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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.
05-DEC-2018, entry version 222.
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).
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).
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]
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]
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]
HETERODIMERIZATION WITH PPARA, AND FUNCTION.
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]
PHOSPHORYLATION AT SER-27, FUNCTION, 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]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
HETERODIMERIZATION WITH RARA, FUNCTION, 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).
[24]
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).
[25]
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 129-212 IN COMPLEX WITH DNA.
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).
[37]
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).
[38]
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).
[39]
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).
-!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind
as heterodimers to their target response elements in response to
their ligands, all-trans or 9-cis retinoic acid, and regulate gene
expression in various biological processes. The RAR/RXR
heterodimers bind to the retinoic acid response elements (RARE)
composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. The high
affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a
common heterodimeric partner for a number of nuclear receptors. In
the absence of ligand, the RXR-RAR heterodimers associate with a
multiprotein complex containing transcription corepressors that
induce histone acetylation, chromatin condensation and
transcriptional suppression. On ligand binding, the corepressors
dissociate from the receptors and associate with the coactivators
leading to transcriptional activation. The RXRA/PPARA heterodimer
is required for PPARA transcriptional activity on fatty acid
oxidation genes such as ACOX1 and the P450 system genes.
{ECO:0000269|PubMed:10195690, ECO:0000269|PubMed:11162439,
ECO:0000269|PubMed:11915042, ECO:0000269|PubMed:20215566}.
-!- SUBUNIT: Homodimer. Heterodimer with RARA; required for ligand-
dependent retinoic acid receptor transcriptional activity.
Heterodimer with PPARA (via the leucine-like zipper in the LBD);
the interaction is required for PPARA transcriptional activity.
Also heterodimerizes with PPARG. Interacts with NCOA3 and NCOA6
coactivators. Interacts with FAM120B (By similarity). Interacts
with PELP1, SENP6, SFPQ, DNTTIP2 and RNF8. Interacts with PRMT2.
Interacts with ASXL1 (By similarity). Interacts with BHLHE40/DEC1,
BHLHE41/DEC2, NCOR1 and NCOR2. Interacts in a ligand-dependent
fashion with MED1 and NCOA1. Interacts with VDR. {ECO:0000250,
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:15610733, ECO:0000269|PubMed:16574651,
ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:19786558,
ECO:0000269|PubMed:28698609, 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}.
-!- 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: Highly expressed in liver, also found in lung,
kidney and heart.
-!- 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: Phosphorylated on serine and threonine residues mainly in the
N-terminal modulating domain. Constiutively phosphorylated on Ser-
21 in the presence or absence of ligand. 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. This phosphorylation is required for repression of cAMP-
mediated transcriptional activity of RARA. {ECO:0000250,
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]
UniGene; Hs.590886; -.
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; 1LBD; X-ray; 2.70 A; A=201-460.
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; 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.
PDBsum; 1BY4; -.
PDBsum; 1DSZ; -.
PDBsum; 1FBY; -.
PDBsum; 1FM6; -.
PDBsum; 1FM9; -.
PDBsum; 1G1U; -.
PDBsum; 1G5Y; -.
PDBsum; 1K74; -.
PDBsum; 1LBD; -.
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; 6A5Y; -.
PDBsum; 6A5Z; -.
PDBsum; 6A60; -.
DisProt; DP00062; -.
ProteinModelPortal; P19793; -.
SMR; P19793; -.
BioGrid; 112168; 119.
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; -.
MaxQB; P19793; -.
PaxDb; P19793; -.
PeptideAtlas; P19793; -.
PRIDE; P19793; -.
ProteomicsDB; 53687; -.
DNASU; 6256; -.
Ensembl; ENST00000481739; ENSP00000419692; ENSG00000186350. [P19793-1]
GeneID; 6256; -.
KEGG; hsa:6256; -.
UCSC; uc004cfb.3; human. [P19793-1]
CTD; 6256; -.
DisGeNET; 6256; -.
EuPathDB; HostDB:ENSG00000186350.9; -.
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; -.
HOVERGEN; HBG005606; -.
InParanoid; P19793; -.
KO; K08524; -.
OMA; LTCGMKR; -.
OrthoDB; EOG091G0YX6; -.
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.
CleanEx; HS_RXRA; -.
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:0004886; F:9-cis retinoic acid receptor activity; TAS:ProtInc.
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:0003708; F:retinoic acid receptor activity; TAS:BHF-UCL.
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: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: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: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: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.
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; Alternative splicing; Complete proteome; DNA-binding;
Host-virus interaction; Isopeptide bond; Metal-binding; 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 201 224 Hinge.
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 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}.
STRAND 131 134 {ECO:0000244|PDB:4CN5}.
TURN 136 138 {ECO:0000244|PDB:1DSZ}.
STRAND 141 146 {ECO:0000244|PDB:1DSZ}.
STRAND 149 151 {ECO:0000244|PDB:4CN5}.
HELIX 153 165 {ECO:0000244|PDB:1DSZ}.
STRAND 172 175 {ECO:0000244|PDB:2NLL}.
TURN 181 186 {ECO:0000244|PDB:1DSZ}.
HELIX 188 197 {ECO:0000244|PDB:1DSZ}.
HELIX 202 204 {ECO:0000244|PDB:1DSZ}.
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:1LBD}.
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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