ZDS1_YEAST
ID ZDS1_YEAST Reviewed; 915 AA.
AC P50111; D6W0A0; P41373;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein ZDS1;
DE AltName: Full=Protein NRC1;
DE AltName: Full=RT2GS1;
GN Name=ZDS1; Synonyms=CES1, CKM1, HST1, NRC1, OSS1, STM2;
GN OrderedLocusNames=YMR273C; ORFNames=YM8156.15C;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=8816439; DOI=10.1128/mcb.16.10.5264;
RA Bi E., Pringle J.R.;
RT "ZDS1 and ZDS2, genes whose products may regulate Cdc42p in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 16:5264-5275(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8836740;
RA Schwer B., Shuman S.;
RT "Multicopy suppressors of temperature-sensitive mutations of yeast mRNA
RT capping enzyme.";
RL Gene Expr. 5:331-344(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8647431; DOI=10.1101/gad.10.11.1327;
RA Ma X.-J., Lu Q., Grunstein M.;
RT "A search for proteins that interact genetically with histone H3 and H4
RT amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 10:1327-1340(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=COP161U7;
RA Jia Y., Li J.-P., Butow R.A.;
RT "RTG2S1 over expression suppresses mrtg2-5 in the CIT2 retrograde pathway
RT in yeast.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Linder P.;
RL Submitted (AUG-1994) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RAY-3A;
RX PubMed=8918228; DOI=10.1016/0378-1119(96)00204-1;
RA Tsuchiya E., Matsuzaki G., Kurano K., Fukuchi T., Tsukao A., Miyakawa T.;
RT "The Saccharomyces cerevisiae SSD1 gene is involved in the tolerance to
RT high concentration of Ca2+ with the participation of HST1/NRC1/BFR1.";
RL Gene 176:35-38(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [8]
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 [9]
RP INTERACTION WITH SKG6.
RX PubMed=11489916; DOI=10.1083/jcb.200104057;
RA Drees B.L., Sundin B.A., Brazeau E., Caviston J.P., Chen G.-C., Guo W.,
RA Kozminski K.G., Lau M.W., Moskow J.J., Tong A., Schenkman L.R.,
RA McKenzie A. III, Brennwald P.J., Longtine M., Bi E., Chan C., Novick P.,
RA Boone C., Pringle J.R., Davis T.N., Fields S., Drubin D.G.;
RT "A protein interaction map for cell polarity development.";
RL J. Cell Biol. 154:549-571(2001).
RN [10]
RP INTERACTION WITH BCY1.
RX PubMed=11134339; DOI=10.1128/mcb.21.2.511-523.2001;
RA Griffioen G., Branduardi P., Ballarini A., Anghileri P., Norbeck J.,
RA Baroni M.D., Ruis H.;
RT "Nucleocytoplasmic distribution of budding yeast protein kinase A
RT regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent
RT phosphorylation of its targeting domain.";
RL Mol. Cell. Biol. 21:511-523(2001).
RN [11]
RP FUNCTION.
RX PubMed=12704202; DOI=10.1074/jbc.m210691200;
RA Griffioen G., Swinnen S., Thevelein J.M.;
RT "Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3
RT phosphorylation of a cAMP-dependent protein kinase regulatory subunit.";
RL J. Biol. Chem. 278:23460-23471(2003).
RN [12]
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 [13]
RP FUNCTION.
RX PubMed=16157662; DOI=10.1534/genetics.105.048082;
RA Zanelli C.F., Valentini S.R.;
RT "Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity
RT defects of a yeast eIF5A mutant.";
RL Genetics 171:1571-1581(2005).
RN [14]
RP FUNCTION IN MRNA EXPORT, AND INTERACTION WITH DBP5 AND GFD1.
RX PubMed=15619606; DOI=10.1074/jbc.m413025200;
RA Estruch F., Hodge C.A., Rodriguez-Navarro S., Cole C.N.;
RT "Physical and genetic interactions link the yeast protein Zds1p with mRNA
RT nuclear export.";
RL J. Biol. Chem. 280:9691-9697(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
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: Has a role in establishing cell polarity. Together with cAMP-
CC dependent protein kinase regulatory subunit BCY1, provides a negative
CC feedback control on the cell wall integrity-signaling pathway by acting
CC as a negative regulator of MAP kinase SLT2/MPK1. In heat-stressed cells
CC appears to play a role in localizing BCY1 to the cytoplasm. Seems to
CC interact with, and down-regulate, CDC42. Also acts as a suppressor of
CC PKC1. May act as an integration point for distinct signaling pathways
CC helping to maintain a balance among these different pathways.
CC -!- FUNCTION: When associated with DBP5, GFD1 and nucleoporins at the
CC cytosolic fibrils of the nuclear pore complex, is required for mRNA
CC export form the nucleus.
CC -!- SUBUNIT: Interacts with BCY1, DBP5, GFD1 and SKG6.
CC {ECO:0000269|PubMed:11134339, ECO:0000269|PubMed:11489916,
CC ECO:0000269|PubMed:15619606}.
