ZDS2_YEAST
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 03-AUG-2022, entry version 160.
DE RecName: Full=Protein ZDS2;
GN Name=ZDS2; Synonyms=MCS1; OrderedLocusNames=YML109W; 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; 107.
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; P54786; -.
DR PRIDE; P54786; -.
DR EnsemblFungi; YML109W_mRNA; YML109W; YML109W.
DR GeneID; 854931; -.
DR KEGG; sce:YML109W; -.
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 BioCyc; YEAST:G3O-32692-MON; -.
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 assembly; 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; PTHR28089; 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
