domain), a DNA-binding domain and a C-terminal ligand-binding
domain (AF2 domain).
-!- PTM: Acetylated by EP300; acetylation enhances DNA binding and
transcriptional activity. {ECO:0000269|PubMed:17761950}.
-!- PTM: Phosphorylated on serine and threonine residues mainly in the
N-terminal modulating domain (By similarity). Constitutively
phosphorylated on Ser-21 in the presence or absence of ligand (By
similarity). Under stress conditions, hyperphosphorylated by
activated JNK on Ser-56, Ser-70, Thr-82 and Ser-260 (By
similarity). Phosphorylated on Ser-27, in vitro, by PKA
(PubMed:11162439). This phosphorylation is required for repression
of cAMP-mediated transcriptional activity of RARA
(PubMed:11162439). {ECO:0000250|UniProtKB:P28700,
ECO:0000269|PubMed:11162439}.
-!- PTM: Sumoylation negatively regulates transcriptional activity.
Desumoylated specifically by SENP6. {ECO:0000269|PubMed:16912044}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/rxra/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Retinoid X receptor entry;
URL="https://en.wikipedia.org/wiki/Retinoid_X_receptor";
-----------------------------------------------------------------------
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EMBL; X52773; CAA36982.1; -; mRNA.
EMBL; AB307705; BAH02296.1; -; mRNA.
EMBL; AK131192; BAG54745.1; -; mRNA.
EMBL; AC156789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL354796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL669970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL683798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW88123.1; -; Genomic_DNA.
EMBL; BC110998; AAI10999.1; -; mRNA.
EMBL; DQ303444; ABB96254.1; -; Genomic_DNA.
CCDS; CCDS35172.1; -. [P19793-1]
PIR; S09592; S09592.
RefSeq; NP_001278850.1; NM_001291921.1. [P19793-2]
RefSeq; NP_002948.1; NM_002957.5. [P19793-1]
PDB; 1BY4; X-ray; 2.10 A; A/B/C/D=129-209.
PDB; 1DSZ; X-ray; 1.70 A; B=129-212.
PDB; 1FBY; X-ray; 2.25 A; A/B=224-462.
PDB; 1FM6; X-ray; 2.10 A; A/U=225-462.
PDB; 1FM9; X-ray; 2.10 A; A=225-462.
PDB; 1G1U; X-ray; 2.50 A; A/B/C/D=225-462.
PDB; 1G5Y; X-ray; 2.00 A; A/B/C/D=225-462.
PDB; 1K74; X-ray; 2.30 A; A=225-462.
PDB; 1MV9; X-ray; 1.90 A; A=223-462.
PDB; 1MVC; X-ray; 1.90 A; A=223-462.
PDB; 1MZN; X-ray; 1.90 A; A/C/E/G=223-462.
PDB; 1R0N; X-ray; 2.60 A; A=130-206.
PDB; 1RDT; X-ray; 2.40 A; A=225-462.
PDB; 1RXR; NMR; -; A=130-212.
PDB; 1XLS; X-ray; 2.96 A; A/B/C/D=227-458.
PDB; 1XV9; X-ray; 2.70 A; A/C=227-462.
PDB; 1XVP; X-ray; 2.60 A; A/C=227-462.
PDB; 1YNW; X-ray; 3.00 A; B=130-228.
PDB; 2ACL; X-ray; 2.80 A; A/C/E/G=225-462.
PDB; 2NLL; X-ray; 1.90 A; A=135-200.
PDB; 2P1T; X-ray; 1.80 A; A=223-462.
PDB; 2P1U; X-ray; 2.20 A; A=223-462.
PDB; 2P1V; X-ray; 2.20 A; A=223-462.
PDB; 2ZXZ; X-ray; 3.00 A; A=223-462.
PDB; 2ZY0; X-ray; 2.90 A; A/C=223-462.
PDB; 3DZU; X-ray; 3.20 A; A=11-462.
PDB; 3DZY; X-ray; 3.10 A; A=11-462.
PDB; 3E00; X-ray; 3.10 A; A=11-462.
PDB; 3E94; X-ray; 1.90 A; A=223-462.
