ID   ESR1_XENLA              Reviewed;         586 AA.
AC   P81559;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
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;
GN   Name=esr1; Synonyms=esr, nr3a1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3274894; DOI=10.1210/mend-1-5-355;
RA   Weiler I.J., Lew D., Shapiro D.J.;
RT   "The Xenopus laevis estrogen receptor: sequence homology with human and
RT   avian receptors and identification of multiple estrogen receptor messenger
RT   ribonucleic acids.";
RL   Mol. Endocrinol. 1:355-362(1987).
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   -!- 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; L20735; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; A40907; QRXLE.
DR   AlphaFoldDB; P81559; -.
DR   SMR; P81559; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF12743; ESR1_C; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF02159; Oest_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PIRSF; PIRSF500101; ER-a; 1.
DR   PIRSF; PIRSF002527; ER-like_NR; 1.
DR   PRINTS; PR00543; OESTROGENR.
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..586
FT                   /note="Estrogen receptor"
FT                   /id="PRO_0000053639"
FT   DOMAIN          303..539
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        180..245
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         180..200
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         216..240
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..179
FT                   /note="Modulating"
FT   REGION          144..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..302
FT                   /note="Hinge"
FT   REGION          252..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..569
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   586 AA;  66081 MW;  0EDC77EB0D6F08BF CRC64;
     MTMPLPNKTT GVTFLHQIQS SELETLTRPP LKISLERPLG EMYVENNRTG IFNYPEGTTY
     DFAAAAAPVY SSASLSYAAS SETFGSSSLT GLHTLNNVPP SPVVFLAKLP QLSPFIHHHG
     QQVPYYLESE QGTFAVREAA PPTFYRSSSD NRRQSGRERM SSANDKGPPS MESTKETRYC
     AVCSDYASGY HYGVWSCEGC KAFFKRSIQG HNDYMCPATN QCTIDKNRRK SCQACRLRKC
     YEVGMMKGGI RKDRRGGRLL KHKRQKEEQE QKNDVDPSEI RTASIWVNPS VKSMKLSPVL
     SLTAEQLISA LMEAEAPIVY SEHDSTKPLS EASMMTLLTN LADRELVHMI NWAKRVPGFV
     DLTLHDQVHL LECAWLEILM VGLIWRSVEH PGKLSFAPNL LLDRNQGRCV EGLVEIFDML
     VTTATRFRMM RLRGEEFICL KSIILLNSGV YTFLSSTLES LEDTDLIHII LDKIIDTLVH
     FMAKSGLSLQ QQQRRLAQLL LILSHIRHMS NKGMEHLYSM KCKNVVPLYD LLLEMLDAHR
     IHTPKDKTTT QEEDSRSPPT TTVNGASPCL QPYYTNTEEV SLQSTV