ID   ESR2_STUVU              Reviewed;         554 AA.
AC   Q9PVE2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=NR3A2;
OS   Sturnus vulgaris (Starling).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sturnidae; Sturnus.
OX   NCBI_TaxID=9172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10499520; DOI=10.1210/endo.140.10.7024;
RA   Bernard D.J., Bentley G.E., Balthazart J., Turek F.W., Ball G.F.;
RT   "Androgen receptor, estrogen receptor alpha, and estrogen receptor beta
RT   show distinct patterns of expression in forebrain song control nuclei of
RT   European starlings.";
RL   Endocrinology 140:4633-4643(1999).
CC   -!- FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha,
CC       and activates expression of reporter genes containing estrogen response
CC       elements (ERE) in an estrogen-dependent manner. Locally synthesized
CC       estrogens may act via ER beta, in addition to ER alpha, to mediate
CC       seasonal or developmental effects on nearby song nuclei.
CC       {ECO:0000250|UniProtKB:Q92731}.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-alpha
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Brain, pituitary, skeletal muscle, liver, adrenal,
CC       kidney, intestine and ovary.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC       DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF113513; AAD56593.1; -; mRNA.
DR   RefSeq; NP_001310518.1; NM_001323589.1.
DR   AlphaFoldDB; Q9PVE2; -.
DR   SMR; Q9PVE2; -.
DR   PRIDE; Q9PVE2; -.
DR   GeneID; 106850206; -.
DR   CTD; 2100; -.
DR   OrthoDB; 487299at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:InterPro.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:InterPro.
DR   GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:InterPro.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 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   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; 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   2: Evidence at transcript level;
KW   DNA-binding; Lipid-binding; Metal-binding; Nucleus; Receptor;
KW   Steroid-binding; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..554
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053650"
FT   DOMAIN          289..521
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        174..239
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         174..194
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         210..234
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          25..173
FT                   /note="Modulating"
FT   REGION          529..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  62174 MW;  EC13A961CEBE59C9 CRC64;
     MSLCTSSHKD FSQLLPLQDI GCNKTEIKNS PAGVISPAPY SCNQSTLTAE HSPVYIPSSY
     MESRHEYSTM AFCSPAMVNY NIASNFGDPE AVAARQTSSP GALWSAPGHL SPLSLHCQSS
     LLYAEQPKSL WCEARPMEPV LPGSRETLKR KTNGNDCTSP IANNPGSKKD AHFCAVCSDY
     ASGYHYGVWS CEGCKAFFKR SIQGHNDYIC PATNQCTIDK NRRKSCQACR LRKCYEVGMM
     KCGSRRERCG YRILRSHRGA EERVHCLGRA RRYSEAATRV KEILLSTVSP EQFVLTLLEA
     EPPHVLVSRP SKPFTEASMM MSLTKLADKE LVHMIGWAKK IPGFIDLSLY DQVRLLESCW
     MEVLMIGLMW RSIDHPGKLI FAPDLVLDRD EGKCVEGILE IFDMLLAMTS RFRELKLQHK
     EYLCVKAMIL LNSSMFPLSA EEPESNRKLH HLLNVVTEAL VWVIAKSGIP SQQQTTRLAN
     LLMLLSHVRH ASNKGMEHLL SMKCKNVVPV YDLLLEMLNA HTLRGQRKPL ATHPEFGPLE
     QMEPGESLRK GEPQ