ID ESR2_MOUSE Reviewed; 530 AA. AC O08537; B2RUC6; E9QKX7; O35635; O70519; Q8BG65; Q91Z86; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 3. DT 27-MAR-2024, entry version 214. DE RecName: Full=Estrogen receptor beta; DE Short=ER-beta; DE AltName: Full=Nuclear receptor subfamily 3 group A member 2; GN Name=Esr2; Synonyms=Estrb, Nr3a2; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Ovary; 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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530, AND MUTAGENESIS OF SER-105 AND RP SER-139. RC STRAIN=129/Sv; TISSUE=Ovary; RX PubMed=9058381; DOI=10.1210/mend.11.3.9902; RA Tremblay G.B., Tremblay A., Copeland N.G., Gilbert D.J., Jenkins N.A., RA Labrie F., Giguere V.; RT "Cloning, chromosomal localization, and functional analysis of the murine RT estrogen receptor beta."; RL Mol. Endocrinol. 11:353-365(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-530, AND CHARACTERIZATION. RC TISSUE=Ovary; RX PubMed=9280064; DOI=10.1210/mend.11.10.9989; RA Pettersson K., Grandien K., Kuiper G.G.J.M., Gustafsson J.-A.; RT "Mouse estrogen receptor beta forms estrogen response element-binding RT heterodimers with estrogen receptor alpha."; RL Mol. Endocrinol. 11:1486-1496(1997). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), AND INDUCTION. RC STRAIN=ddY; TISSUE=Calvaria; RX PubMed=11878304; DOI=10.1359/jbmr.2002.17.3.394; RA Dang Z.C., van Bezooijen R.L., Karperien M., Papapoulos S.E., Lowik C.W.; RT "Exposure of KS483 cells to estrogen enhances osteogenesis and inhibits RT adipogenesis."; RL J. Bone Miner. Res. 17:394-405(2002). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60. RC TISSUE=Ovary; RA Leygue E., Lu B., Dotzlaw H., Glor C., Watson P.H., Murphy L.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-60. RC TISSUE=Ovary; RA Rosenfeld C.S., Lubahn D.B.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP INTERACTION WITH NCOA3. RX PubMed=9192892; DOI=10.1038/42652; RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., RA Rosenfeld M.G.; RT "The transcriptional co-activator p/CIP binds CBP and mediates nuclear- RT receptor function."; RL Nature 387:677-684(1997). RN [10] RP TISSUE SPECIFICITY. RX PubMed=9607809; DOI=10.1210/endo.139.6.6028; RA Rosenfeld C.S., Ganjam V.K., Taylor J.A., Yuan X., Stiehr J.R., Hardy M.P., RA Lubahn D.B.; RT "Transcription and translation of estrogen receptor-beta in the male RT reproductive tract of estrogen receptor-alpha knock-out and wild-type RT mice."; RL Endocrinology 139:2982-2987(1998). RN [11] RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5). RC TISSUE=Ovary; RX PubMed=9685228; DOI=10.1016/s0303-7207(98)00050-1; RA Lu B., Leygue E., Dotzlaw H., Murphy L.J., Murphy L.C., Watson P.H.; RT "Estrogen receptor-beta mRNA variants in human and murine tissues."; RL Mol. Cell. Endocrinol. 138:199-203(1998). RN [12] RP PHOSPHORYLATION AT SER-87 AND SER-105. RX PubMed=10230404; DOI=10.1016/s1097-2765(00)80479-7; RA Tremblay A., Tremblay G.B., Labrie F., Giguere V.; RT "Ligand-independent recruitment of SRC-1 to estrogen receptor beta through RT phosphorylation of activation function AF-1."; RL Mol. Cell 3:513-519(1999). RN [13] RP GLYCOSYLATION AT SER-61, AND PHOSPHORYLATION AT SER-61. RX PubMed=10995228; DOI=10.1021/bi000755i; RA Cheng X., Cole R.N., Zaia J., Hart G.W.; RT "Alternative O-glycosylation/O-phosphorylation of the murine estrogen RT receptor beta."; RL Biochemistry 39:11609-11620(2000). RN [14] RP INTERACTION WITH NCOA6. RX PubMed=10788465; DOI=10.1074/jbc.275.18.13510; RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.; RT "Isolation and characterization of peroxisome proliferator-activated RT receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR."; RL J. Biol. Chem. 275:13510-13516(2000). RN [15] RP INTERACTION WITH RBM39. RX PubMed=11704680; DOI=10.1074/jbc.m110417200; RA Jung D.