ID   ZDS2_YEAST              Reviewed;         942 AA.
AC   P54786; D6W0H5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Protein ZDS2;
GN   Name=ZDS2; Synonyms=MCS1; OrderedLocusNames=YML109W;
GN   ORFNames=YM8339.10;
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].
RX   PubMed=8816438; DOI=10.1128/mcb.16.10.5254;
RA   Yu Y., Jiang Y.W., Wellinger R.J., Carlson K., Roberts J.M., Stillman D.J.;
RT   "Mutations in the homologous ZDS1 and ZDS2 genes affect cell cycle
RT   progression.";
RL   Mol. Cell. Biol. 16:5254-5263(1996).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, 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   [9]
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   [10]
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: Acts as a negative regulator of polarized growth via an
CC       alternative mechanism to ZDS1. In heat-stressed cells appears to play a
CC       role in localizing BCY1 to the cytoplasm. Seems to interact with, and
CC       down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an
CC       integration point for distinct signaling pathways helping to maintain a
CC       balance among these different pathways. {ECO:0000269|PubMed:12704202,
CC       ECO:0000269|PubMed:16157662}.
CC   -!- SUBUNIT: Interacts with SKG6. {ECO:0000269|PubMed:11489916}.
CC   -!- INTERACTION:
CC       P54786; P38041: BOI1; NbExp=3; IntAct=EBI-29637, EBI-3719;
CC       P54786; P32790: SLA1; NbExp=3; IntAct=EBI-29637, EBI-17313;
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 105 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: To yeast ZDS1/NRC1/CES1. {ECO:0000305}.
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DR   EMBL; U32938; AAB37541.1; -; Genomic_DNA.
DR   EMBL; Z49210; CAA89109.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09789.1; -; Genomic_DNA.
DR   PIR; S53963; S53963.
DR   RefSeq; NP_013598.1; NM_001182471.1.
DR   AlphaFoldDB; P54786; -.
DR   SMR; P54786; -.
DR   BioGRID; 35095; 112.
DR   DIP; DIP-1517N; -.
DR   IntAct; P54786; 57.
DR   MINT; P54786; -.
DR   STRING; 4932.YML109W; -.
DR   MoonDB; P54786; Predicted.
DR   CarbonylDB; P54786; -.
DR   iPTMnet; P54786; -.
DR   MaxQB; P54786; -.
DR   PaxDb; 4932-YML109W; -.
DR   PeptideAtlas; P54786; -.
DR   EnsemblFungi; YML109W_mRNA; YML109W; YML109W.
DR   GeneID; 854931; -.
DR   KEGG; sce:YML109W; -.
DR   AGR; SGD:S000004577; -.
DR   SGD; S000004577; ZDS2.
DR   VEuPathDB; FungiDB:YML109W; -.
DR   eggNOG; ENOG502RC08; Eukaryota.
DR   GeneTree; ENSGT00940000176802; -.
DR   HOGENOM; CLU_011999_0_0_1; -.
DR   InParanoid; P54786; -.
DR   OMA; QNLLWVP; -.
DR   OrthoDB; 1367409at2759; -.
DR   BioCyc; YEAST:G3O-32692-MONOMER; -.
DR   BioGRID-ORCS; 854931; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P54786; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P54786; 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:0030010; P:establishment of cell polarity; IGI:SGD.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:SGD.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IMP:SGD.
DR   GO; GO:0032880; P:regulation of protein localization; IGI:SGD.
DR   InterPro; IPR040206; Zds1/2.
DR   InterPro; IPR013941; ZDS1_C.
DR   PANTHER; PTHR28089; PROTEIN ZDS1-RELATED; 1.
DR   PANTHER; PTHR28089:SF1; PROTEIN ZDS1-RELATED; 1.
DR   Pfam; PF08632; Zds_C; 1.
DR   SMART; SM01327; Zds_C; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..942
FT                   /note="Protein ZDS2"
FT                   /id="PRO_0000066570"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..138
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   CONFLICT        7
FT                   /note="M -> V (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="T -> S (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        530
FT                   /note="A -> P (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="A -> G (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        633
FT                   /note="V -> A (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        668
FT                   /note="N -> S (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        711
FT                   /note="V -> VNC (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723
FT                   /note="Missing (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        729
FT                   /note="A -> E (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        833
FT                   /note="S -> P (in Ref. 1; AAB37541)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        914..942
FT                   /note="TGDIAFNGDSALGMMDKNDSDGTILIPDI -> HWRYSLQW (in Ref.
FT                   1; AAB37541)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   942 AA;  105496 MW;  A1C9DD9A539E4291 CRC64;
     MVLMEDMQNK DGHNTVENSS GGTDSNNNIQ MRRMRKTQLS KKELFEKRKS DVLIAAKSLD
     TEIQNVKNLK RLSIGSMDLV IDPELEFKVN SRNSYSSDSS KESLQESLHE ENIIRSEQKE
     EQGSEDNDAY EEGDATNVDD SIDITQTEYL HDEETLEKEK IIRNASSSTS SSARVTSRNR
     RLSGVKTLAH DVVLDVENDH DSKMVDLTQN LLWVPADQHP NVKPENYLEL IQDTLQNIQI
     STNQDIDENK LELGNNHVIS NRKRTGSVVR RPSRLKTSYT KFDDEPPLAD KPQEGEIQVD
     KRISSSDIKT IRSVSLKEIT EELTKISNNA GLTDSDAVTL ARSLSMSGSF TNESLHLNGN
     HTENDNEFAS NMFNETGLTI PERSSLRRSK FNTYKIRLEG SSLPQAVKLN SLMNIQTNDN
     RRSASSPASY TQVPQEQASL NDFHEIFDHY RRTSTDWSTE NEKYVDSTNY YSDEEDLTHA
     SISQESSLLS TDSSNNSVLI KPHNTGSMIS EKLDQHVSSS EKSNTNNSEA NHGWSWLNSS
     NGSLNANEQT YQQLTDDEDD EECVDNEKAD FVNLSVSRRA KSTKRASERI NHSKNRHSPI
     FQIHSEEAKS VVITPSVVSS SESQPSKPTA PAVVEKKVEL PTDTQASTHK KNSLEKRLAK
     LFKRKQHNGT CKSDVKVIKK SVKKELKKKA SHSSLSKFRK SPKKKPQEAE VERPSSPTKT
     ITTEDIDTAS VIEPEVRSSN ASTLLPDSHT SHSSEFVVET ISELDGDDSF DISGGDVNYD
     VEVHSSISRD TTAGLEEDIG AEREDNTSPT APQISTLPPR KLTFEDVVKP DYSNAPIKFT
     DSAFGFPLPM ITNSTVIMFD HRLGINVERA IYRLSHLKLS DPGRELRQQV LLSNFMYSYL
     NLVNHTLYME QVGTGDIAFN GDSALGMMDK NDSDGTILIP DI
//