ESR1_ORENI
ID ESR1_ORENI Reviewed; 585 AA.
AC Q9YH33;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chang X.T., Kobayashi T., Todo T., Yoshiura Y., Ikeuchi T., Kajiura H.,
RA Nakamura M., Nagahama Y.;
RT "cDNA sequence of Tilapia type alpha estrogen receptor.";
RL Submitted (OCT-1996) 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; U75604; AAD00245.1; -; mRNA.
DR RefSeq; NP_001266699.1; NM_001279770.1.
DR AlphaFoldDB; Q9YH33; -.
DR SMR; Q9YH33; -.
DR STRING; 8128.ENSONIP00000016788; -.
DR GeneID; 100534514; -.
DR KEGG; onl:100534514; -.
DR CTD; 2099; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_11_1_1; -.
DR InParanoid; Q9YH33; -.
DR OrthoDB; 487299at2759; -.
DR Proteomes; UP000005207; Unplaced.
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; 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..585
FT /note="Estrogen receptor"
FT /id="PRO_0000053633"
FT DOMAIN 267..503
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 139..204
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..159
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 175..199
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..138
FT /note="Modulating"
FT /evidence="ECO:0000250"
FT REGION 205..266
FT /note="Hinge"
FT REGION 210..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 64166 MW; 36A96BCB668707B0 CRC64;
MYPEESRGSG GVATVDFLEG TYDYAAPTPA PTPLYSHSTT GCYSAPLDAH GPLSDGSLQS
LGSGPTSPLV FVPSSPRLSP FMHPPSHHYL ETTSTPVYRS SHQPVPREDQ CGTRDEAYSV
GELGAGAGGF EMTKDTRFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH NDYMCPATNQ
CTIDKNRRKS CQACRLRKCY EVGMMKGGMR KDRGRVLRRE KRRACDRDKP AKDLPHTRAS
PQDGRKRAMS SSSTSGGGGR SSLNNMPPDQ VLLLLQGAEP PILSSRQKMS RPYTEVTIMT
LLTSMADKEL VHMITWAKKL PGFLQLSLHD QVLLLESSWL EVLMIGLIWR SIQCPGKLIF
AQDLILDRNE GTCVEGMAEI FDMLLATASR FRVLKLKPEE FVCLKAIILL NSGAFSFCTG
TMEPLHDSAA VQHMLDTITD ALIFHISHLG CSAQQQSRRQ AQLLLLLSHI RHMSNKGMEH
LYSMKCKNKV PLYDLLLEML DAHRIHRPVK PFQSWSQGDR DSPTASSTSS SGGGGGDDEG
ASSAGSSSGP QGSHESPRRE NLSRAPTGPG VLQYRGSHSD CTRIP
