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   27-MAR-2024, entry version 193.
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; 53.
DR   DIP; DIP-1515N; -.
DR   IntAct; P19541; 5.
DR   MINT; P19541; -.
DR   STRING; 4932.YPL133C; -.
DR   iPTMnet; P19541; -.
DR   MaxQB; P19541; -.
DR   PaxDb; 4932-YPL133C; -.
DR   PeptideAtlas; P19541; -.
DR   EnsemblFungi; YPL133C_mRNA; YPL133C; YPL133C.
DR   GeneID; 855970; -.
DR   KEGG; sce:YPL133C; -.
DR   AGR; SGD:S000006054; -.
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; RWMDSNV; -.
DR   OrthoDB; 2562146at2759; -.
DR   BioCyc; YEAST:G3O-34032-MONOMER; -.
DR   BioGRID-ORCS; 855970; 2 hits in 13 CRISPR screens.
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; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   PANTHER; PTHR31986; REGULATOR OF DRUG SENSITIVITY 2; 1.
DR   PANTHER; PTHR31986:SF7; REGULATOR OF DRUG SENSITIVITY 2; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 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
//