PDB; 3FAL; X-ray; 2.36 A; A/C=225-462.
PDB; 3FC6; X-ray; 2.06 A; A/C=225-462.
PDB; 3FUG; X-ray; 2.00 A; A=223-462.
PDB; 3H0A; X-ray; 2.10 A; A=228-455.
PDB; 3KWY; X-ray; 2.30 A; A=223-462.
PDB; 3NSP; X-ray; 2.90 A; A/B=223-462.
PDB; 3NSQ; X-ray; 2.60 A; A/B=223-462.
PDB; 3OAP; X-ray; 2.05 A; A=228-458.
PDB; 3OZJ; X-ray; 2.10 A; A/C=225-462.
PDB; 3PCU; X-ray; 2.00 A; A=229-458.
PDB; 3R29; X-ray; 2.90 A; A/B=223-462.
PDB; 3R2A; X-ray; 3.00 A; A/B/C/D=223-462.
PDB; 3R5M; X-ray; 2.80 A; A/C=223-462.
PDB; 3UVV; X-ray; 2.95 A; B=225-462.
PDB; 4CN2; X-ray; 2.07 A; C/D=130-212.
PDB; 4CN3; X-ray; 2.35 A; A/B/C=130-212, D=130-173, D=175-212.
PDB; 4CN5; X-ray; 2.00 A; A/B=130-212.
PDB; 4CN7; X-ray; 2.34 A; A/B/E/F=130-212.
PDB; 4J5W; X-ray; 2.80 A; C/D=227-462.
PDB; 4J5X; X-ray; 2.80 A; C/D=227-462.
PDB; 4K4J; X-ray; 2.00 A; A=228-458.
PDB; 4K6I; X-ray; 2.10 A; A=228-458.
PDB; 4M8E; X-ray; 2.40 A; A=228-458.
PDB; 4M8H; X-ray; 2.20 A; A=228-458.
PDB; 4N5G; X-ray; 2.11 A; A/B/C/D=223-462.
PDB; 4N8R; X-ray; 2.03 A; A/B/C/D=223-462.
PDB; 4NQA; X-ray; 3.10 A; A/H=98-462.
PDB; 4OC7; X-ray; 2.50 A; A=223-462.
PDB; 4POH; X-ray; 2.30 A; A=228-458.
PDB; 4POJ; X-ray; 2.00 A; A=228-458.
PDB; 4PP3; X-ray; 2.00 A; A=228-458.
PDB; 4PP5; X-ray; 2.00 A; A=228-458.
PDB; 4RFW; X-ray; 2.40 A; A=228-458.
PDB; 4RMC; X-ray; 2.70 A; A=228-458.
PDB; 4RMD; X-ray; 1.90 A; A=228-462.
PDB; 4RME; X-ray; 2.30 A; A=228-462.
PDB; 4ZO1; X-ray; 3.22 A; B=231-455.
PDB; 4ZSH; X-ray; 1.80 A; A=223-462.
PDB; 5EC9; X-ray; 2.30 A; A=229-456.
PDB; 5GYM; X-ray; 2.60 A; A/B/C/D/E/F/G/H=227-462.
PDB; 5JI0; X-ray; 1.98 A; A=223-462.
PDB; 5LYQ; X-ray; 2.17 A; A=223-462.
PDB; 5MJ5; X-ray; 1.90 A; A=229-457.
PDB; 5MK4; X-ray; 2.00 A; A/C=229-457.
PDB; 5MKJ; X-ray; 2.50 A; A=229-458.
PDB; 5MKU; X-ray; 1.78 A; A=229-456.
PDB; 5MMW; X-ray; 2.70 A; A=229-457.
PDB; 5TBP; X-ray; 2.60 A; A/B/C/D=223-462.
PDB; 5UAN; X-ray; 3.51 A; A=98-462.
PDB; 5Z12; X-ray; 2.75 A; B/C=228-458.
PDB; 5ZQU; X-ray; 2.60 A; A/B/C/D=224-462.
PDB; 6A5Y; X-ray; 2.10 A; D=225-462.
PDB; 6A5Z; X-ray; 2.95 A; D/L=225-462.
