ID   ESR2_COTJA              Reviewed;         472 AA.
AC   O93511;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   03-AUG-2022, entry version 120.
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   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Foidart A., Lakaye B., Grisar T., Ball G.F., Balthazart J.;
RT   "Sequence and neuroanatomical distribution of estrogen receptor beta in the
RT   quail brain.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-286.
RC   TISSUE=Testis;
RX   PubMed=9760113; DOI=10.1097/00001756-199808240-00011;
RA   Lakaye B., Foidart A., Grisar T., Balthazart J.;
RT   "Partial cloning and distribution of estrogen receptor beta in the avian
RT   brain.";
RL   NeuroReport 9:2743-2748(1998).
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       {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: A high expression is seen in the telencephalon,
CC       diencephalon, pituitary, testis and kidneys but little or no expression
CC       is seen in the cerebellum, pectoral muscle and adrenal gland.
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; AF045149; AAC36463.2; -; mRNA.
DR   AlphaFoldDB; O93511; -.
DR   SMR; O93511; -.
DR   Proteomes; UP000694412; Unplaced.
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   Reference proteome; Steroid-binding; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..472
FT                   /note="Estrogen receptor beta"
FT                   /id="PRO_0000053649"
FT   DOMAIN          217..449
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        105..170
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         105..125
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         141..165
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..104
FT                   /note="Modulating"
SQ   SEQUENCE   472 AA;  53411 MW;  DF7A78F0FDBD18BD CRC64;
     MAFCSPAMMN YNIASNFGDS ESASVRQTSS PSLLWSAPGH LSPLTLHCQL SLLYAEQPKS
     PWCEARPLEP VLPVSRETLK RKTNGSDCTS PIASNPGSKR DAHFCAVCSD YASGYHYGVW
     SCEGCKAFFK RSIQGHNDYI CPATNQCTID KNRRKSCQAC RLRKCYEVGM MKCGSRRERC
     GYRILRRHRN SEDCMGKTKK YNEAATRVKE ILLSTVSPEQ FVLTLLEAEP PNVLVSRPSK
     PFTEASMMMS LTKLADKELV HMIGWAKKIP GFIDLSLYDQ VRLLESCWLE VLMIGLMWRS
     IDHPGKLIFA PDLVLDRDEG KCVEGILEIF DMLLAMTSRF RELKLQHKEY LCVKAMILLN
     SSMFPLSAEE PESNRKLHHL LNVVTDALVW VIAKSGIPSQ QQTTRLANLL MLLSHVRHAS
     NKGMEHLLSM KCKNVVPVYD LLLEMLNAHT LRGQRKSPVT HPDFEQVSHF QV