ID   ERR1_CANLF              Reviewed;         422 AA.
AC   Q6QMY5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Steroid hormone receptor ERR1;
DE   AltName: Full=Estrogen-related receptor alpha;
DE            Short=ERR-alpha;
DE   AltName: Full=Nuclear receptor subfamily 3 group B member 1;
GN   Name=ESRRA; Synonyms=NR3B1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lu P., Colitz C.;
RT   "Dog estrogen related receptor alpha (Estrra) mRNA.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a
CC       single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-
CC       chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and
CC       may act as an important regulator of MCAD promoter. May function as a
CC       modulator of the estrogen signaling pathway in the uterus. Induces the
CC       expression of PERM1 in the skeletal muscle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the AF2
CC       domain) with coactivator PPARGC1A (via the L3 motif); the interaction
CC       greatly enhances transcriptional activity of genes involved in energy
CC       metabolism. Interacts with PIAS4; the interaction enhances sumoylation.
CC       Interacts with MAPK15; promotes re-localization of ESRRA to the
CC       cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA
CC       transcriptional activity. {ECO:0000250|UniProtKB:P11474}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11474,
CC       ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P11474}. Note=Co-localizes to the cytoplasm only
CC       in presence of MAPK15. {ECO:0000250|UniProtKB:P11474}.
CC   -!- PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14
CC       increasing repression of transcriptional activity. {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by
CC       phosphorylation on Ser-19, cofactor activation, and by interaction with
CC       PIAS4. Sumoylation enhances repression of transcriptional activity, but
CC       has no effect on subcellular location nor on DNA binding (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-
CC       138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional
CC       activity probably by inhibiting DNA-binding activity; deacetylation
CC       involves SIRT1 and HDAC8 and increases DNA-binding (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY533243; AAS20260.1; -; mRNA.
DR   RefSeq; NP_001002936.1; NM_001002936.1.
DR   AlphaFoldDB; Q6QMY5; -.
DR   SMR; Q6QMY5; -.
DR   STRING; 9615.ENSCAFP00000021334; -.
DR   PaxDb; 9612-ENSCAFP00000021334; -.
DR   GeneID; 403169; -.
DR   KEGG; cfa:403169; -.
DR   CTD; 2101; -.
DR   eggNOG; KOG3575; Eukaryota.
DR   InParanoid; Q6QMY5; -.
DR   OrthoDB; 5387678at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0034056; F:estrogen response element binding; IBA:GO_Central.
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:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07170; NR_DBD_ERR; 1.
DR   CDD; cd06946; NR_LBD_ERR; 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; 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   PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48092:SF15; STEROID HORMONE RECEPTOR ERR1; 1.
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; 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   Acetylation; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..422
FT                   /note="Steroid hormone receptor ERR1"
FT                   /id="PRO_0000295231"
FT   DOMAIN          192..420
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT   DNA_BIND        76..151
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         79..99
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   ZN_FING         115..134
FT                   /note="NR C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         129
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         138
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         160
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine; by PCAF/KAT2B"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   CROSSLNK        189
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
FT   CROSSLNK        402
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P11474"
SQ   SEQUENCE   422 AA;  45457 MW;  2739152CA0B355F4 CRC64;
     MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH KEEEDGEGAG
     PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE
     CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGSFPAGP
     LAVAGGPRKT APVNALVSHL LVVEPEKLYA MPDPAGPDGH LPAVATLCDL FDREIVVTIS
     WAKSIPGFSS LSLSDQMSVL QSVWMEVLVL GVAQRSLPLQ DELAFAEDLV LDEEGARAAG
     LGELGAVLLQ LVRRLQALRL EREEYVLLKA LALANSDSVH IEDAEAVEQL REALHEALLE
     YEAGRAGPGG GAERRRAGRL LLTLPLLRQT AGKVLAHFYG VKLEGKVPMH KLFLEMLEAM
     MD
//