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CZF1_CANAL
ID   CZF1_CANAL              Reviewed;         385 AA.
AC   Q5A0W9; A0A1D8PMN7;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Zinc cluster transcription factor CZF1;
GN   Name=CZF1; Synonyms=ZNF1; OrderedLocusNames=CAALFM_C406820CA;
GN   ORFNames=CaO19.10639, CaO19.3127;
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   FUNCTION.
RX   PubMed=1409649; DOI=10.1073/pnas.89.20.9410;
RA   Whiteway M., Dignard D., Thomas D.Y.;
RT   "Dominant negative selection of heterologous genes: isolation of Candida
RT   albicans genes that interfere with Saccharomyces cerevisiae mating factor-
RT   induced cell cycle arrest.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9410-9414(1992).
RN   [5]
RP   DNA-BINDING.
RX   PubMed=9290251; DOI=10.1006/fgbi.1997.0993;
RA   Todd R.B., Andrianopoulos A.;
RT   "Evolution of a fungal regulatory gene family: the Zn(II)2Cys6 binuclear
RT   cluster DNA binding motif.";
RL   Fungal Genet. Biol. 21:388-405(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=10564506; DOI=10.1046/j.1365-2958.1999.01619.x;
RA   Brown D.H. Jr., Giusani A.D., Chen X., Kumamoto C.A.;
RT   "Filamentous growth of Candida albicans in response to physical
RT   environmental cues and its regulation by the unique CZF1 gene.";
RL   Mol. Microbiol. 34:651-662(1999).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH EFG1.
RX   PubMed=11973327; DOI=10.1093/genetics/160.4.1749;
RA   Giusani A.D., Vinces M., Kumamoto C.A.;
RT   "Invasive filamentous growth of Candida albicans is promoted by Czf1p-
RT   dependent relief of Efg1p-mediated repression.";
RL   Genetics 160:1749-1753(2002).
RN   [8]
RP   DNA-BINDING.
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   [9]
RP   INDUCTION.
RX   PubMed=16682460; DOI=10.1128/ec.5.5.825-835.2006;
RA   Vinces M.D., Haas C., Kumamoto C.A.;
RT   "Expression of the Candida albicans morphogenesis regulator gene CZF1 and
RT   its regulation by Efg1p and Czf1p.";
RL   Eukaryot. Cell 5:825-835(2006).
RN   [10]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=17768232; DOI=10.1099/mic.0.2007/005983-0;
RA   Vinces M.D., Kumamoto C.A.;
RT   "The morphogenetic regulator Czf1p is a DNA-binding protein that regulates
RT   white opaque switching in Candida albicans.";
RL   Microbiology 153:2877-2884(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=17880264; DOI=10.1371/journal.pbio.0050256;
RA   Zordan R.E., Miller M.G., Galgoczy D.J., Tuch B.B., Johnson A.D.;
RT   "Interlocking transcriptional feedback loops control white-opaque switching
RT   in Candida albicans.";
RL   PLoS Biol. 5:E256-E256(2007).
RN   [12]
RP   FUNCTION.
RX   PubMed=18551173; DOI=10.1371/journal.ppat.1000089;
RA   Ramirez-Zavala B., Reuss O., Park Y.N., Ohlsen K., Morschhauser J.;
RT   "Environmental induction of white-opaque switching in Candida albicans.";
RL   PLoS Pathog. 4:E1000089-E1000089(2008).
RN   [13]
RP   FUNCTION.
RX   PubMed=18579689; DOI=10.1091/mbc.e07-12-1272;
RA   Hope H., Bogliolo S., Arkowitz R.A., Bassilana M.;
RT   "Activation of Rac1 by the guanine nucleotide exchange factor Dck1 is
RT   required for invasive filamentous growth in the pathogen Candida
RT   albicans.";
RL   Mol. Biol. Cell 19:3638-3651(2008).
RN   [14]
RP   INDUCTION.
RX   PubMed=19197361; DOI=10.1371/journal.ppat.1000294;
RA   Bastidas R.J., Heitman J., Cardenas M.E.;
RT   "The protein kinase Tor1 regulates adhesin gene expression in Candida
RT   albicans.";
RL   PLoS Pathog. 5:E1000294-E1000294(2009).
RN   [15]
RP   FUNCTION.
RX   PubMed=20735781; DOI=10.1111/j.1365-2958.2010.07331.x;
RA   Lohse M.B., Johnson A.D.;
RT   "Temporal anatomy of an epigenetic switch in cell programming: the white-
RT   opaque transition of C. albicans.";
RL   Mol. Microbiol. 78:331-343(2010).
RN   [16]
RP   FUNCTION.
RX   PubMed=21407800; DOI=10.1371/journal.pone.0017046;
RA   Wachtler B., Wilson D., Haedicke K., Dalle F., Hube B.;
RT   "From attachment to damage: defined genes of Candida albicans mediate
RT   adhesion, invasion and damage during interaction with oral epithelial
RT   cells.";
RL   PLoS ONE 6:E17046-E17046(2011).
RN   [17]
RP   FUNCTION.
RX   PubMed=22897889; DOI=10.1186/1471-2164-13-396;
RA   Dhamgaye S., Bernard M., Lelandais G., Sismeiro O., Lemoine S.,
RA   Coppee J.Y., Le Crom S., Prasad R., Devaux F.;
RT   "RNA sequencing revealed novel actors of the acquisition of drug resistance
RT   in Candida albicans.";
RL   BMC Genomics 13:396-396(2012).
