ERR2_MOUSE
ID ERR2_MOUSE Reviewed; 433 AA.
AC Q61539; A2RTQ7; O09067; O09146; Q8C7A6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Steroid hormone receptor ERR2 {ECO:0000305};
DE AltName: Full=Estrogen receptor-like 2;
DE AltName: Full=Estrogen-related receptor beta {ECO:0000250|UniProtKB:O95718};
DE Short=ERR-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group B member 2;
GN Name=Esrrb {ECO:0000312|MGI:MGI:1346832}; Synonyms=Err-2, Err2, Nr3b2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RX PubMed=8652414; DOI=10.1016/0925-4773(95)00479-3;
RA Pettersson K., Svensson K., Mattsson R., Carlsson B., Ohlsson R.,
RA Berkenstam A.;
RT "Expression of a novel member of estrogen response element-binding nuclear
RT receptors is restricted to the early stages of chorion formation during
RT mouse embryogenesis.";
RL Mech. Dev. 54:211-223(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=9285590; DOI=10.1038/42022;
RA Luo J., Sladek R., Bader J.A., Matthyssen A., Rossant J., Giguere V.;
RT "Placental abnormalities in mouse embryos lacking the orphan nuclear
RT receptor ERR-beta.";
RL Nature 388:778-782(1997).
RN [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17765677; DOI=10.1016/j.devcel.2007.07.011;
RA Chen J., Nathans J.;
RT "Estrogen-related receptor beta/NR3B2 controls epithelial cell fate and
RT endolymph production by the stria vascularis.";
RL Dev. Cell 13:325-337(2007).
RN [7]
RP INTERACTION WITH POU5F1, AND FUNCTION.
RX PubMed=18662995; DOI=10.1128/mcb.00301-08;
RA van den Berg D.L., Zhang W., Yates A., Engelen E., Takacs K.,
RA Bezstarosti K., Demmers J., Chambers I., Poot R.A.;
RT "Estrogen-related receptor beta interacts with Oct4 to positively regulate
RT Nanog gene expression.";
RL Mol. Cell. Biol. 28:5986-5995(2008).
RN [8]
RP INTERACTION WITH NANOG, FUNCTION, AND REGION.
RX PubMed=18957414; DOI=10.1074/jbc.m803481200;
RA Zhang X., Zhang J., Wang T., Esteban M.A., Pei D.;
RT "Esrrb activates Oct4 transcription and sustains self-renewal and
RT pluripotency in embryonic stem cells.";
RL J. Biol. Chem. 283:35825-35833(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18472334; DOI=10.1016/j.neulet.2008.04.044;
RA Real M.A., Heredia R., Davila J.C., Guirado S.;
RT "Efferent retinal projections visualized by immunohistochemical detection
RT of the estrogen-related receptor beta in the postnatal and adult mouse
RT brain.";
RL Neurosci. Lett. 438:48-53(2008).
RN [10]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=20534447; DOI=10.1073/pnas.1000102107;
RA Onishi A., Peng G.H., Poth E.M., Lee D.A., Chen J., Alexis U., de Melo J.,
RA Chen S., Blackshaw S.;
RT "The orphan nuclear hormone receptor ERRbeta controls rod photoreceptor
RT survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11579-11584(2010).
RN [11]
RP INDUCTION, AND FUNCTION.
RX PubMed=23040477; DOI=10.1016/j.stem.2012.08.002;
RA Festuccia N., Osorno R., Halbritter F., Karwacki-Neisius V., Navarro P.,
RA Colby D., Wong F., Yates A., Tomlinson S.R., Chambers I.;
RT "Esrrb is a direct Nanog target gene that can substitute for Nanog function
RT in pluripotent cells.";
RL Cell Stem Cell 11:477-490(2012).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=23040478; DOI=10.1016/j.stem.2012.06.008;
RA Martello G., Sugimoto T., Diamanti E., Joshi A., Hannah R., Ohtsuka S.,
RA Goettgens B., Niwa H., Smith A.;
RT "Esrrb is a pivotal target of the Gsk3/Tcf3 axis regulating embryonic stem
RT cell self-renewal.";
RL Cell Stem Cell 11:491-504(2012).