PDB; 6A60; X-ray; 3.05 A; D=225-462.
PDB; 6FBQ; X-ray; 1.60 A; A/B=130-212.
PDB; 6FBR; X-ray; 2.10 A; A/B=130-212.
PDB; 6HN6; X-ray; 2.71 A; A=201-462.
PDBsum; 1BY4; -.
PDBsum; 1DSZ; -.
PDBsum; 1FBY; -.
PDBsum; 1FM6; -.
PDBsum; 1FM9; -.
PDBsum; 1G1U; -.
PDBsum; 1G5Y; -.
PDBsum; 1K74; -.
PDBsum; 1MV9; -.
PDBsum; 1MVC; -.
PDBsum; 1MZN; -.
PDBsum; 1R0N; -.
PDBsum; 1RDT; -.
PDBsum; 1RXR; -.
PDBsum; 1XLS; -.
PDBsum; 1XV9; -.
PDBsum; 1XVP; -.
PDBsum; 1YNW; -.
PDBsum; 2ACL; -.
PDBsum; 2NLL; -.
PDBsum; 2P1T; -.
PDBsum; 2P1U; -.
PDBsum; 2P1V; -.
PDBsum; 2ZXZ; -.
PDBsum; 2ZY0; -.
PDBsum; 3DZU; -.
PDBsum; 3DZY; -.
PDBsum; 3E00; -.
PDBsum; 3E94; -.
PDBsum; 3FAL; -.
PDBsum; 3FC6; -.
PDBsum; 3FUG; -.
PDBsum; 3H0A; -.
PDBsum; 3KWY; -.
PDBsum; 3NSP; -.
PDBsum; 3NSQ; -.
PDBsum; 3OAP; -.
PDBsum; 3OZJ; -.
PDBsum; 3PCU; -.
PDBsum; 3R29; -.
PDBsum; 3R2A; -.
PDBsum; 3R5M; -.
PDBsum; 3UVV; -.
PDBsum; 4CN2; -.
PDBsum; 4CN3; -.
PDBsum; 4CN5; -.
PDBsum; 4CN7; -.
PDBsum; 4J5W; -.
PDBsum; 4J5X; -.
PDBsum; 4K4J; -.
PDBsum; 4K6I; -.
PDBsum; 4M8E; -.
PDBsum; 4M8H; -.
PDBsum; 4N5G; -.
PDBsum; 4N8R; -.
PDBsum; 4NQA; -.
PDBsum; 4OC7; -.
PDBsum; 4POH; -.
PDBsum; 4POJ; -.
PDBsum; 4PP3; -.
PDBsum; 4PP5; -.
PDBsum; 4RFW; -.
PDBsum; 4RMC; -.
PDBsum; 4RMD; -.
PDBsum; 4RME; -.
PDBsum; 4ZO1; -.
PDBsum; 4ZSH; -.
PDBsum; 5EC9; -.
PDBsum; 5GYM; -.
PDBsum; 5JI0; -.
PDBsum; 5LYQ; -.
PDBsum; 5MJ5; -.
PDBsum; 5MK4; -.
PDBsum; 5MKJ; -.
PDBsum; 5MKU; -.
PDBsum; 5MMW; -.
PDBsum; 5TBP; -.
PDBsum; 5UAN; -.
PDBsum; 5Z12; -.
PDBsum; 5ZQU; -.
PDBsum; 6A5Y; -.
PDBsum; 6A5Z; -.
PDBsum; 6A60; -.
PDBsum; 6FBQ; -.
PDBsum; 6FBR; -.
PDBsum; 6HN6; -.
SMR; P19793; -.
BioGrid; 112168; 132.
ComplexPortal; CPX-496; RXRalpha-PXR retinoic acid receptor complex.
ComplexPortal; CPX-508; RXRalpha-RARalpha retinoic acid receptor complex.
ComplexPortal; CPX-631; RXRalpha-VDR nuclear hormone receptor complex.
ComplexPortal; CPX-632; RXRalpha-LXRalpha nuclear hormone receptor complex.
ComplexPortal; CPX-654; RXRalpha-TRbeta nuclear hormone receptor complex.