-J., Na S.-Y., Na D.S., Lee J.W.; RT "Molecular cloning and characterization of CAPER, a novel coactivator of RT activating protein-1 and estrogen receptors."; RL J. Biol. Chem. 277:1229-1234(2002). CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity CC similar to that of ESR1/ER-alpha, and activates expression of reporter CC genes containing estrogen response elements (ERE) in an estrogen- CC dependent manner. {ECO:0000250|UniProtKB:Q92731}. CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1. CC Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a CC strong increase of transcription of target genes. Interacts with UBE1C CC and AKAP13. Interacts with DNTTIP2 (By similarity). Interacts with CC CCDC62 in the presence of estradiol/E2; this interaction seems to CC enhance the transcription of target genes. Interacts with DNAAF4. CC Interacts with PRMT2. Interacts with CCAR2 (via N-terminus) in a CC ligand-independent manner (By similarity). Interacts with RBM39, in the CC presence of estradiol (E2) (PubMed:11704680). Interacts with STUB1/CHIP CC (By similarity). {ECO:0000250|UniProtKB:Q62986, CC ECO:0000250|UniProtKB:Q92731, ECO:0000269|PubMed:11704680}. CC -!- INTERACTION: CC O08537; P01101: Fos; NbExp=2; IntAct=EBI-2526214, EBI-4288185; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Beta-1; CC IsoId=O08537-1; Sequence=Displayed; CC Name=2; Synonyms=Beta-2; CC IsoId=O08537-2; Sequence=VSP_003693; CC Name=3; Synonyms=Beta-5A; CC IsoId=O08537-4; Sequence=VSP_003696; CC Name=4; CC IsoId=O08537-6; Sequence=VSP_042429, VSP_042430; CC Name=5; CC IsoId=O08537-7; Sequence=VSP_042431, VSP_042432; CC -!- TISSUE SPECIFICITY: Expressed in prostate, ovary, Leydig cells and in CC epithelium of the efferent ductules and of the initial segment of the CC epididymis. {ECO:0000269|PubMed:9607809}. CC -!- INDUCTION: Isoforms 1 and 2 are down-regulated by 17-beta-estradiol. CC {ECO:0000269|PubMed:11878304}. CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a CC DNA-binding domain and a C-terminal ligand-binding domain. CC -!- PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1. CC {ECO:0000269|PubMed:10230404, ECO:0000269|PubMed:10995228}. CC -!- MISCELLANEOUS: [Isoform 3]: Corresponds to exons 5 and 6 deletion. CC {ECO:0000305|PubMed:9685228}. CC -!- MISCELLANEOUS: [Isoform 4]: Corresponds to exon 5 deletion CC (PubMed:9685228). May be produced at very low levels due to a premature CC stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No CC experimental confirmation available. {ECO:0000305|PubMed:9685228}. CC -!- MISCELLANEOUS: [Isoform 5]: Corresponds to exon 6 deletion CC (PubMed:9685228). May be produced at very low levels due to a premature CC stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No CC experimental confirmation available. {ECO:0000305|PubMed:9685228}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC17919.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI41076.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI45330.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAL15175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC35719.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC35770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK054290; BAC35719.1; ALT_INIT; mRNA. DR EMBL; AK054413; BAC35770.1; ALT_INIT; mRNA. DR EMBL; AC164121; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC141075; AAI41076.1; ALT_INIT; mRNA. DR EMBL; BC145329; AAI45330.1; ALT_INIT; mRNA. DR EMBL; U81451; AAB51132.1; -; mRNA. DR EMBL; AJ000220; CAA03949.1; -; Genomic_DNA. DR EMBL; AY054413; AAL15175.1; ALT_INIT; mRNA. DR EMBL; AF067422; AAC17919.1; ALT_INIT; mRNA. DR EMBL; AF063853; AAC16656.1; -; mRNA. DR RefSeq; NP_034287.3; NM_010157.3. DR