RN [13]
RP REGION, MUTAGENESIS OF LYS-259; LEU-424 AND PHE-425, FUNCTION, AND
RP INTERACTION WITH NCOA3.
RX PubMed=23019124; DOI=10.1101/gad.195545.112;
RA Percharde M., Lavial F., Ng J.H., Kumar V., Tomaz R.A., Martin N.,
RA Yeo J.C., Gil J., Prabhakar S., Ng H.H., Parker M.G., Azuara V.;
RT "Ncoa3 functions as an essential Esrrb coactivator to sustain embryonic
RT stem cell self-renewal and reprogramming.";
RL Genes Dev. 26:2286-2298(2012).
RN [14]
RP TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH NR0B1, AND FUNCTION.
RX PubMed=23508100; DOI=10.1128/mcb.01520-12;
RA Uranishi K., Akagi T., Sun C., Koide H., Yokota T.;
RT "Dax1 associates with Esrrb and regulates its function in embryonic stem
RT cells.";
RL Mol. Cell. Biol. 33:2056-2066(2013).
RN [15]
RP FUNCTION.
RX PubMed=23169531; DOI=10.1002/stem.1279;
RA Hutchins A.P., Choo S.H., Mistri T.K., Rahmani M., Woon C.T., Ng C.K.,
RA Jauch R., Robson P.;
RT "Co-motif discovery identifies an Esrrb-Sox2-DNA ternary complex as a
RT mediator of transcriptional differences between mouse embryonic and
RT epiblast stem cells.";
RL Stem Cells 31:269-281(2013).
RN [16]
RP FUNCTION, AND INTERACTION WITH KDM1A AND INTEGRATOR COMPLEX.
RX PubMed=26206133; DOI=10.1038/ncomms8776;
RA Latos P.A., Goncalves A., Oxley D., Mohammed H., Turro E., Hemberger M.;
RT "Fgf and Esrrb integrate epigenetic and transcriptional networks that
RT regulate self-renewal of trophoblast stem cells.";
RL Nat. Commun. 6:7776-7776(2015).
RN [17]
RP INTERACTION WITH NR0B1, AND FUNCTION.
RX PubMed=27601327; DOI=10.1016/j.bbrc.2016.09.011;
RA Uranishi K., Akagi T., Koide H., Yokota T.;
RT "Esrrb directly binds to Gata6 promoter and regulates its expression with
RT Dax1 and Ncoa3.";
RL Biochem. Biophys. Res. Commun. 478:1720-1725(2016).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27723719; DOI=10.1038/ncb3418;
RA Festuccia N., Dubois A., Vandormael-Pournin S., Gallego Tejeda E.,
RA Mouren A., Bessonnard S., Mueller F., Proux C., Cohen-Tannoudji M.,
RA Navarro P.;
RT "Mitotic binding of Esrrb marks key regulatory regions of the pluripotency
RT network.";
RL Nat. Cell Biol. 18:1139-1148(2016).
RN [19]
RP INTERACTION WITH JARID2.
RX PubMed=26523946; DOI=10.1002/stem.2243;
RA Iseki H., Nakachi Y., Hishida T., Yamashita-Sugahara Y., Hirasaki M.,
RA Ueda A., Tanimoto Y., Iijima S., Sugiyama F., Yagami K., Takahashi S.,
RA Okuda A., Okazaki Y.;
RT "Combined Overexpression of JARID2, PRDM14, ESRRB, and SALL4A Dramatically
RT Improves Efficiency and Kinetics of Reprogramming to Induced Pluripotent
RT Stem Cells.";
RL Stem Cells 34:322-333(2016).