ComplexPortal; CPX-662; RXRalpha-TRalpha nuclear hormone receptor complex.
ComplexPortal; CPX-664; RXRalpha-RXRalpha retinoic acid receptor complex.
ComplexPortal; CPX-678; RXRalpha-LXRbeta nuclear hormone receptor complex.
ComplexPortal; CPX-816; RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex.
CORUM; P19793; -.
DIP; DIP-641N; -.
ELM; P19793; -.
IntAct; P19793; 50.
MINT; P19793; -.
STRING; 9606.ENSP00000419692; -.
BindingDB; P19793; -.
ChEMBL; CHEMBL2061; -.
DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DrugBank; DB00459; Acitretin.
DrugBank; DB00210; Adapalene.
DrugBank; DB00523; Alitretinoin.
DrugBank; DB00307; Bexarotene.
DrugBank; DB00749; Etodolac.
DrugBank; DB00926; Etretinate.
DrugBank; DB08601; tributylstannanyl.
GuidetoPHARMACOLOGY; 610; -.
SwissLipids; SLP:000001552; -.
MoonDB; P19793; Predicted.
iPTMnet; P19793; -.
PhosphoSitePlus; P19793; -.
BioMuta; RXRA; -.
DMDM; 133701; -.
EPD; P19793; -.
jPOST; P19793; -.
MaxQB; P19793; -.
PaxDb; P19793; -.
PeptideAtlas; P19793; -.
PRIDE; P19793; -.
ProteomicsDB; 3832; -.
ProteomicsDB; 53687; -. [P19793-1]
DNASU; 6256; -.
Ensembl; ENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneID; 6256; -.
KEGG; hsa:6256; -.
UCSC; uc004cfb.3; human. [P19793-1]
CTD; 6256; -.
DisGeNET; 6256; -.
GeneCards; RXRA; -.
HGNC; HGNC:10477; RXRA.
HPA; CAB004565; -.
HPA; CAB005352; -.
MIM; 180245; gene.
neXtProt; NX_P19793; -.
OpenTargets; ENSG00000186350; -.
PharmGKB; PA34890; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000159789; -.
InParanoid; P19793; -.
KO; K08524; -.
OMA; LTCGMKR; -.
OrthoDB; 912470at2759; -.
PhylomeDB; P19793; -.
TreeFam; TF352097; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLink; P19793; -.
SIGNOR; P19793; -.
ChiTaRS; RXRA; human.
EvolutionaryTrace; P19793; -.
GeneWiki; Retinoid_X_receptor_alpha; -.
GenomeRNAi; 6256; -.
PMAP-CutDB; P19793; -.
PRO; PR:P19793; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000186350; Expressed in 231 organ(s), highest expression level in liver.
ExpressionAtlas; P19793; baseline and differential.
Genevisible; P19793; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0031490; F:chromatin DNA binding; IEA:Ensembl.
GO; GO:0050692; F:DBD domain binding; IDA:CAFA.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0050693; F:LBD domain binding; IDA:CAFA.
GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL.
GO; GO:0016922; F:nuclear receptor binding; IPI:CAFA.
GO; GO:0042277; F:peptide binding; IDA:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:CAFA.
GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
GO; GO:0038023; F:signaling receptor activity; TAS:BHF-UCL.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0042809; F:vitamin D receptor binding; IPI:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0008203; P:cholesterol metabolic process; TAS:BHF-UCL.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001893; P:maternal placenta development; IEA:Ensembl.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045994; P:positive regulation of translational initiation by iron; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IDA:MGI.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0032526; P:response to retinoic acid; IMP:BHF-UCL.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0055012; P:ventricular cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
GO; GO:0006766; P:vitamin metabolic process; TAS:ProtInc.
DisProt; DP00062; -.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR021780; Nuc_recep-AF1.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000003; Retinoid-X_rcpt/HNF4.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF11825; Nuc_recep-AF1; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00545; RETINOIDXR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; Host-virus interaction; Isopeptide bond;
Metal-binding; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 462 Retinoic acid receptor RXR-alpha.
/FTId=PRO_0000053566.
