ID   WAR1_YEAST              Reviewed;         944 AA.
AC   Q03631; D6W0K7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 163.
DE   RecName: Full=Weak acid resistance protein 1;
GN   Name=WAR1; OrderedLocusNames=YML076C;
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=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   [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, SUBCELLULAR LOCATION, SUBUNIT, AND PHOSPHORYLATION.
RX   PubMed=12588995; DOI=10.1128/mcb.23.5.1775-1785.2003;
RA   Kren A., Mamnun Y.M., Bauer B.E., Schueller C., Wolfger H.,
RA   Hatzixanthis K., Mollapour M., Gregori C., Piper P.W., Kuchler K.;
RT   "War1p, a novel transcription factor controlling weak acid stress response
RT   in yeast.";
RL   Mol. Cell. Biol. 23:1775-1785(2003).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION.
RX   PubMed=14617816; DOI=10.1091/mbc.e03-05-0322;
RA   Schueller C., Mamnun Y.M., Mollapour M., Krapf G., Schuster M., Bauer B.E.,
RA   Piper P.W., Kuchler K.;
RT   "Global phenotypic analysis and transcriptional profiling defines the weak
RT   acid stress response regulon in Saccharomyces cerevisiae.";
RL   Mol. Biol. Cell 15:706-720(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=16911515; DOI=10.1111/j.1567-1364.2006.00094.x;
RA   Hazelwood L.A., Tai S.L., Boer V.M., de Winde J.H., Pronk J.T.,
RA   Daran J.-M.;
RT   "A new physiological role for Pdr12p in Saccharomyces cerevisiae: export of
RT   aromatic and branched-chain organic acids produced in amino acid
RT   catabolism.";
RL   FEMS Yeast Res. 6:937-945(2006).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-762; PHE-763 AND
RP   ARG-764.
RX   PubMed=17509074; DOI=10.1111/j.1742-4658.2007.05837.x;
RA   Gregori C., Bauer B.E., Schwartz C., Kren A., Schueller C., Kuchler K.;
RT   "A genetic screen identifies mutations in the yeast WAR1 gene, linking
RT   transcription factor phosphorylation to weak-acid stress adaptation.";
RL   FEBS J. 274:3094-3107(2007).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF SER-368; TYR-452; TYR-463; ALA-640; SER-703
RP   AND LYS-762.
RX   PubMed=18621731; DOI=10.1074/jbc.m803095200;
RA   Gregori C., Schueller C., Frohner I.E., Ammerer G., Kuchler K.;
RT   "Weak organic acids trigger conformational changes of the yeast
RT   transcription factor War1 in vivo to elicit stress adaptation.";
RL   J. Biol. Chem. 283:25752-25764(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND IDENTIFICATION BY
RP   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: transcription factor which binds to a weak acid response
CC       element (WARE) to mediate stress induction of PDR12 and FUN34, encoding
CC       an acid transporter and a putative ammonia transporter, respectively.
CC       {ECO:0000269|PubMed:12588995, ECO:0000269|PubMed:14617816,
CC       ECO:0000269|PubMed:16911515, ECO:0000269|PubMed:17509074,
CC       ECO:0000269|PubMed:18621731}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12588995}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12588995,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17509074}.
CC   -!- PTM: Phosphorylation is required for PDR12 induction.
CC       {ECO:0000269|PubMed:12588995}.
CC   -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z46373; CAA86502.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09821.1; -; Genomic_DNA.
DR   PIR; S48821; S48821.
DR   RefSeq; NP_013635.1; NM_001182435.1.
DR   AlphaFoldDB; Q03631; -.
DR   BioGRID; 35065; 72.
DR   MINT; Q03631; -.
DR   STRING; 4932.YML076C; -.
DR   GlyGen; Q03631; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q03631; -.
DR   MaxQB; Q03631; -.
DR   PaxDb; 4932-YML076C; -.
DR   PeptideAtlas; Q03631; -.
DR   EnsemblFungi; YML076C_mRNA; YML076C; YML076C.
DR   GeneID; 854899; -.
DR   KEGG; sce:YML076C; -.
DR   AGR; SGD:S000004541; -.
DR   SGD; S000004541; WAR1.
DR   VEuPathDB; FungiDB:YML076C; -.
DR   eggNOG; ENOG502QRSG; Eukaryota.
