ID   ERR3_PONAB              Reviewed;         435 AA.
AC   Q5RAM2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Estrogen-related receptor gamma;
DE   AltName: Full=Estrogen receptor-related protein 3;
DE   AltName: Full=Nuclear receptor subfamily 3 group B member 3;
GN   Name=ESRRG; Synonyms=ERR3, NR3B3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Orphan receptor that acts as transcription activator in the
CC       absence of bound ligand. Binds specifically to an estrogen response
CC       element and activates reporter genes controlled by estrogen response
CC       elements. Induces the expression of PERM1 in the skeletal muscle (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with NRIP1, NCOA1 and NCOR2. Binds TLE1,
CC       PNRC1 and PNRC2. Binds GRIP1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000250}.
CC   -!- MISCELLANEOUS: No physiological activating ligand is known for this
CC       orphan receptor, but 4-hydroxytamoxifen and diethylstilbestrol act as
CC       inverse agonists and deactivate ESRRG. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR858993; CAH91188.1; -; mRNA.
DR   RefSeq; NP_001125696.1; NM_001132224.1.
DR   AlphaFoldDB; Q5RAM2; -.
DR   SMR; Q5RAM2; -.
DR   STRING; 9601.ENSPPYP00000000224; -.
DR   GeneID; 100172620; -.
DR   KEGG; pon:100172620; -.
DR   CTD; 2104; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; Q5RAM2; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0003707; F:nuclear steroid receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:InterPro.
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; IPR003078; Retinoic_acid_rcpt.
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; PR01292; RETNOICACIDR.
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; Activator; DNA-binding; Metal-binding; Nucleus; Receptor;
KW   Reference proteome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..435
FT                   /note="Estrogen-related receptor gamma"
FT                   /id="PRO_0000053667"
FT   DOMAIN          210..434
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        102..177
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         105..125
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         141..160
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  48555 MW;  A0F81CDBE3A9C2C7 CRC64;
     MSNKDRHIDS SCSSFIKTEP SSPASLTDSV NHHSPGGSSD ASGSYSSTMN GHQNGLDSPP
     LYPSAPILGG SGPVRKLYDD CSSTIVEDPQ TKCEYMLNSM PKRLCLVCGD IASGYHYGVA
     SCEACKAFFK RTIQGNIEYS CPATNECEIT KRRRKSCQAC RFMKCLKVGM LKEGVRLDRV
     RGGRQKYKRR IDAENSPYLN PQLVQPAKKP YNKIVSHLLV AEPEKIYAMP DPTVPDSDIK
     ALTTLCDLAD RELVVIIGWA KHIPGFSTLS LADQMSLLQS AWMEILILGV VYRSLSFEDE
     LVYADDYIMD EDQSKLAGLL DLNNAILQLV KKYKSMKLEK EEFVTLKAIA LANSDSMHIE
     DVEAVQKLQD VLHEALQDYE AGQHMEDPRR AGKMLMTLPL LRQTSTKAVQ HFYNIKLEGK
     VPMHKLFSEM LEAKV