ESR1_DANRE
ID ESR1_DANRE Reviewed; 569 AA.
AC P57717; Q98SM9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Morimoto J., Miyasho T., Iwano H., Teraoka H., Hiraga T., Yokota H.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Akten B., Kishida M., Callard G.V.;
RT "Estrogen receptor cDNAs in zebrafish.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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; AB037185; BAB16893.1; -; mRNA.
DR EMBL; AF349412; AAK16740.1; -; mRNA.
DR RefSeq; NP_694491.1; NM_152959.1.
DR AlphaFoldDB; P57717; -.
DR SMR; P57717; -.
DR STRING; 7955.ENSDARP00000024987; -.
DR PaxDb; P57717; -.
DR GeneID; 259252; -.
DR KEGG; dre:259252; -.
DR CTD; 2099; -.
DR ZFIN; ZDB-GENE-020806-5; esr1.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; P57717; -.
DR OrthoDB; 487299at2759; -.
DR Reactome; R-DRE-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DRE-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-DRE-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-DRE-5689896; Ovarian tumor domain proteases.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DRE-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-DRE-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-DRE-8939211; ESR-mediated signaling.
DR Reactome; R-DRE-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-DRE-9018519; Estrogen-dependent gene expression.
DR SignaLink; P57717; -.
DR PRO; PR:P57717; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1903924; F:estradiol binding; IDA:ZFIN.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:ZFIN.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:ZFIN.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990239; F:steroid hormone binding; IDA:ZFIN.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071391; P:cellular response to estrogen stimulus; IDA:ZFIN.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048920; P:posterior lateral line neuromast primordium migration; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032355; P:response to estradiol; IDA:ZFIN.
DR GO; GO:0043627; P:response to estrogen; IDA:ZFIN.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:ZFIN.
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; PIRSF500101; ER-a; 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..569
FT /note="Estrogen receptor"
FT /id="PRO_0000053628"
FT DOMAIN 279..515
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 152..217
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 152..172
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 188..212
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..151
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 28..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..278
FT /note="Hinge"
FT REGION 223..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31
FT /note="T -> A (in Ref. 1; BAB16893)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="S -> P (in Ref. 1; BAB16893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62846 MW; CFA0C1AD4376A53C CRC64;
MYPKEEHSAG GISSSVNYLD GAYEYPNPTQ TFGTSSPAEP ASVGYYPAPP DPHEEHLQTL
GGGSSSPLMF APSSPQLSPY LSHHGGHHTT PHQVSYYLDS SSSTVYRSSV VSSQQAAVGL
CEELCSATDR QELYTGSRAA GGFDSGKETR FCAVCSDYAS GYHYGVWSCE GCKAFFKRSI
QGHNDYVCPA TNQCTIDRNR RKSCQACRLR KCYEVGMMKG GIRKDRGGRS VRRERRRSSN
EDRDKSSSDQ CSRAGVRTTG PQDKRKKRSG GVVSTLCMSP DQVLLLLLGA EPPAVCSRQK
HSRPYTEITM MSLLTNMADK ELVHMIAWAK KVPGFQDLSL HDQVQLLESS WLEVLMIGLI
WRSIHSPGKL IFAQDLILDR SEGECVEGMA EIFDMLLATV ARFRSLKLKL EEFVCLKAII
LINSGAFSFC SSPVEPLMDN FMVQCMLDNI TDALIYCISK SGASLQLQSR RQAQLLLLLS
HIRHMSNKGM EHLYRMKCKN RVPLYDLLLE MLDAQRFQSS GKVQRVWSQS EKNPPSTPTT
SSSSSNNSPR GGAAAIQSNG ACHSHSPDP