CC -!- FUNCTION: Transcription factor that binds a canonical ESRRB recognition
CC (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of
CC targets genes regulating their expression or their transcriptional
CC activity (PubMed:27601327, PubMed:23169531, PubMed:23508100,
CC PubMed:26206133, PubMed:20534447, PubMed:18662995, PubMed:18957414,
CC PubMed:27723719, PubMed:23019124). Plays a role, in a LIF-independent
CC manner, in maintainance of self-renewal and pluripotency of embryonic
CC and trophoblast stem cells through different signaling pathways
CC including FGF signaling pathway and Wnt signaling pathways
CC (PubMed:18957414, PubMed:26206133, PubMed:20534447, PubMed:23040478,
CC PubMed:23040477, PubMed:23019124, PubMed:23169531). Upon FGF signaling
CC pathway activation, interacts with KDM1A by directly binding to
CC enhancer site of ELF5 and EOMES and activating their transcription
CC leading to self-renewal of trophoblast stem cells (PubMed:26206133).
CC Also regulates expression of multiple rod-specific genes and is
CC required for survival of this cell type (PubMed:20534447). Plays a role
CC as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1
CC (PubMed:18662995, PubMed:23508100, PubMed:18957414). Plays a role as
CC transcription factor repressor of NFE2L2 transcriptional activity and
CC ESR1 transcriptional activity (By similarity). During mitosis remains
CC bound to a subset of interphase target genes, including pluripotency
CC regulators, through the canonical ESRRB recognition (ERRE) sequence,
CC leading to their transcriptional activation in early G1 phase
CC (PubMed:27723719). Can coassemble on structured DNA elements with other
CC transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger
CC ESRRB-dependent gene activation (PubMed:23019124, PubMed:23169531,
CC PubMed:18662995, PubMed:26206133). This mechanism, in the case of SOX2
CC corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem
CC cells (EpiSC) transition through positive regulation of NR0B1 that
CC inhibits the EpiSC transcriptional program (PubMed:23169531). Also
CC plays a role inner ear development by controlling expression of ion
CC channels and transporters and in early placentation (PubMed:9285590,
CC PubMed:17765677). {ECO:0000250|UniProtKB:O95718,
CC ECO:0000269|PubMed:17765677, ECO:0000269|PubMed:18662995,
CC ECO:0000269|PubMed:18957414, ECO:0000269|PubMed:20534447,
CC ECO:0000269|PubMed:23019124, ECO:0000269|PubMed:23040477,
CC ECO:0000269|PubMed:23040478, ECO:0000269|PubMed:23169531,
CC ECO:0000269|PubMed:23508100, ECO:0000269|PubMed:26206133,
CC ECO:0000269|PubMed:27601327, ECO:0000269|PubMed:27723719,
CC ECO:0000269|PubMed:9285590}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with NR0B1;
CC represses ESRRB activity at the GATA6 promoter (PubMed:27601327,
CC PubMed:23508100). Interacts with NANOG; reciprocally modulates their
CC transcriptional activities and activates POU5F1 expression
CC (PubMed:18957414). Interacts with NCOA3; mediates the interaction
CC between ESRRB and RNA polymerase II complexes and allows NCOA3
CC corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to
CC trigger ESRRB-dependent gene activation involved in self-renewal and
CC pluripotency (PubMed:23019124). Interacts with KDM1A; co-occupes the
CC core set of ESRRB targets including ELF5 and EOMES (PubMed:26206133).
CC Interacts with the multiprotein complex Integrator, at least composed
CC of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7, INTS8, INTS9/RC74,
CC INTS10, INTS11/CPSF3L and INTS12; ESRRB is probably not a core
CC component of the integrator complex and associates to integrator via
CC its interaction with INTS1 and INTS9; attracts the transcriptional
CC machinery (PubMed:26206133). Interacts with JARID2 (PubMed:26523946).
CC Interacts with POU5F1; recruits ESRRB near the POU5F1-SOX2 element in
CC the NANOG proximal promoter leading to activation of NANOG expression;
CC the interaction is DNA independent (PubMed:18662995).
CC {ECO:0000250|UniProtKB:O95718, ECO:0000269|PubMed:18662995,
CC ECO:0000269|PubMed:18957414, ECO:0000269|PubMed:23019124,
CC ECO:0000269|PubMed:23508100, ECO:0000269|PubMed:26206133,
CC ECO:0000269|PubMed:26523946, ECO:0000269|PubMed:27601327}.
