ESR1_TAEGU
ID ESR1_TAEGU Reviewed; 587 AA.
AC Q91250;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
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 Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus;
RX PubMed=9010328; DOI=10.1016/s0960-0760(96)00096-9;
RA Jacobs E.C., Arnold A.P., Campagnoni A.T.;
RT "Zebra finch estrogen receptor cDNA: cloning and mRNA expression.";
RL J. Steroid Biochem. Mol. Biol. 59:135-145(1996).
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. The
CC modulating domain, also known as A/B or AF-1 domain has a ligand-
CC independent transactivation function. The C-terminus contains a ligand-
CC dependent transactivation domain, also known as E/F or AF-2 domain
CC which overlaps with the ligand binding domain. AF-1 and AF-2 activate
CC transcription independently and synergistically and act in a
CC promoter- and cell-specific manner (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; L79911; AAB81108.1; -; mRNA.
DR RefSeq; NP_001070169.1; NM_001076701.1.
DR AlphaFoldDB; Q91250; -.
DR SMR; Q91250; -.
DR STRING; 59729.ENSTGUP00000011604; -.
DR GeneID; 751998; -.
DR KEGG; tgu:751998; -.
DR CTD; 2099; -.
DR InParanoid; Q91250; -.
DR OrthoDB; 487299at2759; -.
DR Proteomes; UP000007754; Unplaced.
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; ISS:AgBase.
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 GO; GO:0055001; P:muscle cell development; IMP:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
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..587
FT /note="Estrogen receptor"
FT /id="PRO_0000053636"
FT DOMAIN 303..539
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 177..242
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 177..197
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 213..237
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..176
FT /note="Modulating (transactivation AF-1)"
FT REGION 243..302
FT /note="Hinge"
FT REGION 248..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..587
FT /note="Transactivation AF-2"
FT /evidence="ECO:0000250"
FT COMPBIAS 248..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 66553 MW; 2B254168A7A910AB CRC64;
MTLHTKTSGV TLLHQIQGTE LETLSRPQLK IPLERSLSDM YVETNKTGVF NYPEGATYDF
GTTAPVYSST TLSYAPTSES FGSSSLAGFH SLNSVPPSPV VFLQTAPHWS PFIHHHSQQV
PYYLENDQGS FGMREAAPPA FYRPNSDNRR HSIRERMSSA NEKGSLSMES TKETRYCAVC
NDYASGYHYG VWSCEGCKAF FKRSIQGHND YMCPATNQCT IDKNRRKSCQ ACRLRKCYEV
GMMKGGIRKD RRGGRVMKQK RQREEQDSRN GEASSTELRA PTLWASPLVV KHNKKNSPAL
SLTAEQMVSA LLEAEPPLVY SEYDPNRPFN EASMMTLLTN LADRELVHMI NWAKRVPGFV
DLTLHDQVHL LECAWLEILM IGLVWRSMEH PGKLLFAPNL LLDRNQGKCV EGMVEIFDML
LATAARFRMM NLQGEEFVCL KSIILLNSGV YTFLSSTLKS LEEKDYIHRV LDKITDTLIH
LMAKSGLSLQ QQHRRLAQLL LILSHIRHMS NKGMEHLYNM KCKNVVPLYD LLLEMLDAHR
LHAPAARSAA PMEEENRSQL TTASASSHSL QSFYINSKEE ENMQNTL