RefSeq; NP_997590.1; NM_207707.1. DR AlphaFoldDB; O08537; -. DR SMR; O08537; -. DR BioGRID; 199522; 3. DR IntAct; O08537; 2. DR STRING; 10090.ENSMUSP00000151463; -. DR BindingDB; O08537; -. DR ChEMBL; CHEMBL2995; -. DR DrugCentral; O08537; -. DR GuidetoPHARMACOLOGY; 621; -. DR GlyConnect; 146; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; O08537; 1 site, 1 glycan. DR GlyGen; O08537; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O08537; -. DR PhosphoSitePlus; O08537; -. DR PaxDb; 10090-ENSMUSP00000098849; -. DR Antibodypedia; 11874; 1947 antibodies from 45 providers. DR DNASU; 13983; -. DR Ensembl; ENSMUST00000101291.11; ENSMUSP00000098849.5; ENSMUSG00000021055.15. [O08537-2] DR Ensembl; ENSMUST00000110421.9; ENSMUSP00000106051.3; ENSMUSG00000021055.15. [O08537-1] DR Ensembl; ENSMUST00000133564.9; ENSMUSP00000138637.3; ENSMUSG00000021055.15. [O08537-6] DR GeneID; 13983; -. DR KEGG; mmu:13983; -. DR UCSC; uc007nxu.1; mouse. [O08537-2] DR UCSC; uc007nxv.1; mouse. [O08537-1] DR AGR; MGI:109392; -. DR CTD; 2100; -. DR MGI; MGI:109392; Esr2. DR VEuPathDB; HostDB:ENSMUSG00000021055; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000156116; -. DR InParanoid; O08537; -. DR OMA; HRNSEDQ; -. DR OrthoDB; 5387678at2759; -. DR TreeFam; TF323751; -. DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling. DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway. DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-MMU-8939211; ESR-mediated signaling. DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling. DR BioGRID-ORCS; 13983; 2 hits in 81 CRISPR screens. DR ChiTaRS; Esr2; mouse. DR PRO; PR:O08537; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; O08537; Protein. DR Bgee; ENSMUSG00000021055; Expressed in animal zygote and 68 other cell types or tissues. DR ExpressionAtlas; O08537; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; ISO:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:1903924; F:estradiol binding; ISO:MGI. DR GO; GO:0099130; F:estrogen binding; ISO:MGI. DR GO; GO:0034056; F:estrogen response element binding; ISO:MGI. DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI. DR GO; GO:0042562; F:hormone binding; ISO:MGI. DR GO; GO:0030284; F:nuclear estrogen receptor activity; ISO:MGI. DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI. DR GO; GO:0003707; F:nuclear steroid receptor activity; ISO:MGI. DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI. DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI. DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB. DR GO; GO:1990239; F:steroid hormone binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI. DR GO; GO:0001662; P:behavioral fear response; ISO:MGI. DR GO; GO:0007420; P:brain development; IMP:MGI. DR GO; GO:0008283; P:cell population proliferation; IGI:MGI. DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:MGI. DR GO; GO:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI. DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IMP:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI. DR GO; GO:0044849; P:estrous cycle; ISO:MGI. DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; IMP:MGI. DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IMP:MGI. DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISO:MGI. DR GO; GO:0007611; P:learning or memory; ISO:MGI. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:MGI. DR GO; GO:0048521; P:negative regulation of behavior; ISO:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI. DR GO; GO:2000252; P:negative regulation of feeding behavior; ISO:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0001764; P:neuron migration; IMP:MGI. DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0033574; P:response to testosterone; ISO:MGI. DR GO; GO:0060011; P:Sertoli cell proliferation; ISO:MGI. DR GO; GO:0060065; P:uterus development; IGI:MGI. DR GO; GO:0060068; P:vagina development; IGI:MGI. DR GO; GO:0042311; P:vasodilation; ISO:MGI. DR CDD; cd07171; NR_DBD_ER; 1. DR CDD; cd06949; NR_LBD_ER; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR021064; ER-beta-like_N. DR InterPro; IPR028355; ER-beta/gamma. 