RN   [18]
RP   FUNCTION, DNA-BINDING, INTERACTION WITH EFG1, AND MUTAGENESIS OF ARG-321
RP   AND LYS-322.
RX   PubMed=22761849; DOI=10.1371/journal.pone.0039624;
RA   Petrovska I., Kumamoto C.A.;
RT   "Functional importance of the DNA binding activity of Candida albicans
RT   Czf1p.";
RL   PLoS ONE 7:E39624-E39624(2012).
RN   [19]
RP   FUNCTION.
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: Transcriptional regulator of the switch between 2 heritable
CC       states, the white and opaque states. These 2 cell types differ in many
CC       characteristics, including cell structure, mating competence, and
CC       virulence. Each state is heritable for many generations, and switching
CC       between states occurs stochastically, at low frequency. Contributes to
CC       formation of the opaque state, but is not necessary for heritability of
CC       the opaque state. Plays a role in cell adhesion and pseudohyphal
CC       growth. Involved in acquisition of drug resistance and acts as a
CC       repressor of beta-glucan synthesis, thus negatively regulating cell
CC       wall integrity. Plays a role in adherence, invasion and damage to oral
CC       epithelial cells. {ECO:0000269|PubMed:10564506,
CC       ECO:0000269|PubMed:11973327, ECO:0000269|PubMed:1409649,
CC       ECO:0000269|PubMed:17768232, ECO:0000269|PubMed:17880264,
CC       ECO:0000269|PubMed:18551173, ECO:0000269|PubMed:18579689,
CC       ECO:0000269|PubMed:20735781, ECO:0000269|PubMed:21407800,
CC       ECO:0000269|PubMed:22359502, ECO:0000269|PubMed:22761849,
CC       ECO:0000269|PubMed:22897889}.
CC   -!- SUBUNIT: Interacts with EFG1. {ECO:0000269|PubMed:11973327,
CC       ECO:0000269|PubMed:22761849}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- INDUCTION: Regulated in response to carbon source, temperature, growth
CC       phase, and physical environment. Expression is up-regulated by
CC       rapamycine, and thus is under the regulation of the TOR pathway. Binds
CC       its own promoter and is also under the control of EFG1.
CC       {ECO:0000269|PubMed:16682460, ECO:0000269|PubMed:19197361}.
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DR   EMBL; CP017626; AOW29403.1; -; Genomic_DNA.
DR   RefSeq; XP_715436.1; XM_710343.2.
DR   AlphaFoldDB; Q5A0W9; -.
DR   SMR; Q5A0W9; -.
DR   BioGRID; 1225956; 3.
DR   STRING; 237561.Q5A0W9; -.
DR   PRIDE; Q5A0W9; -.
DR   GeneID; 3642915; -.
DR   KEGG; cal:CAALFM_C406820CA; -.
DR   CGD; CAL0000193101; CZF1.
DR   VEuPathDB; FungiDB:C4_06820C_A; -.
DR   eggNOG; ENOG502RK5N; Eukaryota.
DR   HOGENOM; CLU_705961_0_0_1; -.
DR   InParanoid; Q5A0W9; -.
DR   OMA; LRLNCTW; -.
DR   OrthoDB; 1601379at2759; -.
DR   PRO; PR:Q5A0W9; -.
DR   Proteomes; UP000000559; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:CGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR   GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CGD.
DR   GO; GO:1900241; P:positive regulation of phenotypic switching; IMP:CGD.
DR   GO; GO:0009372; P:quorum sensing; IMP:CGD.
DR   GO; GO:1900443; P:regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:1900239; P:regulation of phenotypic switching; IMP:CGD.
DR   GO; GO:1900231; P:regulation of single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
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   Pfam; PF00172; Zn_clus; 1.
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   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Virulence; Zinc.
FT   CHAIN           1..385
FT                   /note="Zinc cluster transcription factor CZF1"
FT                   /id="PRO_0000420154"
FT   DNA_BIND        315..342
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          1..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..364
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         321
FT                   /note="R->A: Impairs DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:22761849"
FT   MUTAGEN         322
FT                   /note="K->A: Decreases DNA-binding."
FT                   /evidence="ECO:0000269|PubMed:22761849"
SQ   SEQUENCE   385 AA;  43379 MW;  561544C4119C4D6C CRC64;
     MSSIPNINWN DPNNGKSNTS RQSQPQPQLP SNVSPPNSRA VPTSGSIGGP QYGSSQFSNE
     YSRNPNTIGG PPFPLQSNQR GYMPNTGYPV QQTAQQRSGD KLQQVHSQQQ QQQQQPLYQQ
     YPPQSVGYLA GDVYNPQHQE YVQMNQLPNQ HYNLQQRQQA QGQQLKSQLN EQNAMMSAST
     QQYPVQDFTN PYPNAQNPAE QQQQQQPLRT QSQQWDGYQS QPLYSAAGNT IPSSIQQQIP
     PQNLSPSEQQ QVKQQQPSPP EQGTKKKPGR KPKLRKLSES SSETPQVPKT ASSSSSSPTA
     VNSGKPITKR SRMGCLTCRQ RKKRCCETRP RCTECTRLRL NCTWPKPGTE HKNKPKDQKD
     DENTIEHAEF GRIKVLRGIV EYRSK
 
 
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