CRZ1_YEAST
ID CRZ1_YEAST Reviewed; 678 AA.
AC P53968; D6W1F1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Transcriptional regulator CRZ1;
GN Name=CRZ1; Synonyms=HAL8, TCN1; OrderedLocusNames=YNL027W; ORFNames=N2760;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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.
RX PubMed=9407036; DOI=10.1101/gad.11.24.3445;
RA Matheos D.P., Kingsbury T.J., Ahsan U.S., Cunningham K.W.;
RT "Tcn1p/Crz1p, a calcineurin-dependent transcription factor that
RT differentially regulates gene expression in Saccharomyces cerevisiae.";
RL Genes Dev. 11:3445-3458(1997).
RN [4]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10197980; DOI=10.1101/gad.13.7.798;
RA Stathopoulos-Gerontides A., Guo J.J., Cyert M.S.;
RT "Yeast calcineurin regulates nuclear localization of the Crz1p
RT transcription factor through dephosphorylation.";
RL Genes Dev. 13:798-803(1999).
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 PHOSPHORYLATION.
RX PubMed=16455487; DOI=10.1016/j.molcel.2005.12.011;
RA Sopko R., Huang D., Preston N., Chua G., Papp B., Kafadar K., Snyder M.,
RA Oliver S.G., Cyert M., Hughes T.R., Boone C., Andrews B.J.;
RT "Mapping pathways and phenotypes by systematic gene overexpression.";
RL Mol. Cell 21:319-330(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170; SER-175 AND SER-385, AND
RP IDENTIFICATION BY 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: Involved in the regulation of calcium ion homeostasis. Binds
CC to the calcineurin-dependent response element. Transcriptionally
CC regulates PMC1, PMR1, PMR2A and FKS2. {ECO:0000269|PubMed:9407036}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10197980}. Cytoplasm
CC {ECO:0000269|PubMed:10197980}.
CC -!- PTM: Phosphorylated. Dephosphorylated by calcineurin which leads to
CC rapid translocation from the cytoplasm to the nucleus. Phosphorylated
CC by the cyclin-CDK PHO80-PHO85. {ECO:0000269|PubMed:10197980,
CC ECO:0000269|PubMed:16455487}.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z71303; CAA95889.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10517.1; -; Genomic_DNA.
DR PIR; S62939; S62939.
DR RefSeq; NP_014371.1; NM_001182866.1.
DR AlphaFoldDB; P53968; -.
DR BioGRID; 35799; 216.
DR DIP; DIP-2724N; -.
DR ELM; P53968; -.
DR IntAct; P53968; 21.
DR MINT; P53968; -.
DR STRING; 4932.YNL027W; -.
DR iPTMnet; P53968; -.
DR MaxQB; P53968; -.
DR PaxDb; P53968; -.
DR PRIDE; P53968; -.
DR EnsemblFungi; YNL027W_mRNA; YNL027W; YNL027W.
DR GeneID; 855704; -.
DR KEGG; sce:YNL027W; -.
DR SGD; S000004972; CRZ1.
DR VEuPathDB; FungiDB:YNL027W; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_030450_0_0_1; -.
DR InParanoid; P53968; -.
DR OMA; HTHINEG; -.
DR BioCyc; YEAST:G3O-33065-MON; -.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:P53968; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53968; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
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:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0006038; P:cell wall chitin biosynthetic process; IGI:SGD.
DR GO; GO:0071483; P:cellular response to blue light; IDA:SGD.
DR GO; GO:0050801; P:ion homeostasis; IMP:SGD.
DR GO; GO:2001040; P:positive regulation of cellular response to drug; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
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..678
FT /note="Transcriptional regulator CRZ1"
FT /id="PRO_0000046804"
FT ZN_FING 569..591
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 597..619
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 678 AA; 76301 MW; 247175416AFC186A CRC64;
MSFSNGNMAS YMTSSNGEEQ SINNKNDIDD NSAYRRNNFR NSSNSGSHTF QLSDLDLDVD
MRMDSANSSE KISKNLSSGI PDSFDSNVNS LLSPSSGSYS ADLNYQSLYK PDLPQQQLQQ
QQLQQQQQQQ QQQQQQQQKQ TPTLKVEQSD TFQWDDILTP ADNQHRPSLT NQFLSPRSNY
DGTTRSSGID SNYSDTESNY HTPYLYPQDL VSSPAMSHLT ANNDDFDDLL SVASMNSNYL
LPVNSHGYKH ISNLDELDDL LSLTYSDNNL LSASNNSDFN NSNNGIINTA DTQNSTIAIN
KSKVGTNQKM LLTIPTSSTP SPSTHAAPVT PIISIQEFNE GHFPVKNEDD GTLQLKVRDN
ESYSATNNNN LLRPDDNDYN NEALSDIDRS FEDIINGRKL KLKKSRRRSS QTSNNSFTSR
RSSRSRSISP DEKAKSISAN REKLLEMADL LPSSENDNNR ERYDNDSKTS YNTINSSNFN
EDNNNNNLLT SKPKIESGIV NIKNELDDTS KDLGILLDID SLGQFEQKVG FKNDDNHENN
DNGTFSVKKN DNLEKLDSVT NNRKNPANFA CDVCGKKFTR PYNLKSHLRT HTNERPFICS
ICGKAFARQH DRKRHEDLHT GKKRYVCGGK LKDGKPWGCG KKFARSDALG RHFKTESGRR
CITPLYEEAR QEKSGQES