DOMAIN 227 458 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 135 200 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 135 155 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 171 195 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 134 Modulating. {ECO:0000250}.
REGION 160 165 Nuclear localization signal.
{ECO:0000269|PubMed:12145331}.
REGION 201 224 Hinge.
REGION 348 368 Required for nuclear export.
{ECO:0000269|PubMed:15509776}.
METAL 135 135 Zinc 1. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 138 138 Zinc 1. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 152 152 Zinc 1. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 155 155 Zinc 1. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 171 171 Zinc 2. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 177 177 Zinc 2. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 187 187 Zinc 2. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
METAL 190 190 Zinc 2. {ECO:0000244|PDB:1BY4,
ECO:0000269|PubMed:10669605}.
BINDING 316 316 9-cis retinoic acid.
{ECO:0000244|PDB:2ACL,
ECO:0000244|PDB:3FAL,
ECO:0000244|PDB:3FC6,
ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:18800767,
ECO:0000269|PubMed:19167885}.
BINDING 327 327 9-cis retinoic acid; via amide nitrogen.
{ECO:0000244|PDB:2ACL,
ECO:0000244|PDB:3FAL,
ECO:0000244|PDB:3FC6,
ECO:0000269|PubMed:16107141,
ECO:0000269|PubMed:18800767,
ECO:0000269|PubMed:19167885}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:P28700}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000269|PubMed:11162439}.
MOD_RES 56 56 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000250|UniProtKB:P28700}.
MOD_RES 70 70 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000250|UniProtKB:P28700}.
MOD_RES 82 82 Phosphothreonine; by MAPK8 and MAPK9.
{ECO:0000250|UniProtKB:P28700}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 145 145 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:17761950}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 260 260 Phosphoserine; by MAPK8 and MAPK9.
{ECO:0000250|UniProtKB:P28700}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 108 108 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:16912044}.
VAR_SEQ 1 97 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056565.
VARIANT 261 261 P -> L (in dbSNP:rs2234960).
/FTId=VAR_014620.
VARIANT 327 327 A -> S (in dbSNP:rs1805345).
/FTId=VAR_050582.
VARIANT 336 336 S -> I (in dbSNP:rs1805345).
/FTId=VAR_014621.
VARIANT 398 398 A -> V (in dbSNP:rs11542209).
/FTId=VAR_050583.
MUTAGEN 27 27 S->A: Abolishes phosphorylation. No
change in increase of RARA-mediated
transcriptional activity.
{ECO:0000269|PubMed:11162439,
ECO:0000269|PubMed:20215566}.
MUTAGEN 27 27 S->A: Increase in RARA-mediated
transcriptional activity.
{ECO:0000269|PubMed:11162439,
ECO:0000269|PubMed:20215566}.
MUTAGEN 133 156 Missing: Abolishes acetylation by EP300.
{ECO:0000269|PubMed:17761950}.
MUTAGEN 145 145 K->R: Abolishes acetylation by EP300, DNA
binding and transcriptional activity.
Impairs interaction with EP300.
{ECO:0000269|PubMed:17761950}.
MUTAGEN 158 159 FF->AA: Abolishes nuclear export.
{ECO:0000269|PubMed:12145331}.
MUTAGEN 160 165 KRTVRK->QGTVGQ: Abolishes nuclear
localization and transcriptional
activity. {ECO:0000269|PubMed:12145331}.
MUTAGEN 206 216 Missing: No impact on acetylation by
EP300. {ECO:0000269|PubMed:17761950}.
MUTAGEN 352 462 Missing: No impact on acetylation by
EP300. {ECO:0000269|PubMed:17761950}.
MUTAGEN 357 360 MRDM->ARDA: Abolishes nuclear export.
{ECO:0000269|PubMed:15509776}.
MUTAGEN 418 430 LLLRLPALRSIGL->ALARLPALRSIGA: Abolishes
nuclear localization.
{ECO:0000269|PubMed:15509776}.
MUTAGEN 434 434 E->N,Q,K,A: As a heterodimer with NR1H4,
impairs interaction with coactivator
NCOA1. Impairs transcriptional activity.
{ECO:0000269|PubMed:30275017}.
