ESR1_ONCMY
ID ESR1_ONCMY Reviewed; 622 AA.
AC P16058; Q9PSZ8; Q9PSZ9; Q9YGE6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 150.
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 Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2915648; DOI=10.1210/mend-3-1-44;
RA Pakdel F., le Guellec C., Vaillant C., Le Roux M.G., Valotaire Y.;
RT "Identification and estrogen induction of two estrogen receptors (ER)
RT messenger ribonucleic acids in the rainbow trout liver: sequence homology
RT with other ERs.";
RL Mol. Endocrinol. 3:44-51(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=2210031; DOI=10.1016/0303-7207(90)90025-4;
RA Pakdel F., le Gac F., le Goff P., Valotaire Y.;
RT "Full-length sequence and in vitro expression of rainbow trout estrogen
RT receptor cDNA.";
RL Mol. Cell. Endocrinol. 71:195-204(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary;
RX PubMed=10650938; DOI=10.1210/endo.141.2.7296;
RA Pakdel F., Metivier R., Flouriot G., Valotaire Y.;
RT "Two estrogen receptor (ER) isoforms with different estrogen dependencies
RT are generated from the trout ER gene.";
RL Endocrinology 141:571-580(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 270-622.
RX PubMed=10696781; DOI=10.1093/toxsci/53.2.326;
RA Matthews J.B., Zacharewski T.R.;
RT "Differential binding affinities PCBs, HO-PCBs and Aroclors with
RT recombinant human, rainbow trout (Onchorhynkiss mykiss) and green anole
RT (Anolis carolinensis) estrogen receptors using a semi-high throughput
RT competitive binding assay.";
RL Toxicol. Sci. 53:326-339(2000).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ER(L);
CC IsoId=P16058-1; Sequence=Displayed;
CC Name=2; Synonyms=ER(S);
CC IsoId=P16058-2; Sequence=VSP_003683;
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are
CC thought to be weakly associated with nuclear components; hormone
CC binding greatly increases receptor affinity. The hormone-receptor
CC complex appears to recognize discrete DNA sequences upstream of
CC transcriptional start sites.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49552.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M31559; AAA49552.1; ALT_FRAME; mRNA.
DR EMBL; AJ242740; CAB45139.1; -; mRNA.
DR EMBL; AJ242741; CAB45140.1; -; mRNA.
DR EMBL; AF099079; AAD13610.2; -; mRNA.
DR RefSeq; NP_001117821.1; NM_001124349.1. [P16058-1]
DR AlphaFoldDB; P16058; -.
DR SMR; P16058; -.
DR GeneID; 100136026; -.
DR KEGG; omy:100136026; -.
DR CTD; 2099; -.
DR OrthoDB; 487299at2759; -.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005497; F:androgen binding; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IMP:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:1903924; F:estradiol binding; IDA:AgBase.
DR GO; GO:0034056; F:estrogen response element binding; IDA:AgBase.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:AgBase.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:AgBase.
DR GO; GO:1990239; F:steroid hormone binding; IDA:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:AgBase.
DR GO; GO:0046686; P:response to cadmium ion; IMP:AgBase.
DR GO; GO:0032355; P:response to estradiol; IDA:AgBase.
DR GO; GO:0033574; P:response to testosterone; IDA: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; 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 Alternative splicing; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW Receptor; Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..622
FT /note="Estrogen receptor"
FT /id="PRO_0000053631"
FT DOMAIN 324..560
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 193..258
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 193..213
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 229..253
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..192
FT /note="Modulating"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..323
FT /note="Hinge"
FT REGION 275..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10650938,
FT ECO:0000303|PubMed:2210031"
FT /id="VSP_003683"
FT CONFLICT 60..91
FT /note="FNYLDGGYDYTAPAQGPAPLYYSTTPQDAHGP -> LTTWMEGMTTQPLPKA
FT RPLSITPPPPRMPTD (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 289..298
FT /note="YGDLEHRTAP -> TVTWSTGQR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..337
FT /note="AEP -> QT (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="R -> G (in Ref. 1; AAA49552)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="S -> P (in Ref. 1; AAA49552)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="S -> A (in Ref. 1; AAA49552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 68084 MW; AD70DD7136B5A6F3 CRC64;
MLVRQSHTQI SKPLGAPLRS RTTLESHVIS PPKLSPQQPT TPNSNMYPEE TRGGGGAAAF
NYLDGGYDYT APAQGPAPLY YSTTPQDAHG PPSDGSMQSL GSSPTGPLVF VSSSPQLSPQ
LSPFLHPPSH HGLPSQSYYL ETSSTPLYRS SVVTNQLSAS EEKLCIASDR QQSYSAAGSG
VRVFEMANET RYCAVCSDFA SGYHYGVWSC EGCKAFFKRS IQGHNDYMCP ATNQCTMDRN
RRKSCQACRL RKCYEVGMVK GGLRKDRGGR VLRKDKRYCG PAGDREKPYG DLEHRTAPPQ
DGGRNSSSSL NGGGGWRGPR ITMPPEQVLF LLQGAEPPAL CSRQKVARPY TEVTMMTLLT
SMADKELVHM IAWAKKVPGF QELSLHDQVQ LLESSWLEVL MIGLIWRSIH CPGKLIFAQD
LILDRSEGDC VEGMAEIFDM LLATVSRFRM LKLKPEEFVC LKAIILLNSG AFSFCSNSVE
SLHNSSAVES MLDNITDALI HHISHSGASV QQQPRRQAQL LLLLSHIRHM SNKGMEHLYS
IKCKNKVPLY DLLLEMLDGH RLQSPGKVAQ AGEQTEGPST TTTTSTGSSI GPMRGSQDTH
IRSPGSGVLQ YGSPSSDQMP IP
