ID   ESR22_CARAU             Reviewed;         610 AA.
AC   Q9IAL9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Estrogen receptor beta-2;
DE            Short=ER-beta-2;
DE   AltName: Full=Nuclear receptor subfamily 3 group A member 2-B;
GN   Name=esr2b; Synonyms=nr3a2b;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Pituitary;
RX   PubMed=10786629; DOI=10.1016/s0167-4781(99)00235-3;
RA   Ma C.H., Dong K.W., Yu K.L.;
RT   "cDNA cloning and expression of a novel estrogen receptor beta-subtype in
RT   goldfish (Carassius auratus).";
RL   Biochim. Biophys. Acta 1490:145-152(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: Predominantly expressed in pituitary, telencephalon
CC       and hypothalamus as well as in the liver.
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; AF177465; AAF35170.1; -; mRNA.
DR   AlphaFoldDB; Q9IAL9; -.
DR   SMR; Q9IAL9; -.
DR   Proteomes; UP000515129; Genome assembly.
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..610
FT                   /note="Estrogen receptor beta-2"
FT                   /id="PRO_0000053653"
FT   DOMAIN          302..538
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          1..170
FT                   /note="Modulating"
FT   REGION          566..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  67852 MW;  D29F2CDFCC165C67 CRC64;
     MSSSTGPAPA SASPVQANRG NSPNILPLLY TSQLGMDSQT ICIPSPYVEA CQDYSPPHGG
     EISHGALTLY SPVSSPVLGY THPPVSESLV PLNSAIFWPP HPTHSTPSLH CPSPLAYRET
     HAHTTWEDAK THINQSSSVL THAKLLGQQL DGDDGLNPSP GILGKGDTHF CAVCHDYASG
     YHYGVWSCEG CKAFFKRSIQ GHNDYICPAT NQCTIDKSRR KSCQACRLRK CYEVGMMKCG
     VRRERCSYRG GRHRRNPPIR DSSGGAIGVR GHSQPHLEFP LSPTHPLFPL GDRAEGCGQN
     LSPEQLVNCI LEAEPPQIYL REPIKKPYTE ASMMMSLTNL ADKELVLMIS WAKKIPGFVE
     LTLSDQVHLL ECCWLDILML GLMWRSVDHP GKLIFSPDLK LNRDEGTCVE GIMEIFDMLL
     ATTSRFRELK LQREEYVCLK AMILLNSSNC SRLPQTPEDV ESRGKVLRLL DSVTDALVWT
     ISRTGLSSHQ QSIRLAHLLM LLSHIRHLSN KGIEHLSTMK RKNVVLLYDL LLEMLDANTS
     QSSRMLAAHT KASLRMDTQQ TTEILHTSKQ QPALKESNQD TRHSPQAEGT VDKTLHRVDK
     TLHRVDVDTD