CRZ2_CANAL
ID CRZ2_CANAL Reviewed; 517 AA.
AC Q59SN6; A0A1D8PTD2; Q59SQ8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Transcriptional regulator CRZ2;
DE AltName: Full=Calcineurin-responsive zinc finger protein 2;
GN Name=CRZ2; OrderedLocusNames=CAALFM_CR07060CA;
GN ORFNames=CaO19.2356, CaO19.9892;
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=15554973; DOI=10.1111/j.1365-2958.2004.04350.x;
RA Bensen E.S., Martin S.J., Li M., Berman J., Davis D.A.;
RT "Transcriptional profiling in Candida albicans reveals new adaptive
RT responses to extracellular pH and functions for Rim101p.";
RL Mol. Microbiol. 54:1335-1351(2004).
RN [5]
RP FUNCTION.
RX PubMed=17927701; DOI=10.1111/j.1365-2958.2007.05929.x;
RA Kullas A.L., Martin S.J., Davis D.;
RT "Adaptation to environmental pH: integrating the Rim101 and calcineurin
RT signal transduction pathways.";
RL Mol. Microbiol. 66:858-871(2007).
RN [6]
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 [7]
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 that regulates pH-induced filamentation
CC with RIM101. Required for yeast cell adherence to silicone substrate
CC and biofilm formation. {ECO:0000269|PubMed:17927701,
CC ECO:0000269|PubMed:22359502}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: Expression is down-regulated during growth at pH 8 by the
CC pH-responsive transcription factor RIM101. Induced during exposure to
CC the weak acid stress of acetic acid, through the regulation by the
CC transcription factor MNL1. {ECO:0000269|PubMed:15554973,
CC ECO:0000269|PubMed:18653474}.
CC -!- DISRUPTION PHENOTYPE: Decreases cell adherence to silicone substrate.
CC Blocks biofilm formation. {ECO:0000269|PubMed:22359502}.
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DR EMBL; CP017630; AOW31401.1; -; Genomic_DNA.
DR RefSeq; XP_712647.2; XM_707554.2.
DR AlphaFoldDB; Q59SN6; -.
DR STRING; 237561.Q59SN6; -.
DR GeneID; 3645725; -.
DR KEGG; cal:CAALFM_CR07060CA; -.
DR CGD; CAL0000189549; CRZ2.
DR VEuPathDB; FungiDB:CR_07060C_A; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_528910_0_0_1; -.
DR OrthoDB; 1591573at2759; -.
DR PRO; PR:Q59SN6; -.
DR Proteomes; UP000000559; Chromosome R.
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: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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071468; P:cellular response to acidic pH; IMP:CGD.
DR GO; GO:0070417; P:cellular response to cold; IMP:CGD.
DR GO; GO:0071280; P:cellular response to copper ion; 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: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 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 2: Evidence at transcript level;
KW Cell adhesion; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..517
FT /note="Transcriptional regulator CRZ2"
FT /id="PRO_0000426055"
FT ZN_FING 358..380
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 386..408
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..446
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 19..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57443 MW; F6985D9A857BAB13 CRC64;
MLSTMSNLPI VAGISTTATT GTTSTATAST STSGSVNTTA TNNNNNTSAS NSTSASSATA
NGGIGTNSGN SLQYYYTGNN TSNSVDGNKY SLPSIYFTPQ DSINNTSHTY NPYTTVSGAV
TPQNYQLDYS QSSTVNNNYQ FTLPNQQLSS PQQQQYNRSY SNSLMPNYHY NNTTTNINTN
VGSNTSPQLS NSNTPNPISP VLIPDKDNTY NNTNNVLVSS YPSMTMNQIQ QQQQQYLQPS
QQYQYSYNQY YMQPYYHNPQ QSAPQQVQKP AQTEKLPHLS VTNIDYSSLV SYTVSPSLKR
KRRTAKKSLS PSSTSSLSMM INHDSTNNGT TSTATTTRSS STSSATSSSI GVAAADSFPC
PQCNKVFQKP YNLKSHMKTH SNEKPYHCNI CFKRFARSHD KKRHELLHQG VKNFKCQGYL
NDGVTSWGCG KTFARSDALS RHFRTETGWL CIRPLMEEAK RLEEEEQQRQ QQAQQQQQVP
QQSQVSEQIG VNVGEIKFND EYYDNSNFIK KLLQSNK
