ERR1_CANLF
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 03-AUG-2022, entry version 113.
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; Q6QMY5; -.
DR GeneID; 403169; -.
DR KEGG; cfa:403169; -.
DR CTD; 2101; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q6QMY5; -.
DR OrthoDB; 669799at2759; -.
DR Proteomes; UP000002254; 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: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; IBA:GO_Central.
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: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 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; 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
