ERR2_RAT
ID ERR2_RAT Reviewed; 433 AA.
AC P11475; Q5QJB1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Steroid hormone receptor ERR2 {ECO:0000305};
DE AltName: Full=Estrogen receptor-like 2;
DE AltName: Full=Estrogen-related receptor beta {ECO:0000250|UniProtKB:O95718};
DE Short=ERR-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group B member 2;
GN Name=Esrrb {ECO:0000312|RGD:1359557}; Synonyms=Err2, Esrl2, Nr3b2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=3267207; DOI=10.1038/331091a0;
RA Giguere V., Yang N., Segui P., Evans R.M.;
RT "Identification of a new class of steroid hormone receptors.";
RL Nature 331:91-94(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lui K., Chen S., Chan F.L.;
RT "Molecular cloning and expression study of estrogen receptor-related
RT receptor beta in rat prostate.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:3267207 ORIGINATES FROM RAT.
RX PubMed=10072763; DOI=10.1016/s0378-1119(98)00619-2;
RA Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C., Liu Q.,
RA Caskey C.T.;
RT "Identification of two hERR2-related novel nuclear receptors utilizing
RT bioinformatics and inverse PCR.";
RL Gene 228:101-109(1999).
CC -!- FUNCTION: Transcription factor that binds a canonical ESRRB recognition
CC (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of
CC targets genes regulating their expression or their transcription
CC activity (By similarity). Plays a role, in a LIF independent manner, in
CC maintainance of self-renewal and pluripotency of embryonic and
CC trophoblast stem cells through different signaling pathways including
CC FGF signaling pathway and Wnt signaling pathways. Upon FGF signaling
CC pathway activation, interacts with KDM1A by directly binding to
CC enhancer site of ELF5 and EOMES and activating their transcription
CC leading to self-renewal of trophoblast stem cells. Also regulates
CC expression of multiple rod-specific genes and is required for survival
CC of this cell type (By similarity). Plays a role as transcription factor
CC activator of GATA6, NR0B1, POU5F1 and PERM1 (By similarity). Plays a
CC role as transcription factor repressor of NFE2L2 transcriptional
CC activity and ESR1 transcriptional activity (By similarity). During
CC mitosis remains bound to a subset of interphase target genes, including
CC pluripotency regulators, through the canonical ESRRB recognition (ERRE)
CC sequence, leading to their transcriptional activation in early G1
CC phase. Can coassemble on structured DNA elements with other
CC transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger
CC ESRRB-dependent gene activation. This mechanism, in the case of SOX2
CC corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem
CC cells (EpiSC) transition through positive regulation of NR0B1 that
CC inhibits the EpiSC transcriptional program. Also plays a role inner ear
CC development by controlling expression of ion channels and transporters
CC and in early placentation (By similarity).
CC {ECO:0000250|UniProtKB:O95718, ECO:0000250|UniProtKB:Q61539}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with NR0B1;
CC represses ESRRB activity at the GATA6 promoter. Interacts with NANOG;
CC reciprocally modulates their transcriptional activities and activates
CC POU5F1 expression. Interacts with NCOA3; mediates the interaction
CC between ESRRB and RNA polymerase II complexes and allows NCOA3
CC corecruitment to ESRRB, KLF4, NANOG, and SOX2 enhancer regions to
CC trigger ESRRB-dependent gene activation involved in self-renewal and
CC pluripotency. Interacts with KDM1A; co-occupes the core set of ESRRB
CC targets including ELF5 and EOMES. Interacts with the multiprotein
CC complex Integrator, at least composed of INTS1, INTS2, INTS3, INTS4,
CC INTS5, INTS6, INTS7, INTS8, INTS9/RC74, INTS10, INTS11/CPSF3L and
CC INTS12; ESRRB is probably not a core component of the integrator
CC complex and associates to integrator via its interaction with INTS1 and
CC INTS9; attracts the transcriptional machinery. Interacts with JARID2.
