ID ESR2_BOVIN Reviewed; 527 AA.
AC Q9XSB5; Q9TTS2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 184.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Holstein; TISSUE=Ovarian follicle;
RX PubMed=10026117; DOI=10.1095/biolreprod60.3.691;
RA Rosenfeld C.S., Yuan X., Manikkam M., Calder M.D., Garverick H.A.,
RA Lubahn D.B.;
RT "Cloning, sequencing, and localization of bovine estrogen receptor-beta
RT within the ovarian follicle.";
RL Biol. Reprod. 60:691-697(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-527.
RX PubMed=10432221; DOI=10.1016/s0303-7207(99)00064-7;
RA Walther N., Lioutas C., Tillmann G., Ivell R.;
RT "Cloning of bovine estrogen receptor beta (Erbeta): expression of novel
RT deleted isoforms in reproductive tissues.";
RL Mol. Cell. Endocrinol. 152:37-45(1999).
CC -!- FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity
CC similar to that of ESR1ESR1/ER-alpha, and activates expression of
CC reporter genes containing estrogen response elements (ERE) in an
CC estrogen-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 Interacts with STUB1/CHIP (By similarity).
CC {ECO:0000250|UniProtKB:O08537, ECO:0000250|UniProtKB:Q62986,
CC ECO:0000250|UniProtKB:Q92731}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
CC -!- TISSUE SPECIFICITY: Present in granulosa cells of antral follicles in
CC various stages of follicular growth. {ECO:0000269|PubMed:10026117}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53861.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF110402; AAD24432.1; -; mRNA.
DR EMBL; Y18017; CAB53861.1; ALT_INIT; mRNA.
DR RefSeq; NP_776476.2; NM_174051.3.
DR RefSeq; XP_010807738.1; XM_010809436.2.
DR AlphaFoldDB; Q9XSB5; -.
DR SMR; Q9XSB5; -.
DR STRING; 9913.ENSBTAP00000005899; -.
DR ChEMBL; CHEMBL2404; -.
DR PaxDb; 9913-ENSBTAP00000005899; -.
DR Ensembl; ENSBTAT00000005899.5; ENSBTAP00000005899.4; ENSBTAG00000004498.5.
DR GeneID; 281146; -.
DR KEGG; bta:281146; -.
DR CTD; 2100; -.
DR VEuPathDB; HostDB:ENSBTAG00000004498; -.
DR VGNC; VGNC:28605; ESR2.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156116; -.
DR HOGENOM; CLU_007368_11_1_1; -.
DR InParanoid; Q9XSB5; -.
DR OMA; HRNSEDQ; -.
DR OrthoDB; 5387678at2759; -.
DR TreeFam; TF323751; -.
DR Reactome; R-BTA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-BTA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-BTA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-BTA-8939211; ESR-mediated signaling.
DR Reactome; R-BTA-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:Q9XSB5; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000004498; Expressed in oviduct epithelium and 37 other cell types or tissues.
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; IBA:GO_Central.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
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:0071391; P:cellular response to estrogen stimulus; IBA:GO_Central.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07171; NR_DBD_ER; 1.
DR CDD; cd06949; NR_LBD_ER; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 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 PANTHER; PTHR48092:SF12; ESTROGEN RECEPTOR BETA; 1.
DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW 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_0000053640"
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 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 CONFLICT 60
FT /note="N -> D (in Ref. 2; CAB53861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 59032 MW; 9CEFFE106F4E4C84 CRC64;
MDVKNSPSSL NSPVSYNCGQ SILPLEPGPI YLPSSYVESR HEYSAVTFYS PAVMNYSIPN
NSEDGPGRQT TSPNVLWPTP GHLSPLAIHC QPSVLYAEPQ KSPWRETRSL EHTLPVNRET
LKRKASGSSC ASPATSPSSK RDAHFCAVCS DYASGYHYGV WSCEGCKAFF KRSIQGHNDY
ICPATNQCTI DKNRRKSCQA CRLRKCYEVG MVKCGSRRER CGYRIVRRQR NSDEQLHCLS
KTKRNGGPMT RVKELLLSAL SPEQLVLTLL EAEPPHVLIS RPSTPFTEAS MMMSLTKLAD
KELVHMISWA KKIPGFVELS LYDQVRLLES CWLEVLMVGL MWRSIDHPGK LIFAPDLILD
RDEGKCVEGI LEIFDMLLAT TSRFRELKLQ HKEYLCVKAM ILLNSSMYPS ATAPQEADSG
RKLTHLLNAV TDALVWVIAK SGMSSQQQSM RLANLLMLLS HVRHASNKGM EHLLNMKCKN
VVPVYDLLLE MLNAHTLRGN KSLVTGSERN LVEDSESKEG SQKPQAQ
//
