ID   ESR1_MICUN              Reviewed;         525 AA.
AC   P57753;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Estrogen receptor;
DE            Short=ER;
DE   AltName: Full=ER-alpha;
DE   AltName: Full=Estradiol receptor;
DE   AltName: Full=Nuclear receptor subfamily 3 group A member 1;
DE   Flags: Fragment;
GN   Name=esr1; Synonyms=esr, nr3a1;
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=Liver;
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: The steroid hormones and their receptors are involved in the
CC       regulation of eukaryotic gene expression and affect cellular
CC       proliferation and differentiation in target tissues.
CC   -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ER-beta
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Abundant in the liver, less abundant in the testes
CC       and barely detectable in the ovary and brain.
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; AF298183; AAG16713.1; -; mRNA.
DR   AlphaFoldDB; P57753; -.
DR   SMR; P57753; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042562; F:hormone binding; IEA:UniProt.
DR   GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.565.10; -; 1.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR   InterPro; IPR001292; Estr_rcpt.
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; PF00104; Hormone_recep; 1.
DR   Pfam; PF02159; Oest_recep; 1.
DR   Pfam; PF00105; zf-C4; 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; 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..525
FT                   /note="Estrogen receptor"
FT                   /id="PRO_0000053630"
FT   DOMAIN          210..446
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        83..148
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         83..103
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         119..143
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          <1..82
FT                   /note="Modulating"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..209
FT                   /note="Hinge"
FT   REGION          154..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   525 AA;  57638 MW;  2DD254E5083707C7 CRC64;
     PTSPLVFVPS SPRLSPFMHP PSHHYLETTS TPVYRSSVSS SQQQLSREDQ CGTSDDSYSV
     GESGAGAGAG AGGFEMAKEM RFCAVCSDYA SGYDYGVWSC EGCKAFFKRS IQGHNDYMCP
     ATNQCTIDRN RRKSCQACRL RKCYQVGMMK GGVRKDRGRV LRRDKRRTGT SDKASKDLEH
     RTAPPQDRRK HSSSSSSAGG GGKSSIIGMS PDQVLLLLQG AEPPVLCSRQ KLSRPYTEVT
     MMTLLTSMAD KELVHMIAWA KKLPGFLQLS LHDQVQLLES SWLEVLMIGL IWRSIHCPGK
     LIFAQDLILD RSEGDCVEGM AEIFDMLLAT TSRFRMLKLK TEEFVCLKAI ILLNSGAFSF
     CTGTMEPLHD GAAVQNMLDT ITDALIHHIS QSGCSAQQQS RRQAHLLLLL SHIRHMSNKG
     MEHLYSMKCK NKVPLYDLLL EMLDAHRIHR PDRPAESWSQ ADREPPYTTS NNNNSSSSSG
     GGDGGPSSAG SGSGPRVNHE SLSRAPTGPG VLQYGGPRSD CTHIL