STRAND 131 134 {ECO:0000244|PDB:4CN5}.
TURN 136 138 {ECO:0000244|PDB:6FBQ}.
STRAND 141 146 {ECO:0000244|PDB:6FBQ}.
STRAND 149 151 {ECO:0000244|PDB:6FBQ}.
HELIX 153 164 {ECO:0000244|PDB:6FBQ}.
STRAND 172 175 {ECO:0000244|PDB:2NLL}.
TURN 181 185 {ECO:0000244|PDB:6FBQ}.
HELIX 188 198 {ECO:0000244|PDB:6FBQ}.
HELIX 202 204 {ECO:0000244|PDB:6FBQ}.
HELIX 226 229 {ECO:0000244|PDB:3FC6}.
HELIX 232 241 {ECO:0000244|PDB:5MKU}.
HELIX 246 250 {ECO:0000244|PDB:1MZN}.
TURN 251 253 {ECO:0000244|PDB:1FM9}.
STRAND 258 261 {ECO:0000244|PDB:1XVP}.
HELIX 264 284 {ECO:0000244|PDB:5MKU}.
HELIX 289 291 {ECO:0000244|PDB:5MKU}.
HELIX 294 316 {ECO:0000244|PDB:5MKU}.
HELIX 317 319 {ECO:0000244|PDB:5MKU}.
STRAND 320 325 {ECO:0000244|PDB:5MKU}.
TURN 327 329 {ECO:0000244|PDB:4N8R}.
STRAND 331 333 {ECO:0000244|PDB:2P1T}.
HELIX 334 339 {ECO:0000244|PDB:5MKU}.
TURN 340 342 {ECO:0000244|PDB:6HN6}.
HELIX 343 352 {ECO:0000244|PDB:5MKU}.
HELIX 354 360 {ECO:0000244|PDB:5MKU}.
HELIX 364 375 {ECO:0000244|PDB:5MKU}.
STRAND 380 382 {ECO:0000244|PDB:3DZU}.
HELIX 386 407 {ECO:0000244|PDB:5MKU}.
HELIX 414 419 {ECO:0000244|PDB:5MKU}.
HELIX 422 441 {ECO:0000244|PDB:5MKU}.
STRAND 447 449 {ECO:0000244|PDB:5MKU}.
HELIX 450 454 {ECO:0000244|PDB:5MKU}.
HELIX 457 459 {ECO:0000244|PDB:3NSQ}.
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


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U2297h CLIA kit Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
U2297h CLIA Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
E2297h ELISA Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
E2297h ELISA kit Homo sapiens,Human,NR1B1,Nuclear receptor subfamily 1 group B member 1,RARA,RAR-alpha,Retinoic acid receptor alpha 96T
Pathways :
WP1963: The effect of Glucocorticoids on target gene expression
WP566: canonical wnt - zebrafish
WP878: EPO Receptor Signaling
WP2272: Pathogenic Escherichia coli infection
WP362: TGF-beta Receptor Signaling Pathway
WP1121: Kit Receptor Signaling Pathway
WP768: EPO Receptor Signaling
WP1309: Toll-like receptor signaling pathway
WP26: Signal Transduction of S1P Receptor
WP474: Endochondral Ossification
WP1011: T Cell Receptor Signaling Pathway
WP780: T Cell Receptor Signaling Pathway
WP1618: alpha-Linolenic acid metabolism
WP1025: B Cell Receptor Signaling Pathway
WP886: Kit Receptor Signaling Pathway
WP1781: Advanced glycosylation endproduct receptor signaling
WP23: B Cell Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP897: Androgen receptor signaling pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP794: B Cell Receptor Signaling Pathway
WP1341: Kit Receptor Signaling Pathway
WP2118: Arrhythmogenic right ventricular cardiomyopathy
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1067: Toll-like receptor signaling pathway

Related Genes :
[rxrga nr2b1 nr2b3a rxr rxra rxrg] Retinoic acid receptor RXR-gamma-A (Nuclear receptor subfamily 2 group B member 3-A) (Retinoic acid receptor RXR-alpha) (Retinoid X receptor alpha) (Retinoid X receptor gamma-A)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rxra Nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[rxrbb nr2b2b rxrd] Retinoic acid receptor RXR-beta-B (Nuclear receptor subfamily 2 group B member 2-B) (Retinoic acid receptor RXR-delta) (Retinoid X receptor beta-B) (Retinoid X receptor delta)
[Rxrb Nr2b2] Retinoic acid receptor RXR-beta (MHC class I regulatory element-binding protein H-2RIIBP) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta)