CC Interacts with POU5F1; recruits ESRRB near the POU5F1-SOX2 element in
CC the NANOG proximal promoter leading to activation of NANOG expression;
CC the interaction is DNA independent (By similarity).
CC {ECO:0000250|UniProtKB:O95718, ECO:0000250|UniProtKB:Q61539}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61539}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61539}. Chromosome
CC {ECO:0000250|UniProtKB:Q61539}.
CC -!- PTM: Acetylated by PCAF/KAT2 (in vitro).
CC {ECO:0000250|UniProtKB:O95718}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:3267207) thought to originate from
CC human but was later shown (PubMed:10072763) to be derived from rat.
CC {ECO:0000305|PubMed:10072763, ECO:0000305|PubMed:3267207}.
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DR EMBL; X51417; CAA35779.1; -; mRNA.
DR EMBL; AY383731; AAR89824.1; -; mRNA.
DR RefSeq; NP_001008516.2; NM_001008516.2.
DR AlphaFoldDB; P11475; -.
DR BMRB; P11475; -.
DR SMR; P11475; -.
DR STRING; 10116.ENSRNOP00000013867; -.
DR PhosphoSitePlus; P11475; -.
DR PaxDb; P11475; -.
DR GeneID; 299210; -.
DR KEGG; rno:299210; -.
DR UCSC; RGD:1359557; rat.
DR CTD; 2103; -.
DR RGD; 1359557; Esrrb.
DR VEuPathDB; HostDB:ENSRNOG00000010259; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_11_0_1; -.
DR InParanoid; P11475; -.
DR OMA; CPAANDC; -.
DR OrthoDB; 669799at2759; -.
DR PhylomeDB; P11475; -.
DR TreeFam; TF323751; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR PRO; PR:P11475; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000010259; Expressed in stomach and 7 other tissues.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0032039; C:integrator complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043697; P:cell dedifferentiation; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IDA:BHF-UCL.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:2000035; P:regulation of stem cell division; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0017145; P:stem cell division; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0001834; P:trophectodermal cell proliferation; ISO:RGD.
DR GO; GO:0001831; P:trophectodermal cellular morphogenesis; ISO:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
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; IPR027289; Oest-rel_rcp.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PIRSF; PIRSF500939; ERR1-2-3; 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 Acetylation; Chromosome; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Receptor; Reference proteome; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..433
FT /note="Steroid hormone receptor ERR2"
FT /id="PRO_0000053664"
FT DOMAIN 208..432
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 100..186
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 103..123
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..163
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..211
FT /note="Interaction with NANOG"
FT /evidence="ECO:0000250|UniProtKB:Q61539"
FT REGION 203..433
FT /note="Essential for ESRRB transcriptional activity and
FT interaction with NCOA3"
FT /evidence="ECO:0000250|UniProtKB:Q61539"
FT SITE 185
FT /note="Important for stabilizing DNA-binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 48288 MW; EE2C4C5B2F9A3E13 CRC64;
MSSEDRHLGS SCGSFIKTEP SSPSSGIDAL SHHSPSGSSD ASGGFGMALG THANGLDSPP
MFAGAGLGGN PCRKSYEDCT SGIMEDSAIK CEYMLNAIPK RLCLVCGDIA SGYHYGVASC
EACKAFFKRT IQGNIEYSCP ATNECEITKR RRKSCQACRF MKCLKVGMLK EGVRLDRVRG
GRQKYKRRLD SENSPYLSLQ ISPPAKKPLT KIVSYLLVAE PDKLYAMPPD DVPEGDIKAL
TTLCDLADRE LVFLISWAKH IPGFSNLTLG DQMSLLQSAW MEILILGIVY RSLPYDDKLA
YAEDYIMDEE HSRLVGLLEL YRAILQLVRR YKKLKVEKEE FVMLKALALA NSDSMYIENL
EAVQKLQDLL HEALQDYELS QRHEEPRRAG KLLLTLPLLR QTAAKAVQHF YSVKLQGKVP
MHKLFLEMLE AKV
