TOG1_YEAST
ID TOG1_YEAST Reviewed; 794 AA.
AC P39961; D3DM93;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription factor TOG1 {ECO:0000303|PubMed:24998441};
DE AltName: Full=Transcriptional regulator of oleate 1 {ECO:0000303|PubMed:24998441};
GN Name=TOG1 {ECO:0000303|PubMed:24998441}; OrderedLocusNames=YER184C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11353088; DOI=10.1093/nar/29.10.2181;
RA Akache B., Wu K., Turcotte B.;
RT "Phenotypic analysis of genes encoding yeast zinc cluster proteins.";
RL Nucleic Acids Res. 29:2181-2190(2001).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=24998441; DOI=10.1016/j.bbrc.2014.06.128;
RA Thepnok P., Ratanakhanokchai K., Soontorngun N.;
RT "The novel zinc cluster regulator Tog1 plays important roles in oleate
RT utilization and oxidative stress response in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 450:1276-1282(2014).
CC -!- FUNCTION: Transcriptional activator required for growth on non-
CC fermentable carbon sources and that regulates genes involved in fatty
CC acid utilization (PubMed:11353088, PubMed:24998441). Acts as a direct
CC activator that binds the promoters of oleate utilizing genes, encoded
CC key enzymes in beta-oxidation and NADPH regeneration (POX1, FOX2,POT1
CC and IDP2), the glyoxylate shunt (MLS1 and ICL1), and gluconeogenesis
CC (PCK1 and FBP1) (PubMed:24998441). Regulates also the abundance of
CC peroxisomes that are vital for fatty acid oxidation (PubMed:24998441).
CC {ECO:0000269|PubMed:11353088, ECO:0000269|PubMed:24998441}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24998441}.
CC -!- DISRUPTION PHENOTYPE: Confers sensitivity to calcofluor white, and
CC prevents growth on non-fermentable carbon sources such as glycerol or
CC lactate (PubMed:11353088, PubMed:24998441). Sensitizes cells to
CC oxidative stress (PubMed:24998441). Leads to a decrease in peroxisome
CC abundance when oleate was used as a sole carbon source
CC (PubMed:24998441). {ECO:0000269|PubMed:11353088,
CC ECO:0000269|PubMed:24998441}.
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DR EMBL; U18922; AAB64711.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07847.1; -; Genomic_DNA.
DR PIR; S50687; S50687.
DR RefSeq; NP_011111.1; NM_001179074.1.
DR AlphaFoldDB; P39961; -.
DR BioGRID; 36938; 22.
DR DIP; DIP-5488N; -.
DR IntAct; P39961; 3.
DR MINT; P39961; -.
DR STRING; 4932.YER184C; -.
DR MaxQB; P39961; -.
DR PaxDb; P39961; -.
DR PRIDE; P39961; -.
DR EnsemblFungi; YER184C_mRNA; YER184C; YER184C.
DR GeneID; 856933; -.
DR KEGG; sce:YER184C; -.
DR SGD; S000000986; TOG1.
DR VEuPathDB; FungiDB:YER184C; -.
DR eggNOG; ENOG502RYRF; Eukaryota.
DR GeneTree; ENSGT00940000176364; -.
DR HOGENOM; CLU_023197_0_0_1; -.
DR InParanoid; P39961; -.
DR OMA; GLNRWEY; -.
DR BioCyc; YEAST:G3O-30340-MON; -.
DR PRO; PR:P39961; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39961; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IC:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..794
FT /note="Transcription factor TOG1"
FT /id="PRO_0000114995"
FT DNA_BIND 18..44
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 794 AA; 91077 MW; 7A0CBBBB342AA203 CRC64;
MAAKRGLAKQ KSRVTKACDR CHRKKIKCNS KKPCFGCIGS QSKCTYRNQF REPIEAFFNY
TGSLSNDLDN AKCSIAKLKA QLPPSAPASL QKGLANICTE LEKIQPQLYL NLDSKEISSY
GGLKSIETEI IGKQSKSLNR FSNAFESNTA QNVSMYFGVY SPLLYFASTG ISWITKKLIS
CSNDRETRET IYLFLKFLDA SSASHAGPKV TSISPLEYYS KLNGLSCGND VLIQHIMSNI
SNEIKGNTNI NQTIKFNKPT DWFMYGVQLM EQHHKALDRK SSKKLLPLKY FLEQDELIFC
LCLEYFERSL FSTMYDLTIL KGLVSLMKHR YWIDDPFVLG RIISTMSRRS LDAGLNRWEY
YIGQDEDTAE EYRKLWWDCY WWDRWYSLVT GKQPLIPHEM TSCLFPKDVV GLGVDDSMDC
FTLINLVELD PSKFDICISF GYILLTKIIT AVFSGLLYNR HFTDYRLFAT PNAKDLNGTA
RQLMVEFSKI CKIFQCIQDK LIPFLKQYSE NSNVFELYTH FGFAKVCCFQ GMESLILRIQ
NLLQERERIE LDSCVKDIRL QTFEASVDIL TDVLKHEDTF YIFRCSWFIY AILMNITLNF
IETPRRNSIC YLSLMCRMIA SYNDLFVSSG NVNFKGNNAF SKKLENGTAV SFILTRICCQ
MYTRSQKMAK ESLFCELKKY GQACSDAGQA ALDIECIWYR NIIGEHKESS FRKEILSILD
REMGDLVNNR VIGVQGKNQE GACYEKLSPS STSVSVGMDF CSLENFVTAE SLPDLLNLFW
EDTEFGITKE NLGE