CC -!- INTERACTION:
CC Q61539; Q9R190: Mta2; NbExp=2; IntAct=EBI-2312731, EBI-904134;
CC Q61539; Q61066: Nr0b1; NbExp=2; IntAct=EBI-2312731, EBI-2312665;
CC Q61539; Q3UNW5: Tfcp2l1; NbExp=4; IntAct=EBI-2312731, EBI-5691372;
CC Q61539; Q16665: HIF1A; Xeno; NbExp=2; IntAct=EBI-2312731, EBI-447269;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18472334}. Cytoplasm
CC {ECO:0000269|PubMed:18472334}. Chromosome
CC {ECO:0000269|PubMed:27723719}.
CC -!- TISSUE SPECIFICITY: Highly expressed in undifferentiated ESCs
CC (PubMed:23508100). Expressed in immature horizontal cells and in rod
CC photoreceptors at intermediate and late stages of differentiation
CC (PubMed:20534447). Expressed in endolymph-producing epithelial cells
CC (PubMed:17765677). {ECO:0000269|PubMed:17765677,
CC ECO:0000269|PubMed:20534447, ECO:0000269|PubMed:23508100}.
CC -!- DEVELOPMENTAL STAGE: Found in the extra-embryonic ectoderm at 5.5 dpc,
CC 6 dpc and 6.5 dpc. At 7.5 dpc, is exclusively detected in chorion, and
CC at 8.5 dpc is present only at its free margin. Expression is not
CC detected in the ectoplacental cone at any stage of development, nor is
CC placental expression detected after 8.5 dpc.
CC {ECO:0000269|PubMed:9285590}.
CC -!- INDUCTION: Induced by NANOG (PubMed:23040477). Induced by GSK3
CC inhibition through inhibition of TCF3 repression. Repressed by TCF3
CC (PubMed:23040478). Reduced upon differentiation induced by LIF
CC depletion (PubMed:23508100). {ECO:0000269|PubMed:23040477,
CC ECO:0000269|PubMed:23040478, ECO:0000269|PubMed:23508100}.
CC -!- PTM: Acetylated by PCAF/KAT2 (in vitro).
CC {ECO:0000250|UniProtKB:O95718}.
CC -!- DISRUPTION PHENOTYPE: Homozygote Esrrb mutant embryos die at 10.5 dpc.
CC They have severely impaired placental formation. The mutants display
CC abnormal chorion development associated with an overabundance of
CC trophoblast giant cells and a severe deficiency of diploid trophoblast
CC (PubMed:9285590). Conditional knockdown mice exhibit head bobbing and
CC spinning and running in circles and have hearing impairment
CC (PubMed:17765677). {ECO:0000269|PubMed:17765677,
CC ECO:0000269|PubMed:9285590}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; X89594; CAA61755.1; -; mRNA.
DR EMBL; S82458; AAB37687.1; -; mRNA.
DR EMBL; AK052256; BAC34898.1; -; mRNA.
DR EMBL; AC126685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132595; AAI32596.2; -; mRNA.
DR EMBL; BC132597; AAI32598.2; -; mRNA.
DR PIR; S58087; S58087.
DR RefSeq; NP_001152972.1; NM_001159500.1.
DR RefSeq; NP_036064.3; NM_011934.4.
DR AlphaFoldDB; Q61539; -.
DR BMRB; Q61539; -.
DR SMR; Q61539; -.
DR BioGRID; 204938; 180.
DR DIP; DIP-46110N; -.
DR IntAct; Q61539; 29.
DR STRING; 10090.ENSMUSP00000105833; -.
DR iPTMnet; Q61539; -.
DR PhosphoSitePlus; Q61539; -.
DR MaxQB; Q61539; -.
DR PaxDb; Q61539; -.
DR PRIDE; Q61539; -.
DR ProteomicsDB; 275944; -.
DR Antibodypedia; 13059; 325 antibodies from 35 providers.
