ID   ESR2_SPAAU              Reviewed;         559 AA.
AC   Q9W6M2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 111.
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   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=10927619; DOI=10.1677/joe.0.1660293;
RA   Socorro S., Power D.M., Olsson P.-E., Canario A.V.M.;
RT   "Two estrogen receptors expressed in the teleost fish, Sparus aurata: cDNA
RT   cloning, characterization and tissue distribution.";
RL   J. Endocrinol. 166:293-306(2000).
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-alpha
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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; AF136980; AAD31033.1; -; mRNA.
DR   AlphaFoldDB; Q9W6M2; -.
DR   SMR; Q9W6M2; -.
DR   Proteomes; UP000472265; Unplaced.
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   Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..559
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053658"
FT   DOMAIN          273..509
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        156..221
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         156..176
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         192..216
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..155
FT                   /note="Modulating"
FT   REGION          128..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  62698 MW;  65612384B71DF76D CRC64;
     MAVACSPEKD QSLLQLQKVD SSRVILSPVL SSPMETNQPI CIPSPYTDRG HDFPTIPFYS
     ATNFSYANPP AISDRPSVHQ TLSPSLFWPS HGHVGTTLPL HHLQARPQHG QAVQSPWVEL
     SPLDNVLTSS KSARRRSQEN EEGEVSSGGK ADLHFCAVCH DYASGYHYGV WSCEGCKAFF
     KRSIQRHNDY ICPATNQCTI DKNRRKSCQA CRLHKCYNVG MTKCGMRKER GNFRDPQMRR
     VTRLSSQGRT SGPSVLNGPA VGPLNTPQPP ALTSKQLIER IMEAEPPEIY LMKDMRRPLT
     EANIMMSLTN LADKELVHMI TWAKKIPGFL ELGLLDQVHL LECCWLEVLM IGLMWRSVDH
     PGKLIFSPDL SLSREEGSCV QGFLEIFDML IAATSRVREL KLQREEYVCL KAMILLNSNM
     CLSSSEGSEE LQSRSKLLRL LDAVTDALVW AIAKTGLTFR QQYTRLAHLL MLLSHIRHVS
     NKGMDHLHGM KMKNMVPLYD LLLEMLDAHI MHSSRLPRRS PQQETVEQCD APARPHSPGT
     SGPTNTWTPS CTGGRGEPQ