ERT1_YEAST
ID ERT1_YEAST Reviewed; 529 AA.
AC P38140; D6VQN5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcription activator of gluconeogenesis ERT1;
DE AltName: Full=Ethanol regulator of translation 1;
GN Name=ERT1; OrderedLocusNames=YBR239C; ORFNames=YBR1622;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18419300; DOI=10.1101/sqb.2007.72.040;
RA Klevecz R.R., Li C.M.;
RT "Evolution of the clock from yeast to man by period-doubling folds in the
RT cellular oscillator.";
RL Cold Spring Harb. Symp. Quant. Biol. 72:421-429(2007).
RN [6]
RP FUNCTION.
RX PubMed=18202368; DOI=10.1534/genetics.107.082602;
RA Nyswaner K.M., Checkley M.A., Yi M., Stephens R.M., Garfinkel D.J.;
RT "Chromatin-associated genes protect the yeast genome from Ty1 insertional
RT mutagenesis.";
RL Genetics 178:197-214(2008).
RN [7]
RP FUNCTION.
RX PubMed=19686338; DOI=10.1111/j.1567-1364.2009.00555.x;
RA Turcotte B., Liang X.B., Robert F., Soontorngun N.;
RT "Transcriptional regulation of nonfermentable carbon utilization in budding
RT yeast.";
RL FEMS Yeast Res. 10:2-13(2010).
CC -!- FUNCTION: Transcription factor which regulates nonfermentable carbon
CC utilization. Activator of gluconeogenetic genes like PCK1. Involved in
CC restriction of Ty1 transposition. {ECO:0000269|PubMed:18202368,
CC ECO:0000269|PubMed:19686338}.
CC -!- INTERACTION:
CC P38140; P43603: LSB3; NbExp=3; IntAct=EBI-21048, EBI-22980;
CC P38140; P39743: RVS167; NbExp=4; IntAct=EBI-21048, EBI-14500;
CC P38140; P32793: YSC84; NbExp=4; IntAct=EBI-21048, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Increases the periodicity of transcriptional and
CC metabolic oscillation. {ECO:0000269|PubMed:18419300}.
CC -!- MISCELLANEOUS: Present with 85 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ERT1/acuK family. {ECO:0000305}.
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DR EMBL; Z36108; CAA85202.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07355.1; -; Genomic_DNA.
DR PIR; S46116; S46116.
DR RefSeq; NP_009798.3; NM_001178587.3.
DR AlphaFoldDB; P38140; -.
DR SMR; P38140; -.
DR BioGRID; 32934; 77.
DR DIP; DIP-4432N; -.
DR IntAct; P38140; 7.
DR MINT; P38140; -.
DR STRING; 4932.YBR239C; -.
DR iPTMnet; P38140; -.
DR MaxQB; P38140; -.
DR PaxDb; P38140; -.
DR PRIDE; P38140; -.
DR EnsemblFungi; YBR239C_mRNA; YBR239C; YBR239C.
DR GeneID; 852541; -.
DR KEGG; sce:YBR239C; -.
DR SGD; S000000443; ERT1.
DR VEuPathDB; FungiDB:YBR239C; -.
DR eggNOG; ENOG502R1M5; Eukaryota.
DR GeneTree; ENSGT00940000176385; -.
DR HOGENOM; CLU_010748_2_3_1; -.
DR InParanoid; P38140; -.
DR OMA; VMTTCKL; -.
DR BioCyc; YEAST:G3O-29170-MON; -.
DR PRO; PR:P38140; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38140; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061415; P:negative regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0061414; P:positive regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IGI:SGD.
DR CDD; cd00067; GAL4; 1.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Gluconeogenesis; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..529
FT /note="Transcription activator of gluconeogenesis ERT1"
FT /id="PRO_0000114993"
FT DOMAIN 408..480
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DNA_BIND 40..68
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 60311 MW; 6C89B70CBCCA93D8 CRC64;
MCTPDENDYK TSTDPDTSAN TNHTLEKKKR KKRKNTNVAC VNCSRLHVSC EAKRPCLRCI
SKGLTATCVD APRKKSKYLA GIPNRELPMN IQPDLPPRKI MIPIYNNSSN SSLNVNNMGE
QQKFTSPQHI VHKAKFLSNA ADSEYSILSN IIYQDTLSNK IPIDILYSNT NSTSNSTIGN
SSNNSPTGTN TSPEETEMEK IRQLYSEQRA NIPPHPYPSS NQNVYSILLG PNSAKIVASQ
VNLFANHFPL VPVDSADNSL NFKRLLPRDP SEKSSQINWD SSINQYYLNS ETVTFPELAI
PLKRRKNHLV SVSLESCSPD AANIKSNVEW EHSLRYSTPM EIYTSINAPF SHTPGFHHLL
VYLKHRFNQQ DLVKMCRSIA EFRPIFIACS VTLTEEDMIF MEQCYQRTLL EYVKFIAQIG
TPTCIWRRNG QISYVNEEFE ILCGWTREEL LNKMTFIVEI MDDESVRDYF KTLSKVAYRD
FRGSEKMKVC RLLSPIKGKI IHCCCMWTLK RDVSGLPLMI LGNFMPILN