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; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR PANTHER; PTHR48092:SF12; ESTROGEN RECEPTOR BETA; 1. DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1. DR Pfam; PF12497; ERbeta_N; 1. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PIRSF; PIRSF500102; ER-b; 1. DR PIRSF; PIRSF002527; ER-like_NR; 1. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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 Activator; Alternative splicing; DNA-binding; Glycoprotein; Lipid-binding; KW Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome; KW Steroid-binding; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..530 FT /note="Estrogen receptor beta" FT /id="PRO_0000053644" FT DOMAIN 264..498 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 149..214 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 149..169 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 185..209 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT REGION 1..148 FT /note="Modulating" FT REGION 506..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 61 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000269|PubMed:10995228" FT MOD_RES 87 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000269|PubMed:10230404" FT MOD_RES 105 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000269|PubMed:10230404" FT CARBOHYD 61 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000269|PubMed:10995228" FT /id="CAR_000201" FT VAR_SEQ 319..409 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_003696" FT VAR_SEQ 319..343 FT /note="FVELSLLDQVRLLESCWMEVLMVGL -> MRGSAWKGFWKSLTCSWRRRHGS FT VS (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_042429" FT VAR_SEQ 344..530 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_042430" FT VAR_SEQ 364 FT /note="R -> RSSEDPHWHVAQTKSAVPR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11878304, FT ECO:0000303|PubMed:16141072" FT /id="VSP_003693" FT VAR_SEQ 365..377 FT /note="DEGKCVEGILEIF -> YVPLGYRKPGSRE (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_042431" FT VAR_SEQ 378..530 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_042432" FT MUTAGEN 105 FT /note="S->A: Abolishes stimulatory effect of Ras." FT /evidence="ECO:0000269|PubMed:9058381" FT MUTAGEN 139 FT /note="S->A: No loss of the stimulatory effect of Ras." FT /evidence="ECO:0000269|PubMed:9058381" FT CONFLICT 47 FT /note="T -> A (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="A -> T (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" FT CONFLICT 200 FT /note="S -> N (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="D -> G (in Ref. 1; AAB51132 and 6; AAL15175)" FT /evidence="ECO:0000305" FT CONFLICT 412 FT /note="P -> H (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" FT CONFLICT 445 FT /note="G -> R (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="E -> G (in Ref. 5; CAA03949)" FT /evidence="ECO:0000305" SQ SEQUENCE 530 AA; 59070 MW; BEFA25F62650A8D4 CRC64; MEIKNSPSSL TSPASYNCSQ SILPLEHGPI YIPSSYVESR HEYSAMTFYS PAVMNYSVPS STGNLEGGPV RQTASPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN RETLKRKLGG SGCASPVTSP SAKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSASEQVH CLNKAKRTSG HTPRVKELLL NSLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL VLDRDEGKCV EGILEIFDML LATTARFREL KLQHKEYLCV KAMILLNSSM YPLATASQEA ESSRKLTHLL NAVTDALVWV ISKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECCSTEDSKS KEGSQNLQSQ //