CC -!- INTERACTION:
CC P50111; P20449: DBP5; NbExp=3; IntAct=EBI-29626, EBI-5617;
CC P50111; Q04839: GFD1; NbExp=3; IntAct=EBI-29626, EBI-27549;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8816439}.
CC Note=Concentrated at incipient bud site of unbudded cells and at the
CC bud tip of small and medium-sized buds.
CC -!- MISCELLANEOUS: 'ZDS' means 'zillion different screens' as both ZDS1 and
CC ZDS2 have been found by a wide variety of genetic screens.
CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast ZDS2/MCS1. {ECO:0000305}.
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DR EMBL; L42821; AAB38423.1; -; Genomic_DNA.
DR EMBL; U32580; AAA74626.1; -; Genomic_DNA.
DR EMBL; U63849; AAB49281.1; -; Genomic_DNA.
DR EMBL; U65682; AAB06617.1; -; Genomic_DNA.
DR EMBL; D50276; BAA08819.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89256.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10174.1; -; Genomic_DNA.
DR PIR; S54485; S54485.
DR RefSeq; NP_014000.1; NM_001182780.1.
DR AlphaFoldDB; P50111; -.
DR SMR; P50111; -.
DR BioGRID; 35452; 188.
DR DIP; DIP-5774N; -.
DR IntAct; P50111; 19.
DR MINT; P50111; -.
DR STRING; 4932.YMR273C; -.
DR iPTMnet; P50111; -.
DR MaxQB; P50111; -.
DR PaxDb; P50111; -.
DR PRIDE; P50111; -.
DR EnsemblFungi; YMR273C_mRNA; YMR273C; YMR273C.
DR GeneID; 855316; -.
DR KEGG; sce:YMR273C; -.
DR SGD; S000004886; ZDS1.
DR VEuPathDB; FungiDB:YMR273C; -.
DR eggNOG; ENOG502S5WJ; Eukaryota.
DR GeneTree; ENSGT00940000176802; -.
DR HOGENOM; CLU_011999_0_0_1; -.
DR InParanoid; P50111; -.
DR OMA; INNTMTW; -.
DR BioCyc; YEAST:G3O-32944-MON; -.
DR PRO; PR:P50111; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50111; protein.
DR GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IMP:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR InterPro; IPR040206; Zds1/2.
DR InterPro; IPR013941; ZDS1_C.
DR PANTHER; PTHR28089; PTHR28089; 1.
DR Pfam; PF08632; Zds_C; 1.
DR SMART; SM01327; Zds_C; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Cytoplasm; mRNA transport;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..915
FT /note="Protein ZDS1"
FT /id="PRO_0000066569"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 84
FT /note="S -> P (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="D -> E (in Ref. 2; AAA74626)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="S -> C (in Ref. 2; AAA74626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 915 AA; 103358 MW; E5F4C2117DBE1210 CRC64;
MSNRDNESML RTTSSDKAIA SQRDKRKSEV LIAAQSLDNE IRSVKNLKRL SIGSMDLLID
PELDIKFGGE SSGRRSWSGT TSSSASMPSD TTTVNNTRYS DPTPLENLHG RGNSGIESSN
KTKQGNYLGI KKGVHSPSRK LNANVLKKNL LWVPANQHPN VKPDNFLELV QDTLQNIQLS
DNGEDNDGNS NENNDIEDNG EDKESQSYEN KENNTINLNR GLSRHGNASL IRRPSTLRRS
YTEFDDNEDD DNKGDSASET VNKVEERISK IKERPVSLRD ITEELTKISN SAGLTDNDAI
TLARTLSMAG SYSDKKDQPQ PEGHYDEGDI GFSTSQANTL DDGEFASNMP INNTMTWPER
SSLRRSRFNT YRIRSQEQEK EVEQSVDEMK NDDEERLKLT KNTIKVEIDP HKSPFRQQDE
DSENMSSPGS IGDFQDIYNH YRQSSGEWEQ EMGIEKEAEE VPVKVRNDTV EQDLELREGT
TDMVKPSATD DNKETKRHRR RNGWTWLNNK MSREDDNEEN QGDDENEENV DSQRMELDNS
KKHYISLFNG GEKTEVSNKE EMNNSSTSTA TSQTRQKIEK TFANLFRRKP HHKHDASSSP
SSSPSSSPSI PNNDAVHVRV RKSKKLGNKS GREPVEPIVL RNRPRPHRHH HSRHGSQKIS
VKTLKDSQPQ QQIPLQPQLE GAIEIEKKEE SDSESLPQLQ PAVSVSSTKS NSRDREEEEA
KKKNKKRSNT TEISNQQHSK HVQKENTDEQ KAQLQAPAQE QVQTSVPVQA SAPVQNSAPV
QTSAPVEASA QTQAPAAPPL KHTSILPPRK LTFADVKKPD KPNSPVQFTD SAFGFPLPLL
TVSTVIMFDH RLPINVERAI YRLSHLKLSN SKRGLREQVL LSNFMYAYLN LVNHTLYMEQ
VAHDKEQQQQ QQQQP
