CRZ1_CANAL
ID CRZ1_CANAL Reviewed; 731 AA.
AC Q5A4H5; A0A1D8PKB1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Transcriptional regulator CRZ1;
DE AltName: Full=Calcineurin-responsive zinc finger protein 1;
GN Name=CRZ1; OrderedLocusNames=CAALFM_C305780CA; ORFNames=CaO19.7359;
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 INDUCTION.
RX PubMed=12397174; DOI=10.1073/pnas.232566499;
RA Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA Agabian N.;
RT "Metabolic specialization associated with phenotypic switching in
RT Candidaalbicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
RN [5]
RP FUNCTION.
RX PubMed=15557662; DOI=10.1128/iai.72.12.7330-7333.2004;
RA Onyewu C., Wormley F.L. Jr., Perfect J.R., Heitman J.;
RT "The calcineurin target, Crz1, functions in azole tolerance but is not
RT required for virulence of Candida albicans.";
RL Infect. Immun. 72:7330-7333(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16044281; DOI=10.1007/s00294-005-0003-8;
RA Santos M., de Larrinoa I.F.;
RT "Functional characterization of the Candida albicans CRZ1 gene encoding a
RT calcineurin-regulated transcription factor.";
RL Curr. Genet. 48:88-100(2005).
RN [7]
RP FUNCTION.
RX PubMed=17056742; DOI=10.1128/ec.00274-06;
RA Cowen L.E., Carpenter A.E., Matangkasombut O., Fink G.R., Lindquist S.;
RT "Genetic architecture of Hsp90-dependent drug resistance.";
RL Eukaryot. Cell 5:2184-2188(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16468987; DOI=10.1111/j.1365-2958.2005.05037.x;
RA Karababa M., Valentino E., Pardini G., Coste A.T., Bille J., Sanglard D.;
RT "CRZ1, a target of the calcineurin pathway in Candida albicans.";
RL Mol. Microbiol. 59:1429-1451(2006).
RN [9]
RP INDUCTION.
RX PubMed=18653474; DOI=10.1091/mbc.e07-09-0946;
RA Ramsdale M., Selway L., Stead D., Walker J., Yin Z., Nicholls S.M.,
RA Crowe J., Sheils E.M., Brown A.J.;
RT "MNL1 regulates weak acid-induced stress responses of the fungal pathogen
RT Candida albicans.";
RL Mol. Biol. Cell 19:4393-4403(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21457451; DOI=10.1111/j.1567-1364.2011.00730.x;
RA Wang H., Liang Y., Zhang B., Zheng W., Xing L., Li M.;
RT "Alkaline stress triggers an immediate calcium fluctuation in Candida
RT albicans mediated by Rim101p and Crz1p transcription factors.";
RL FEMS Yeast Res. 11:430-439(2011).
CC -!- FUNCTION: Transcription factor involved in the regulation of calcium
CC ion homeostasis and required for the maintenance of membrane integrity.
CC Binds to the calcineurin-dependent response element. Plays a role in
CC azole tolerance. {ECO:0000269|PubMed:15557662,
CC ECO:0000269|PubMed:16044281, ECO:0000269|PubMed:16468987,
CC ECO:0000269|PubMed:17056742, ECO:0000269|PubMed:21457451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes in the nucleus
CC in a calcium- and calcineurin-dependent manner.
CC -!- INDUCTION: Expression is higher in white cells than opaque cells.
CC Induced during exposure to the weak acid stress of acetic acid, through
CC the regulation by the transcription factor MNL1.
CC {ECO:0000269|PubMed:12397174, ECO:0000269|PubMed:18653474}.
CC -!- PTM: Probably phosphorylated in a calcineurin-dependent manner.
CC {ECO:0000269|PubMed:16468987}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to ion stress.
CC {ECO:0000269|PubMed:16044281, ECO:0000269|PubMed:16468987,
CC ECO:0000269|PubMed:21457451}.
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DR EMBL; CP017625; AOW28587.1; -; Genomic_DNA.
DR RefSeq; XP_716600.1; XM_711507.1.
DR AlphaFoldDB; Q5A4H5; -.
DR STRING; 237561.Q5A4H5; -.
DR PRIDE; Q5A4H5; -.
DR GeneID; 3641722; -.
DR KEGG; cal:CAALFM_C305780CA; -.
DR CGD; CAL0000176618; CRZ1.
DR VEuPathDB; FungiDB:C3_05780C_A; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_016101_0_0_1; -.
DR InParanoid; Q5A4H5; -.
DR OMA; PSLYACH; -.
DR OrthoDB; 1591573at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IDA:CGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:CGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IGI:CGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:CGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:CGD.
DR GO; GO:0071468; P:cellular response to acidic pH; IMP:CGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:CGD.
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:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:CGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..731
FT /note="Transcriptional regulator CRZ1"
FT /id="PRO_0000426054"
FT ZN_FING 613..635
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 641..663
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 669..700
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 54..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 81092 MW; C0060DC492315A45 CRC64;
MSNNPHPQDD GSQLYDNFEI SPPSIVIRKA DTDQSLNKIM LNQESQDINN YYTENVKNDN
NPNNSYQDYT FSGNSSNQQH QQQQQQHLYE DLPTQFHYSN NSFFEPPPAP TVELTDDPLP
NFNYPPSNIY INDNASDISL NTKDLPQFTT NEFLSPTSQL STPFSPGHYS QSSQDFLQVN
HTNGSGNNNN NNNNNNLLNP RSPSQYSSHS LYSDNSSQPA SPFLDAASHV SNNSFIPPVI
PTALSDVGSQ NLDPSHNLGL SANQHFDSVN EFLSTGEIQL GQSVSSTNLP SMEEDSIKWG
GGNGQEAYTS LAMMEQRASA DNSGMRLATH QFSETQIKQE DQQTNMNHQY TFSNPQMNFD
FDITVTPPPQ QLEVKPFGND KDMNNSSGTT NNNNNNSQFD IVSTAATNNS NQLLTENNLS
NYNQLQRTEQ GNDNDSLQIH RDATGIIISI NQAPEEIAAK TPSLFSNSSA NSSIHNSPRS
DIDNKSGQYY NNGGDGNSLV PNSQLLPSSP NSNNDNYGGG GSSNDENNLL NPEEFQSVKR
GRRKSHASRT STNPNSLSPR SRSRSRSSAK SSNDAVISDN DESDDVLQSR EKMLELALPS
SSSKRTQKHP SLYACHLCDK RFTRPYNLKS HIRTHTQEKP FICSKCGKSF ARSHDKKRHE
LLHQGIKNFK CEGYLQDGTR WGCGKSFARA DALRRHFQTE AGKQCVKRLL LEEQANSSGK
PLATSSGVEI T
