ID CAT8_YEAST Reviewed; 1433 AA. AC P39113; D6W0A7; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 176. DE RecName: Full=Regulatory protein CAT8; GN Name=CAT8; Synonyms=MSP8; OrderedLocusNames=YMR280C; GN ORFNames=YM8021.06C; 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 [GENOMIC DNA]. RX PubMed=7891685; DOI=10.1128/mcb.15.4.1915; RA Hedges D., Proft M., Entian K.-D.; RT "CAT8, a new zinc cluster-encoding gene necessary for derepression of RT gluconeogenic enzymes in the yeast Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 15:1915-1922(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ENY.WA-1A; RA Boles E., Hettmann C., Zimmermann F.K.; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Activator of the gluconeogenic enzymes FBP1 and PCK1 genes. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- PTM: Could be the target of the SNF1/CAT1 - SNF4/CAT3 kinase complex. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X78344; CAA55139.1; -; Genomic_DNA. DR EMBL; Z49704; CAA89778.1; -; Genomic_DNA. DR EMBL; X94215; CAA63906.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10181.1; -; Genomic_DNA. DR PIR; S54587; S54587. DR RefSeq; NP_014007.1; NM_001182787.1. DR AlphaFoldDB; P39113; -. DR SMR; P39113; -. DR BioGRID; 35459; 111. DR DIP; DIP-4397N; -. DR MINT; P39113; -. DR STRING; 4932.YMR280C; -. DR GlyGen; P39113; 20 sites, 1 O-linked glycan (20 sites). DR iPTMnet; P39113; -. DR MaxQB; P39113; -. DR PaxDb; 4932-YMR280C; -. DR PeptideAtlas; P39113; -. DR EnsemblFungi; YMR280C_mRNA; YMR280C; YMR280C. DR GeneID; 855323; -. DR KEGG; sce:YMR280C; -. DR AGR; SGD:S000004893; -. DR SGD; S000004893; CAT8. DR VEuPathDB; FungiDB:YMR280C; -. DR eggNOG; ENOG502QTKQ; Eukaryota. DR HOGENOM; CLU_004300_1_0_1; -. DR InParanoid; P39113; -. DR OMA; FLAKCMI; -. DR OrthoDB; 1701898at2759; -. DR BioCyc; YEAST:G3O-32951-MONOMER; -. DR BioGRID-ORCS; 855323; 3 hits in 13 CRISPR screens. DR PRO; PR:P39113; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P39113; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0061414; P:positive regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IMP:SGD. DR CDD; cd12148; fungal_TF_MHR; 1. DR CDD; cd00067; GAL4; 1. DR CDD; cd15485; ZIP_Cat8; 1. DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1. DR InterPro; IPR007219; Transcription_factor_dom_fun. DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf. DR InterPro; IPR001138; Zn2Cys6_DnaBD. DR PANTHER; PTHR46910:SF12; REGULATORY PROTEIN CAT8; 1. DR PANTHER; PTHR46910; TRANSCRIPTION FACTOR PDR1; 1. 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; Zn2/Cys6 DNA-binding domain; 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; Carbohydrate metabolism; DNA-binding; Metal-binding; Nucleus; KW Reference proteome; Transcription; Transcription regulation; Zinc. FT CHAIN 1..1433 FT /note="Regulatory protein CAT8" FT /id="PRO_0000114940" FT DNA_BIND 70..97 FT /note="Zn(2)-C6 fungal-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227" FT REGION 20..