[Rxrb Nr2b2 Rcor-1] Retinoic acid receptor RXR-beta (Nuclear receptor coregulator 1) (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta) (Fragment)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[RXRB NR2B2] Retinoic acid receptor RXR-beta (Nuclear receptor subfamily 2 group B member 2) (Retinoid X receptor beta)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rxrba nr2b2a rxrb rxre] Retinoic acid receptor RXR-beta-A (Nuclear receptor subfamily 2 group B member 2-A) (Retinoid X receptor beta-A)
[Rxrg Nr2b3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[rxrab nr2b1b rxra rxrg] Retinoic acid receptor RXR-alpha-B (Nuclear receptor subfamily 2 group B member 1-B) (Retinoid X receptor alpha-B)
[RXRG NR2B3] Retinoic acid receptor RXR-gamma (Nuclear receptor subfamily 2 group B member 3) (Retinoid X receptor gamma)
[NR1H4 BAR FXR HRR1 RIP14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[raraa nr1b1a rara2a zgc:109797] Retinoic acid receptor alpha-A (RAR-alpha-A) (Nuclear receptor subfamily 1 group B member 1-A) (Retinoic acid receptor alpha) (zRAR alpha) (Retinoic acid receptor alpha-2.A) (RAR-alpha-2.A)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[rarab nr1b1b rara2b] Retinoic acid receptor alpha-B (RAR-alpha-B) (Nuclear receptor subfamily 1 group B member 1-B) (Retinoic acid receptor alpha-2.B) (RAR-alpha-2.B)
[rxraa nr2b1a] Retinoic acid receptor RXR-alpha-A (Nuclear receptor subfamily 2 group B member 1-A) (RXRalpha-B) (Retinoid X receptor alpha-A)
[Nr1h4 Bar Fxr Rip14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[rxra nr2b1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[Rara Nr1b1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[Nr1h4 Bar Fxr Rip14] Bile acid receptor (Farnesoid X-activated receptor) (Farnesol receptor HRR-1) (Nuclear receptor subfamily 1 group H member 4) (Retinoid X receptor-interacting protein 14) (RXR-interacting protein 14)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[Rarg Nr1b3] Retinoic acid receptor gamma (RAR-gamma) (Nuclear receptor subfamily 1 group B member 3)
[Rarb Nr1b2] Retinoic acid receptor beta (RAR-beta) (Nuclear receptor subfamily 1 group B member 2)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[RARB HAP NR1B2] Retinoic acid receptor beta (RAR-beta) (HBV-activated protein) (Nuclear receptor subfamily 1 group B member 2) (RAR-epsilon)
[rarga nr1b3a rarg rarg2 si:dkey-148f24.2] Retinoic acid receptor gamma-A (RAR-gamma-A) (zRAR gamma) (Nuclear receptor subfamily 1 group B member 3-A) (RAR-gamma-2)

Bibliography :
[26270486] In Silico Adoption of an Orphan Nuclear Receptor NR4A1.
[17367745] Vitamin D receptor-mediated suppression of RelB in antigen presenting cells: a paradigm for ligand-augmented negative transcriptional regulation.
[16819395] Bile salt excretory pump: biology and pathobiology.
[15707588] Proteasome inhibitors induce peroxisome proliferator-activated receptor transactivation through RXR accumulation and a protein kinase C-dependent pathway.
[9372944] Novel receptor interaction and repression domains in the orphan receptor SHP.
[8530418] Multiple functions of the TR2-11 orphan receptor in modulating activation of two key cis-acting elements involved in the retinoic acid signal transduction system.
[8387200] Retinoic acid is a negative regulator of the Epstein-Barr virus protein (BZLF1) that mediates disruption of latent infection.