ID   ESR2_MICUN              Reviewed;         673 AA.
AC   P57781;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Micropogonias undulatus (Atlantic croaker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Sciaenidae; Micropogonias.
OX   NCBI_TaxID=29154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=11005855; DOI=10.1073/pnas.97.20.10751;
RA   Hawkins M.B., Thornton J.W., Crews D., Skipper J.K., Dotte A., Thomas P.;
RT   "Identification of a third distinct estrogen receptor and reclassification
RT   of estrogen receptors in teleosts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10751-10756(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   -!- TISSUE SPECIFICITY: Abundant in the liver and testes, less abundant in
CC       the ovary and barely detectable in the muscle.
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; AF298181; AAG16711.1; -; mRNA.
DR   AlphaFoldDB; P57781; -.
DR   SMR; P57781; -.
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..673
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053655"
FT   DOMAIN          316..552
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        182..247
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         182..202
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         218..242
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..181
FT                   /note="Modulating"
FT   REGION          553..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  74680 MW;  28394517577E3D01 CRC64;
     MASSPGLDPH PLPMLQLQEV GSSKVSERPR SPGLLPAVYS PPLGMDSHTV CIPSPYTDSS
     HEYNHSHGPL TFYSPSVLSY SRPPITNSPS SLCPSLSPSA FWPSHNHPTM PSLTLHCPES
     IVYNEPSPHA PWLESKAHSI NASSSSIIGC NKSLVKRSEE GVEDMNSSLC SSAVGKADMH
     FCAVCHDYAS GYHYGVWSCE GCKAFFKRSI QGHNDYICPA TNQCTIDKNR RKSCQACRLR
     KCYEVGMMKC GVRRERCSYR GARHRRGGLQ PRDPTGRGLV RVGLGSRAQR HLHLEAPLTP
     LAPILQAKHV HLSAMSPEEF ISRIMDAEPP EIYLMEDLKK PFTEASMMMS LTNLADKELV
     FMISWAKKIP GFVELSLADQ INLLKCCWLE ILMLGLMWRS VDHPGKLIFS PDFKLNREEG
     QCVEGIMEIF DMLLAGTSRF RELKLQREEY VCLKAMILLN SNLCTSSPQT AEELESRNKL
     LRLLDSVIDA LVWAISKMGL TTQQQTLRLG HLTMLLSHIR HVSNKGMDHL STMKRKNVVL
     VYDLLLEMLD ANTSSGGSQP SSSPSSETYS DQHQYPQPPS HLHPGSEQTT ADHAIVPPLG
     PTDDPILDGH LDAMPLQSSP PFQSLVVPHM DTNDYIHPEQ WSLGTGDAAP SVEPTDYITT
     ERVVMETALV TQP