ESR1_ANOCA
ID ESR1_ANOCA Reviewed; 349 AA.
AC Q9YHT3;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 25-MAY-2022, entry version 114.
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=NR3A1;
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Matthews J.B., Wade J., Zacharewski T.R.;
RT "Cloning of the reptilian Anolis carolinensis estrogen receptor ligand
RT binding domain.";
RL Submitted (JUL-1999) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF095911; AAC64412.2; -; mRNA.
DR AlphaFoldDB; Q9YHT3; -.
DR SMR; Q9YHT3; -.
DR STRING; 28377.ENSACAP00000006106; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q9YHT3; -.
DR Proteomes; UP000001646; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR024736; Oestrogen-typ_rcpt_final_C_dom.
DR Pfam; PF12743; ESR1_C; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR SMART; SM00430; HOLI; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 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..349
FT /note="Estrogen receptor"
FT /id="PRO_0000053626"
FT DOMAIN 65..301
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND <1..5
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 349 AA; 39560 MW; 453E9BE12B866384 CRC64;
YEVGMMKGGI RKDRRGGRML KHKRQREEND SRNAGALTEA RSTALWPSPL MIKHSKKNSP
ALSLTADQMV SALLEAEPPV VYSEYDPSRP FNEASVMTLL TNLADRELVH MINWAKRVPG
FVDLALHDQV HLLECAWLEI LMVGLVWRSM EHPGKLLFAP NLLLDRSHGK VVEGFVEIFD
MLLAASSRFR MMNVRGEEFV CLKSIILLNP GIYTYLSSTL KSVEERDHIH RVLDKITDTL
MHLMAKSGLS LQQQHRRLAQ LLLILSHIRH MSNKGMEHLY SMKCKNVVPL YDLLLEMLDA
HRLHAPAAKG SPPSEDDPLN QLAVPSPSMH SLLPCYVNKQ EEGNEQEAI