WAR1_YEAST
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 03-AUG-2022, entry version 155.
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; 70.
DR MINT; Q03631; -.
DR STRING; 4932.YML076C; -.
DR iPTMnet; Q03631; -.
DR MaxQB; Q03631; -.
DR PaxDb; Q03631; -.
DR PRIDE; Q03631; -.
DR EnsemblFungi; YML076C_mRNA; YML076C; YML076C.
DR GeneID; 854899; -.
DR KEGG; sce:YML076C; -.
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; INLYMHE; -.
DR BioCyc; YEAST:G3O-32668-MON; -.
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; IC: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:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; IDA:SGD.
DR CDD; cd00067; GAL4; 1.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 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
