RDS2_YEAST
ID RDS2_YEAST Reviewed; 446 AA.
AC P19541; D6W3N4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Regulator of drug sensitivity 2;
GN Name=RDS2; OrderedLocusNames=YPL133C; ORFNames=LPI12C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RX PubMed=2167832; DOI=10.1002/j.1460-2075.1990.tb07463.x;
RA Tzagoloff A., Capitanio N., Nobrega M.P., Gatti D.;
RT "Cytochrome oxidase assembly in yeast requires the product of COX11, a
RT homolog of the P. denitrificans protein encoded by ORF3.";
RL EMBO J. 9:2759-2764(1990).
RN [5]
RP PRESENCE OF A ZN(2)-CYS(6) FUNGAL-TYPE BINUCLEAR CLUSTER.
RX PubMed=1304897; DOI=10.1002/pro.5560011216;
RA Bork P., Ouzounis C., Sander C., Scharf M., Schneider R., Sonnhammer E.;
RT "Comprehensive sequence analysis of the 182 predicted open reading frames
RT of yeast chromosome III.";
RL Protein Sci. 1:1677-1690(1992).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=11943786; DOI=10.1074/jbc.m202566200;
RA Akache B., Turcotte B.;
RT "New regulators of drug sensitivity in the family of yeast zinc cluster
RT proteins.";
RL J. Biol. Chem. 277:21254-21260(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=16652171; DOI=10.1371/journal.ppat.0020035;
RA Wheeler R.T., Fink G.R.;
RT "A drug-sensitive genetic network masks fungi from the immune system.";
RL PLoS Pathog. 2:E35-E35(2006).
RN [10]
RP DNA-BINDING.
RX PubMed=16785442; DOI=10.1073/pnas.0509185103;
RA Ho S.-W., Jona G., Chen C.T.L., Johnston M., Snyder M.;
RT "Linking DNA-binding proteins to their recognition sequences by using
RT protein microarrays.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9940-9945(2006).
RN [11]
RP FUNCTION, DNA-BINDING, AND PHOSPHORYLATION BY SNF1.
RX PubMed=17875938; DOI=10.1128/mcb.01055-07;
RA Soontorngun N., Larochelle M., Drouin S., Robert F., Turcotte B.;
RT "Regulation of gluconeogenesis in Saccharomyces cerevisiae is mediated by
RT activator and repressor functions of Rds2.";
RL Mol. Cell. Biol. 27:7895-7905(2007).
RN [12]
RP FUNCTION.
RX PubMed=18683633;
RA Moreno I., Tutrone N., Sentandreu R., Valentin E.;
RT "Saccharomyces cerevisiae Rds2 transcription factor involvement in cell
RT wall composition and architecture.";
RL Int. Microbiol. 11:57-63(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND THR-231, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Transcription factor which regulates the expression of genes
CC for gluconeogenesis, the TCA cycle, and glucose metabolism. Involved in
CC the cell wall remodeling process and drug resistance.
CC {ECO:0000269|PubMed:16652171, ECO:0000269|PubMed:17875938,
CC ECO:0000269|PubMed:18683633}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by SNF1 in absence of glucose. The phosphorylation
CC is required for induction of transcription of gluconeogenic genes.
CC {ECO:0000269|PubMed:17875938}.
CC -!- DISRUPTION PHENOTYPE: Sensitivity to ketoconazole.
CC {ECO:0000269|PubMed:11943786}.
CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U43703; AAB68226.1; -; Genomic_DNA.
DR EMBL; AY693168; AAT93187.1; -; Genomic_DNA.
DR EMBL; X55731; CAA39262.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11300.1; -; Genomic_DNA.
DR PIR; S69051; S69051.
DR RefSeq; NP_015192.1; NM_001183947.1.
DR AlphaFoldDB; P19541; -.
DR BioGRID; 36048; 52.
DR DIP; DIP-1515N; -.
DR IntAct; P19541; 5.
DR MINT; P19541; -.
DR STRING; 4932.YPL133C; -.
DR iPTMnet; P19541; -.
DR MaxQB; P19541; -.
DR PaxDb; P19541; -.
DR PRIDE; P19541; -.
DR EnsemblFungi; YPL133C_mRNA; YPL133C; YPL133C.
DR GeneID; 855970; -.
DR KEGG; sce:YPL133C; -.
DR SGD; S000006054; RDS2.
DR VEuPathDB; FungiDB:YPL133C; -.
DR eggNOG; ENOG502QQGC; Eukaryota.
DR GeneTree; ENSGT00940000176385; -.
DR HOGENOM; CLU_010748_0_1_1; -.
DR InParanoid; P19541; -.
DR OMA; TRCVKRN; -.
DR BioCyc; YEAST:G3O-34032-MON; -.
DR PRO; PR:P19541; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P19541; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:0061415; P:negative regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0061414; P:positive regulation of transcription from RNA polymerase II promoter by a nonfermentable carbon source; IMP:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR035965; PAS-like_dom_sf.
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; SSF55785; SSF55785; 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 wall biogenesis/degradation; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..446
FT /note="Regulator of drug sensitivity 2"
FT /id="PRO_0000115006"
FT DNA_BIND 15..45
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 52..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 446 AA; 50082 MW; C78D3632DDCC3EA0 CRC64;
MSANSGVKRA SKAFKTCLFC KRSHVVCDKQ RPCSRCVKRD IAHLCREDDI AVPNEMPSQH
ESSPNDNNIQ GKYANKAHTG IPSDYQNEPV NKSGSTYGEE LSPKLDSSLV NDTTSLLLPQ
QPVFVSENVG SEFSSLNEFL SMLENPLLTQ TSLSSSSASN VHLENGSQTT QSPLEYQNDN
RRDEIGVARQ ENRSPTIMSG SSNSISKGDK QDQEKEESRI LANANENSAP TPKEQFFLTA
ADPSTEMTPE HRLKLVINAK LEAGLLKPYN YAKGYARLQD YMDKYMNQSS KQRILKPLST
IRPAFRTIAR SLKDVDLVLV EESFERMLLS YDRVFTSMSM PACLCRRTGE IYRANKEFAS
LVDCTVDDLR DGKLAIYELM TEESAVNFWE KYGSIAFDKG QKAVLTSCSL RTKDGIRKRP
CCFSFTIRRD RYNIPICIVG NFIPLS