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 936..1024 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1137..1162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1200..1236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1324..1433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..40 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 936..950 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 951..965 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 966..991 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 992..1009 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1324..1394 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1407..1433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 303 FT /note="S -> A (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 747 FT /note="K -> L (in Ref. 1; CAA55139)" FT /evidence="ECO:0000305" FT CONFLICT 768 FT /note="T -> A (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 999..1002 FT /note="Missing (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1008 FT /note="G -> S (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1016 FT /note="H -> Q (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1019 FT /note="Q -> P (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1061 FT /note="V -> M (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1072..1074 FT /note="TDA -> ADS (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1092 FT /note="N -> S (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1100 FT /note="I -> V (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1120 FT /note="M -> L (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" FT CONFLICT 1162 FT /note="S -> A (in Ref. 4; CAA63906)" FT /evidence="ECO:0000305" SQ SEQUENCE 1433 AA; 160485 MW; 5ED790BEFB47B632 CRC64; MANNNSDRQG LEPRVIRTLG SQALSGPSIS NRTSSSEANP HFSKNVKEAM IKTASPTPLS TPIYRIAQAC DRCRSKKTRC DGKRPQCSQC AAVGFECRIS DKLLRKAYPK GYTESLEERV RELEAENKRL LALCDIKEQQ ISLVSQSRPQ TSTDNTINGN FKHDLKDAPL NLSSTNIYLL NQTVNKQLQN GKMDGDNSGS AMSPLGAPPP PPHKDHLCDG VSCTNHLHVK PTSTSLNDPT AISFEQDEAP GLPAVKALKS MTTHQRSTQL ATLVSLSIPR STEEILFIPQ LLTRIRQIFG FNSKQCLYTV SLLSSLKNRL PAPRLLAPST STKLKEKDED KKLDDDSAFV KRFQSTNLSE FVDLKKFLIS LKFNINSFSK QSEKPANDQD DELLSLTEIK ELLHLFFKFW SNQVPILNND HFLIYFNNFV EVVKHLSTEN LETNNTTKST VTTNHEIFAL KLLMMLQMGL LVKIKMEKIK YTVPKNPKAK YARLMAYYHQ LSLIIPKNPY FLNMSTTSLP SLQLLSLASF YYLNVGDISA IYGVRGRIVS MAQQLRLHRC PSAVLSVHSN PVLQKFEQSE RRLLFWAIYY VDVFASLQLG VPRLLKDFDI ECALPISDVE YKDQLSMENE KADKKAKKIQ LQGQVSSFSL QIIRFAKILG NILDSIFKRG MMDERITSEV ALVHENALDN WRNQLPEMYY FQITVNGTVN LDEIRATNQR NTETKFDKKD IILFEKKILL LFYFLAKSMI HLPVIATKPL PKNVDNATKK KQSMFNNDSK GATNQDHMIL DVDMTSPAIR TSSSYIILQQ ATNATLTIFQ AINSMYLPLP LNVSRTLIRF SLLCARGSLE YTKGGALFLD NKNLLLDTIK DIENDRLLDL PGIASWHTLK LFDMSINLLL KAPNVKVERL DKFLEKKLNY YNRLMGLPPA TTTSLKPLFG SQSKNSLENR QRTPNVKREN PEHEYLYGND SNNNNNSEAG HSPMTNTTNG NKRLKYEKDA KRNAKDGGIS KGENAHNFQN DTKKNMSTSN LFPFSFSNTD LTALFTHPEG PNCTNTNNGN VDVCNRASTD ATDANIENLS FLNMAPFLQT GNSNIGQNTI ENKPMHMDAI FSLPSNLDLM KDNMDSKPEQ LEPVIKQNPE NSKNNQFHQK GKSTNMEKNN LSFNNKSNYS LTKLMRLLNN DNSFSNISIN NFLYQNDQNS ASADPGTNKK AVTNAGANFK PPSTGSNTSQ GSILGSTKHG MDNCDFNDLG NFNNFMTNVN YSGVDYDYIV DASLGLAPLL VDTPDISNTN TTSTTSNRSK NSIILDTTFN DDLDRSRMNA REVLNPTDSI LSQGMVSSVS TRNTSNQRSL SSGNDSKGDS SSQENSKSAT GNQLDTPSTL FQMRRTSSGP SASHRGPRRP QKNRYNTDRS KSSGGGSSNT DNVSDLFQWQ NAK //