ID   CHA4_YEAST              Reviewed;         648 AA.
AC   P43634; D6VY98;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Activatory protein CHA4;
GN   Name=CHA4; Synonyms=SIL2, SIL3; OrderedLocusNames=YLR098C;
GN   ORFNames=L8004.8;
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], AND FUNCTION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8889513; DOI=10.1093/genetics/144.2.467;
RA   Holmberg S., Schjerling P.;
RT   "Cha4p of Saccharomyces cerevisiae activates transcription via
RT   serine/threonine response elements.";
RL   Genetics 144:467-478(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-166, AND
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: Activates the CHA1 gene for L-serine dehydratase. Binds to
CC       the DNA sequence 5'-GVGGARAYRTRATTCCRC-3'.
CC       {ECO:0000269|PubMed:8889513}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z49975; CAA90276.1; -; Genomic_DNA.
DR   EMBL; U53876; AAB67542.1; -; Genomic_DNA.
DR   EMBL; Z73270; CAA97662.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09414.1; -; Genomic_DNA.
DR   PIR; S59723; S59723.
DR   RefSeq; NP_013199.1; NM_001181985.1.
DR   AlphaFoldDB; P43634; -.
DR   SMR; P43634; -.
DR   BioGRID; 31371; 130.
DR   DIP; DIP-1798N; -.
DR   IntAct; P43634; 11.
DR   MINT; P43634; -.
DR   STRING; 4932.YLR098C; -.
DR   iPTMnet; P43634; -.
DR   MaxQB; P43634; -.
DR   PaxDb; 4932-YLR098C; -.
DR   PeptideAtlas; P43634; -.
DR   EnsemblFungi; YLR098C_mRNA; YLR098C; YLR098C.
DR   GeneID; 850787; -.
DR   KEGG; sce:YLR098C; -.
DR   AGR; SGD:S000004088; -.
DR   SGD; S000004088; CHA4.
DR   VEuPathDB; FungiDB:YLR098C; -.
DR   eggNOG; ENOG502QTSE; Eukaryota.
DR   HOGENOM; CLU_015811_0_0_1; -.
DR   InParanoid; P43634; -.
DR   OMA; YNFDFTL; -.
DR   OrthoDB; 1786197at2759; -.
DR   BioCyc; YEAST:G3O-32248-MONOMER; -.
DR   BioGRID-ORCS; 850787; 2 hits in 13 CRISPR screens.
DR   PRO; PR:P43634; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P43634; Protein.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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; HDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009063; P:amino acid catabolic process; IMP:SGD.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:SGD.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 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; PTHR31313:SF82; ACTIVATORY PROTEIN CHA4; 1.
DR   PANTHER; PTHR31313; TY1 ENHANCER ACTIVATOR; 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; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..648
FT                   /note="Activatory protein CHA4"
FT                   /id="PRO_0000114942"
FT   DNA_BIND        44..70
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   648 AA;  74393 MW;  CF3381B4C0356F82 CRC64;
     MMLEPSPPPL TTTVTPSLPS SLKKSVTDND QNNNNVPRKR KLACQNCRRR RRKCNMEKPC
     SNCIKFRTEC VFTQQDLRNK RYSTTYVEAL QSQIRSLKEQ LQILSSSSST IASNALSSLK
     NNSDHGDAPN EKILKYGETA QSALPSSESN DENESDAFTK KMPSESPPPV GTNSIYPSNS
     LSIIKKKTDG STRYQQQQVS LKNLSRSPLI LRSLSLFFKW LYPGHYLFIH RETFLSAFFG
     DTNTKSYYCS EELVFAIAAL GSLISYKSET ELFQQSEVFY QRAKTIVLKK IFQLEDSSLA
     ESSSSSKLAI IQTLLCLAFY DIGSGENPMA WYLSGLAFRI AHEIGLHLNP EAWSNVYEDE
     LSIMDFEVRS RIYWGCYIAD HLIAILFGRS TSLRLSNSTV PETDELPEIE TGIEEYIYDP
     KVILSTANPL KKLIVLSRIT EIFASKIFSP NETLLQRSEY LAKFNLEVYN WRRDLPPELQ
     WTKRSLMEMT DFNPTIAYVW FHYYIVLISY NKPFIYEIKQ SRELVEGYVD ELYYLLKVWK
     NKFKTFEKAT IYMIYSAILA IQCMKSNLIK KDRKQDFLNF LSAPTLNYEL ARKFIENSED
     ALHNSETMDL LGTLSHGNDF ALEYNFDFTL LNEIDMLIGG NTNDGLSK
//