DR DNASU; 26380; -.
DR Ensembl; ENSMUST00000021680; ENSMUSP00000021680; ENSMUSG00000021255.
DR Ensembl; ENSMUST00000167891; ENSMUSP00000131335; ENSMUSG00000021255.
DR GeneID; 26380; -.
DR KEGG; mmu:26380; -.
DR UCSC; uc007ohw.2; mouse.
DR CTD; 2103; -.
DR MGI; MGI:1346832; Esrrb.
DR VEuPathDB; HostDB:ENSMUSG00000021255; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000153433; -.
DR HOGENOM; CLU_007368_11_0_1; -.
DR InParanoid; Q61539; -.
DR OrthoDB; 669799at2759; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 26380; 4 hits in 62 CRISPR screens.
DR ChiTaRS; Esrrb; mouse.
DR PRO; PR:Q61539; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q61539; protein.
DR Bgee; ENSMUSG00000021255; Expressed in retinal neural layer and 99 other tissues.
DR ExpressionAtlas; Q61539; baseline and differential.
DR Genevisible; Q61539; MM.
DR GO; GO:0000793; C:condensed chromosome; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043697; P:cell dedifferentiation; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0017145; P:stem cell division; IMP:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0001834; P:trophectodermal cell proliferation; IMP:MGI.
DR GO; GO:0001831; P:trophectodermal cellular morphogenesis; IMP:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR027289; Oest-rel_rcp.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PIRSF; PIRSF500939; ERR1-2-3; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..433
FT /note="Steroid hormone receptor ERR2"
FT /id="PRO_0000053663"
FT DOMAIN 208..432
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 100..186
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 103..123
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..163
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..211
FT /note="Interaction with NANOG"
FT /evidence="ECO:0000269|PubMed:18957414"
FT REGION 203..433
FT /note="Essential for ESRRB transcriptional activity and
FT interaction with NCOA3"
FT /evidence="ECO:0000269|PubMed:23019124"
FT SITE 185
FT /note="Important for stabilizing DNA-binding"
FT /evidence="ECO:0000250"
FT MUTAGEN 259
FT /note="K->A: Loss of self-renewal in embryonic stem cells
FT in absence of LIF. Does not interact with NCOA3."
FT /evidence="ECO:0000269|PubMed:23019124"
FT MUTAGEN 424
FT /note="L->A: Loss of self-renewal in embryonic stem cells
FT in absence of LIF; when associated with A-425. Does not
FT interact with NCOA3; when associated with A-425."
FT /evidence="ECO:0000269|PubMed:23019124"
FT MUTAGEN 425
FT /note="F->A: Loss of self-renewal in embryonic stem cells
FT in absence of LIF; when associated with A-424. Does not
FT interact with NCOA3; when associated with A-424."
FT /evidence="ECO:0000269|PubMed:23019124"
FT CONFLICT 394
FT /note="L -> W (in Ref. 1; CAA61755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 48328 MW; 1A0383E7E2ED8BF3 CRC64;
MSSEDRHLGS SCGSFIKTEP SSPSSGIDAL SHHSPSGSSD ASGGFGIALS THANGLDSPP
MFAGAGLGGN PCRKSYEDCT SGIMEDSAIK CEYMLNAIPK RLCLVCGDIA SGYHYGVASC
EACKAFFKRT IQGNIEYNCP ATNECEITKR RRKSCQACRF MKCLKVGMLK EGVRLDRVRG
GRQKYKRRLD SENSPYLNLP ISPPAKKPLT KIVSNLLGVE QDKLYAMPPN DIPEGDIKAL
TTLCELADRE LVFLINWAKH IPGFPSLTLG DQMSLLQSAW MEILILGIVY RSLPYDDKLA
YAEDYIMDEE HSRLVGLLDL YRAILQLVRR YKKLKVEKEE FMILKALALA NSDSMYIENL
EAVQKLQDLL HEALQDYELS QRHEEPRRAG KLLLTLPLLR QTAAKAVQHF YSVKLQGKVP
MHKLFLEMLE AKV