DR   GeneTree; ENSGT00940000176681; -.
DR   HOGENOM; CLU_004837_0_0_1; -.
DR   InParanoid; Q03631; -.
DR   OMA; IYMHEIG; -.
DR   OrthoDB; 2048266at2759; -.
DR   BioCyc; YEAST:G3O-32668-MONOMER; -.
DR   BioGRID-ORCS; 854899; 0 hits in 13 CRISPR screens.
DR   PRO; PR:Q03631; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03631; Protein.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR   CDD; cd00067; GAL4; 1.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR31644; TRANSCRIPTIONAL ACTIVATOR ARO80-RELATED; 1.
DR   PANTHER; PTHR31644:SF1; WEAK ACID RESISTANCE PROTEIN 1; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..944
FT                   /note="Weak acid resistance protein 1"
FT                   /id="PRO_0000115004"
FT   DNA_BIND        76..109
FT                   /note="Zn(2)-C6 fungal-type"
FT   REGION          114..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         368
FT                   /note="S->L: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:18621731"
FT   MUTAGEN         452
FT                   /note="Y->C: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:18621731"
FT   MUTAGEN         463
FT                   /note="Y->C: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:18621731"
FT   MUTAGEN         640
FT                   /note="A->T: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:18621731"
FT   MUTAGEN         703
FT                   /note="S->P: Causes hyperactivitywith constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:18621731"
FT   MUTAGEN         762
FT                   /note="K->R,N: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:17509074,
FT                   ECO:0000269|PubMed:18621731"
FT   MUTAGEN         763
FT                   /note="F->M: Causes hyperactivity with constitutive
FT                   induction of PDR12."
FT                   /evidence="ECO:0000269|PubMed:17509074"
FT   MUTAGEN         764
FT                   /note="Missing: Causes hypersensitivity to sorbate through
FT                   its inability to induce PDR12."
FT                   /evidence="ECO:0000269|PubMed:17509074"
SQ   SEQUENCE   944 AA;  107561 MW;  020A56745DF52CCC CRC64;
     MDTQIAITGV AVGKEINNDN SKTDQKVSLP KADVPCIDKA TQTIIEGCSK DDPRLSYPTK
     LETTEKGKTK RNSFACVCCH SLKQKCEPSD VNDIYRKPCR RCLKHKKLCK FDLSKRTRKR
     KPRSRSPTPF ESPMVNVSTK SKGPTDSEES SLKDGTSYLA SFPSDPNAKQ FPNSRTVLPG
     LQQSLSDLWS TLSQPPSYGA REAETTSTGE ITTNNHTKSN GSVPTNPAVL ASNDEHTNIS
     DAPVIYSTYN SPVPISSAPT SINSEALFKH RPKIVGDEET QNVKVKRQKK SYSRHMTRSF
     RKQLQSLIIS QKGKIRDISM KLDTWSKQWN DLVEKSMFLP TIADPVSVGI ISHEEATLRL
     HLYKTEISYL SKLPFIKVEE NVSVDELRKK KPILFSVIMS CVSIVLTPKQ TTRGTIMKLD
     SFVLNLITNQ IFKANNKSIE IIESLSTLCL WYNFFEWSSK TRYHIFNYIC CCLTRDLGPT
     YVNRSFGMFS DEDPKRFKSP LELYSNGASL TLLVYISALN ISIFLRQSIQ ARWSHVTEKA
     CEDLVKETKK SRHYDNDKLL LDSADDPILV QFAKMNHVLE NIHTHLHERD LNDDEFDDPI
     FTKKYLNKLM EKYHKQLQEI FTKLDRNRPR VIAFYYSVEA YLYQYKLAVF IGEMSHTINE
     KVELPREIMD DFVKCYHCCK SALEEFSKLE PILITSLPLF HTSRIIYTVG MLLLKLRYSV
     VAIPSFHDLM PLTDDAIALV IGVNNLLEKT SELYPFNNSL YKFRYVIALF CQTYANKVID
     VADRYNAERE KLKEKQVIDE VSNGHDGTKP INAYVTESQK MPTEEDPIID NNTNQNITAV
     PDEMLPVYSR VRDDTAAMNL NINSTSYMNE SPHEHRESMT GTTLLPPPFI SNDVTNSADS
     TNIKPSPSSS VDNLNDYLTD INSLAWGVNS LNDEFWTDLF MNDI
//