ESR2_SHEEP
ID ESR2_SHEEP Reviewed; 527 AA.
AC Q9TU15; Q9N0T6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Estrogen receptor beta;
DE Short=ER-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 2;
GN Name=ESR2; Synonyms=NR3A2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND BETA-1).
RC TISSUE=Ovary;
RX PubMed=11420232; DOI=10.1095/biolreprod65.1.128;
RA Cardenas H., Burke K.A., Bigsby R.M., Pope W.F., Nephew K.P.;
RT "Estrogen receptor beta in the sheep ovary during the estrous cycle and
RT early pregnancy.";
RL Biol. Reprod. 65:128-134(2001).
CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity
CC similar to that of ESR1/ER-alpha, and activates expression of reporter
CC genes containing estrogen response elements (ERE) in an estrogen-
CC dependent manner. {ECO:0000250|UniProtKB:Q92731}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1.
CC Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a
CC strong increase of transcription of target genes. Interacts with UBE1C
CC and AKAP13. Interacts with DNTTIP2. Interacts with CCDC62 in the
CC presence of estradiol/E2; this interaction seems to enhance the
CC transcription of target genes. Interacts with DNAAF4. Interacts with
CC PRMT2. Interacts with CCAR2 (via N-terminus) in a ligand-independent
CC manner. Interacts with RBM39, in the presence of estradiol (E2).
CC {ECO:0000250|UniProtKB:O08537, ECO:0000250|UniProtKB:Q62986,
CC ECO:0000250|UniProtKB:Q92731}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Beta;
CC IsoId=Q9TU15-1; Sequence=Displayed;
CC Name=Beta-1;
CC IsoId=Q9TU15-2; Sequence=VSP_003700, VSP_003701;
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Phosphorylation at Ser-84 and Ser-102 recruits NCOA1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF177936; AAD55772.1; -; mRNA.
DR EMBL; AF257109; AAF71745.1; -; mRNA.
DR RefSeq; NP_001009737.1; NM_001009737.1. [Q9TU15-1]
DR AlphaFoldDB; Q9TU15; -.
DR SMR; Q9TU15; -.
DR STRING; 9940.ENSOARP00000022731; -.
DR BindingDB; Q9TU15; -.
DR ChEMBL; CHEMBL2304421; -.
DR Ensembl; ENSOART00020022015; ENSOARP00020018230; ENSOARG00020014342.
DR GeneID; 443066; -.
DR KEGG; oas:443066; -.
DR CTD; 2100; -.
DR eggNOG; KOG3575; Eukaryota.
DR OrthoDB; 487299at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0034056; F:estrogen response element binding; IEA:Ensembl.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:InterPro.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR021064; ER-beta-like_N.
DR InterPro; IPR028355; ER-beta/gamma.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
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; PF12497; ERbeta_N; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500102; ER-b; 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 Activator; Alternative splicing; DNA-binding; Lipid-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..527
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053647"
FT DOMAIN 261..495
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 146..211
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 146..166
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 182..206
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..145
FT /note="Modulating"
FT REGION 505..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT MOD_RES 102
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT VAR_SEQ 316..324
FT /note="FVELSLYDQ -> MKGNVLKEF (in isoform Beta-1)"
FT /evidence="ECO:0000303|PubMed:11420232"
FT /id="VSP_003700"
FT VAR_SEQ 325..527
FT /note="Missing (in isoform Beta-1)"
FT /evidence="ECO:0000303|PubMed:11420232"
FT /id="VSP_003701"
SQ SEQUENCE 527 AA; 59120 MW; 9CD7A3E89497EDEA CRC64;
MDVKNSPSSL NSPVSYNCGQ SILPLEPGPI YLPSSYVESR HEYSAVTFYS PAVMNYSIPN
NSEDGPGRQT TSPNVLWPTP GHLSPLAIHC QSSLLYAEPQ KSPWCETRSL EHTFPVNRET
LKRKASGSSC ASPVSSPSSK RDAHFCAVCS DYASGYHYGV WSCEGCKAFF KRSIQGHNDY
ICPATNQCTI DKNRRKSCQA CRLRKCYEVG MVKCGSRRER CGYRIVRRQR NSDEQLHCLS
KTKRNGAPMT RVKELLLSAL SPEQLVLTLL EAEPPHVLMS RPSAPFTEAS MMMSLTKLAD
KELVHMISWA KKIPGFVELS LYDQVRLLES CWLEVLMVGL MWRSIDHPGK LIFAPDLVLD
RDEGKCVEGI LEIFDMLLAT TSRFRELKLQ HKEYLCVKAM ILLNSSMYPS ATASQEADSG
RKLTHLLNAV TDALVWVIAK SGMSSQQQSM RLANLLMLLS HVRHASNKGM EHLLNMKCKN
VVPVYDLLLE MLNAHTLRSN KPLVTRSERN LAEDSESKEG SQKPQAQ
