ESR2_CALJA
ID ESR2_CALJA Reviewed; 530 AA.
AC Q95171;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Gaughan J., Scobie G.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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.
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 -!- 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-87 and Ser-105 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; Y09372; CAA70546.2; -; mRNA.
DR AlphaFoldDB; Q95171; -.
DR SMR; Q95171; -.
DR STRING; 9483.ENSCJAP00000036235; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q95171; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IEA:InterPro.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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: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; DNA-binding; Glycoprotein; Lipid-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Steroid-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..530
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053641"
FT DOMAIN 264..498
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 149..214
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..169
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 185..209
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..148
FT /note="Modulating"
FT REGION 507..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT MOD_RES 87
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT MOD_RES 105
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT CARBOHYD 61
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 530 AA; 59088 MW; 45D89107A84C53D1 CRC64;
MDIKNSPSSL NSPSSYNFGQ SILPLEHGPI YIPSSYVESH HEYPAMTFYS PAVMNYSIPS
SVTNLEEGPG RQITSPNMLW STPGHLSPLA VHHQLSHLYA EPQKSPWCEA RSLEHTLPVS
RETLKRKVSG NHCASPVTGP SSKRDAHFCA VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRLVR RQGNAEEQLH
CAGKAKRSGG HVPRVRELLL SALSPEQLVL TLLEAEPPHV LISRPSVPFT EASMMMSLTK
LADEELVHMI SWAKKIPGFV ELSLLDQVRL LESCWLEVLM VGLMWRSIDH PGKLIFAPNL
ILDRDEGKCV EGILEVFDML LATTSRFREL KLQHKEYLCV KAMVLLNSQY DPLVTATQDA
ESSQKLAHLL NAVTDALVWV IAKSGFSSQQ QSVRLANLLM LLSHIRHASN KGMEHLLSMK
CKNVVPVYDL LLEMMNAHVV RGCKSSITGS ECSPAEDSKS TEGSQNPQSP
