ESR1_ASPUN
ID ESR1_ASPUN Reviewed; 307 AA.
AC Q91424;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 109.
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 Aspidoscelis uniparens (Desert grassland whiptail lizard) (Cnemidophorus
OS uniparens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Teiioidea; Teiidae; Aspidoscelis.
OX NCBI_TaxID=37197;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney, and Oviduct;
RX PubMed=7495707; DOI=10.1016/0960-0760(95)00172-v;
RA Young L.J., Godwin J., Grammer M., Gahr M., Crews D.;
RT "Reptilian sex steroid receptors: amplification, sequence and expression
RT analysis.";
RL J. Steroid Biochem. Mol. Biol. 55:261-269(1995).
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; S79923; AAB35739.1; -; mRNA.
DR AlphaFoldDB; Q91424; -.
DR SMR; Q91424; -.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor 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; 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; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
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..307
FT /note="Estrogen receptor"
FT /id="PRO_0000053627"
FT DOMAIN 96..307
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND <1..43
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 7..31
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 44..95
FT /note="Hinge"
FT NON_TER 1
SQ SEQUENCE 307 AA; 35202 MW; D80A1F2FE396AC61 CRC64;
GHNDYMCPAT NQCTIDKNRR KSCQACRLRK CYEVGMMKGG IRKDRRGGRI LKHKRQREEH
DNRNAGAIVE RRSPNLWPSP LMITHNKKNS PALSLTADQI VSALLEAEPP VVYSEYDPSR
PFSEASMMTL LTNLADRELV HMINWAKRVP GFVDLSLHDQ VHLLECAWLE ILMIGLVWRS
VEHPGKLLFA PNLLLDRNQG KCVEGFVEIF DMLLATSSRF RMMNVQGEEF VCLKSIILLN
SGIYTFLSST LKSLEEKDHI HRVLDKIIDT LLHLMAKSGL SLQQQHRRLA QLLLILSHFR
HMSNKGM
