ID   ESR2_ANGJA              Reviewed;         573 AA.
AC   O13012;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8793852; DOI=10.1016/0303-7207(96)03792-6;
RA   Todo T., Adachi S., Yamauchi K.;
RT   "Molecular cloning and characterization of Japanese eel estrogen receptor
RT   cDNA.";
RL   Mol. Cell. Endocrinol. 119:37-45(1996).
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.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-
CC       alpha.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- INDUCTION: By 17-beta-estradiol.
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; AB003356; BAA19851.1; -; mRNA.
DR   AlphaFoldDB; O13012; -.
DR   SMR; O13012; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042562; F:hormone binding; IEA:UniProt.
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..573
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053651"
FT   DOMAIN          291..527
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        171..236
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         171..191
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         207..231
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          15..170
FT                   /note="Modulating"
FT   REGION          534..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  63421 MW;  9C64C1D8D39ED4CC CRC64;
     MAGSPGNELP LLQLQEVDSS KVGESGGSSG LLPTMYNGAL PALSMESHAV CIPSPYTDSS
     HDYAALTFYS PPILSHGGPA VPESPAARQS LSPSLFWPAH GHHGHVSPLA LHFQQPLVYR
     EPAHSPWAEP KPLEHGQAQT SKLAGKRMAE SEEGTSSVGG CFAGKGDMHF CAVCHDYASG
     YHYGVWSCEG CKAFFKRSIQ GHNGYICPAT NQCTIDKNRR KSCQACRLRK CYEVGMMKCG
     VRRERCTYRG ARHRRMPHIR ELAGTGGGAR TQRRGEGVVP QTQEAQSSAL TPEQLINRII
     EAEPPEIYLM KELKKPFTED SMMMSLTNLA DKELVLMISW AKKIPGFVEL DLSDQVHLLE
     CCWLEVLMLG LMWRSVDHPG KLIFSPDLKL NRDEGSCVEG ILEIFDMVLA ATSRFRELKL
     QREEYVCLKA IILLNPNLCT TSSENREELE SRNKLLHMLD SVTDALVWTI AKKGLTFQQQ
     SARLAHLLML LAHIRHLSNK GMEHLSNMKR KNVVPLYDLL LEMLDANTMH SSRMSASYSS
     QPSPWSQAAQ SQPGPPPSCS GECPCPPKES STI