WAR1_CANAL
ID WAR1_CANAL Reviewed; 947 AA.
AC Q59VQ8; A0A1D8PD27; Q59VV4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transcriptional regulator WAR1;
DE AltName: Full=Weak acid resistance protein 1;
GN Name=WAR1; OrderedLocusNames=CAALFM_C103740WA;
GN ORFNames=CaO19.1035, CaO19.8637;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=18629206; DOI=10.1002/cfg.492;
RA Maicas S., Moreno I., Nieto A., Gomez M., Sentandreu R., Valentin E.;
RT "In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear
RT cluster DNA-binding domains in Candida albicans.";
RL Comp. Funct. Genomics 6:345-356(2005).
RN [5]
RP IDENTIFICATION.
RX PubMed=16959962; DOI=10.1128/mmbr.00015-06;
RA MacPherson S., Larochelle M., Turcotte B.;
RT "A fungal family of transcriptional regulators: the zinc cluster
RT proteins.";
RL Microbiol. Mol. Biol. Rev. 70:583-604(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16544288; DOI=10.1002/yea.1346;
RA Lebel K., MacPherson S., Turcotte B.;
RT "New tools for phenotypic analysis in Candida albicans: the WAR1 gene
RT confers resistance to sorbate.";
RL Yeast 23:249-259(2006).
RN [7]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=18083829; DOI=10.1128/ec.00240-07;
RA Chiranand W., McLeod I., Zhou H., Lynn J.J., Vega L.A., Myers H.,
RA Yates J.R. III, Lorenz M.C., Gustin M.C.;
RT "CTA4 transcription factor mediates induction of nitrosative stress
RT response in Candida albicans.";
RL Eukaryot. Cell 7:268-278(2008).
RN [8]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22359502; DOI=10.1371/journal.ppat.1002525;
RA Finkel J.S., Xu W., Huang D., Hill E.M., Desai J.V., Woolford C.A.,
RA Nett J.E., Taff H., Norice C.T., Andes D.R., Lanni F., Mitchell A.P.;
RT "Portrait of Candida albicans adherence regulators.";
RL PLoS Pathog. 8:E1002525-E1002525(2012).
CC -!- FUNCTION: Transcription factor required for yeast cell adherence to
CC silicone substrate. Plays a role in resistance to weak organic acids
CC such as acetate and sorbate. Binds in vitro to a nitric oxide-
CC responsive element (NORE) but seems not to be involved in response to
CC nitrosative stress. {ECO:0000269|PubMed:16544288,
CC ECO:0000269|PubMed:18083829, ECO:0000269|PubMed:22359502}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC -!- INDUCTION: Expression is induced in biofilm.
CC {ECO:0000269|PubMed:22265407}.
CC -!- DISRUPTION PHENOTYPE: Leads to sensitivity to weak organic acids and
CC decreases cell adherence to silicone substrate.
CC {ECO:0000269|PubMed:16544288, ECO:0000269|PubMed:22359502}.
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DR EMBL; CP017623; AOW26051.1; -; Genomic_DNA.
DR RefSeq; XP_713640.2; XM_708547.2.
DR AlphaFoldDB; Q59VQ8; -.
DR STRING; 237561.Q59VQ8; -.
DR PRIDE; Q59VQ8; -.
DR GeneID; 3644691; -.
DR KEGG; cal:CAALFM_C103740WA; -.
DR CGD; CAL0000177698; WAR1.
DR VEuPathDB; FungiDB:C1_03740W_A; -.
DR eggNOG; ENOG502QRSG; Eukaryota.
DR HOGENOM; CLU_004837_1_0_1; -.
DR InParanoid; Q59VQ8; -.
DR OrthoDB; 644551at2759; -.
DR PRO; PR:Q59VQ8; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 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.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Stress response; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..947
FT /note="Transcriptional regulator WAR1"
FT /id="PRO_0000426087"
FT DNA_BIND 54..86
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 105854 MW; 9DAA645E36D94C01 CRC64;
MSDTTPEKGS VDSVSPSASN GSNTNNPLNN SSPQPLKSNE SDKKPKVTRR SVACKSCHSL
KVKCTPSDPN NPSAPCVRCI NANRICEIDL NQTRKRRKKS EILEAKRQAG QSLPEHKKEK
NTPTQSGYNS SENYSSSINN ANDSSLTSRY QSPMTFDPTS PMVFRPQASS AVPPISSNLN
PQSAAPTPIP TSGIPPQLPS PHESAILRGN TTSPTSKDDE INQLKQRVRF LETELANKRL
LANKKGFSND SPTDLQSPPF VSKFDLESEI SILAESSARL TDLTNQLNEA ASRRIQLVSA
KKPVDLISKG VITVAEAEER LKLYREQIYG RHPLIAIPDN MHAIEFSQSQ PFLFNSIMSA
CNLITKNADK DVVLAIDNEA MTSVAVEVMV VGTKSVELVK AFSVLCLYYN SPELFKQRRY
HMLNTICVSL LHDVGIFARP TYSYNQADGT LKQDASSKDK GNDEYRELVL ITYFVTVSTC
LVLRRSIYAR WTPYVEECCS LLENSSQEKH RRLALFARMN NKLDKIHHIV HAPEMPGQKS
GVSQYVIQEL QRLLSDLKLK IKDNQYSLLS YYYSIEAYLH EPILTKVFKS DTELDGKAMK
SIRYCTSSCL NALDEYSKLT PDQIALLPFP FGSRIMYTAG MLLRLRYLIL SLPSHIDKEL
VPKRAVTSIQ CVSKLVEQAN ILNPHNHYLT KMRLVLQLFI QTYATQVLEL LSKNGNTPQN
FKPDESETQQ LRALAREYND IRKVSKVSLV SDTRSAEPLD VLSYAATFRR ENNDKPSAVA
GSLRKSFSEN DQAIKTPSQC GQFVSANNTP VPQVINSPPI SQTNVPVLHQ SQSIINGNNR
NSAPLAFNNT TTPSLHQFGD VLPPSSMPQP DYRQFRLPSI SNTVHYSSNP RLNANLANPD
QLENSYQVLN DEFWSNLLST DSTDRINFTS NNFNGNTSND EVFFMNN
