MDS3_YEAST
ID MDS3_YEAST Reviewed; 1487 AA.
AC P53094; D6VTV6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Negative regulator of sporulation MDS3;
DE AltName: Full=MCK1 dosage suppressor 3;
GN Name=MDS3; OrderedLocusNames=YGL197W; ORFNames=G1307;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046087;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT from Saccharomyces cerevisiae.";
RL Yeast 13:55-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 262-264 AND 403.
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 CHARACTERIZATION.
RX PubMed=9383076; DOI=10.1093/genetics/147.3.1351;
RA Benni M.L., Neigeborn L.;
RT "Identification of a new class of negative regulators affecting
RT sporulation-specific gene expression in yeast.";
RL Genetics 147:1351-1366(1997).
RN [5]
RP FUNCTION.
RX PubMed=12524333; DOI=10.1093/genetics/162.4.1573;
RA Davis D.A., Bruno V.M., Loza L., Filler S.G., Mitchell A.P.;
RT "Candida albicans Mds3p, a conserved regulator of pH responses and
RT virulence identified through insertional mutagenesis.";
RL Genetics 162:1573-1581(2002).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-693 AND SER-781, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621; SER-693; SER-698 AND
RP SER-904, AND 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).
RN [11]
RP FUNCTION.
RX PubMed=19087957; DOI=10.1534/genetics.108.098434;
RA McDonald C.M., Wagner M., Dunham M.J., Shin M.E., Ahmed N.T., Winter E.;
RT "The Ras/cAMP pathway and the CDK-like kinase Ime2 regulate the MAPK Smk1
RT and spore morphogenesis in Saccharomyces cerevisiae.";
RL Genetics 181:511-523(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-475; SER-621;
RP SER-693; SER-744; SER-747; SER-756; SER-757; SER-781; THR-785; SER-787;
RP SER-900; THR-930 AND SER-1187, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Negatively regulates early sporulation-specific genes. Seems
CC to exert its function by positively regulating the Ras/cAMP pathway.
CC Required for growth under alkaline conditions. Acts synergetically with
CC PMD1. {ECO:0000269|PubMed:12524333, ECO:0000269|PubMed:19087957}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X91837; CAA62947.1; -; Genomic_DNA.
DR EMBL; Z72719; CAA96909.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07917.2; -; Genomic_DNA.
DR PIR; S62048; S62048.
DR RefSeq; NP_011318.2; NM_001181062.2.
DR AlphaFoldDB; P53094; -.
DR BioGRID; 33060; 157.
DR DIP; DIP-6381N; -.
DR IntAct; P53094; 25.
DR MINT; P53094; -.
DR STRING; 4932.YGL197W; -.
DR iPTMnet; P53094; -.
DR MaxQB; P53094; -.
DR PaxDb; P53094; -.
DR PRIDE; P53094; -.
DR EnsemblFungi; YGL197W_mRNA; YGL197W; YGL197W.
DR GeneID; 852678; -.
DR KEGG; sce:YGL197W; -.
DR SGD; S000003165; MDS3.
DR VEuPathDB; FungiDB:YGL197W; -.
DR eggNOG; ENOG502QSQ9; Eukaryota.
DR GeneTree; ENSGT00940000176594; -.
DR HOGENOM; CLU_252311_0_0_1; -.
DR InParanoid; P53094; -.
DR OMA; SGGMVFR; -.
DR BioCyc; YEAST:G3O-30678-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P53094; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53094; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0075297; P:negative regulation of ascospore formation; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0031929; P:TOR signaling; IMP:SGD.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kelch repeat; Meiosis; Phosphoprotein; Reference proteome;
KW Repeat; Sporulation.
FT CHAIN 1..1487
FT /note="Negative regulator of sporulation MDS3"
FT /id="PRO_0000119137"
FT REPEAT 171..226
FT /note="Kelch 1"
FT REPEAT 234..287
FT /note="Kelch 2"
FT REPEAT 371..419
FT /note="Kelch 3"
FT REGION 639..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 930
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 262..264
FT /note="QSE -> HPK (in Ref. 1; CAA62947 and 2; CAA96909)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="A -> R (in Ref. 1; CAA62947 and 2; CAA96909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1487 AA; 166971 MW; 31073D68ACA4AF61 CRC64;
MPLLQPSTCF CYPLKLPPLP LTSDSNEFDE CARKRLTLDY RTGSAVTLTR SNIFVHGGLT
IPLNLPVVNS MQLQKELILF FAKEKNNGSS FRNLNEWISK ETFFLDLMSR TWYRVKTSFD
QRTEELLKAE SSSAKADNDT NEIRTDIKKG KSLESPLKER LFHSLCYLDG CLYIFGGLTV
SPQSGYELIA TNELWKLDLN TKKWSLLSDD PQIARRFNHT MHVKNENNDN RDTKLIIVGG
LNNMDQPVKK IDIYNISQNC WQSETIPKQP MEITTNVNGI PLALSKDQNF SILVENNEAN
VPALAFYMRS DQIDEYLGKD SSKIKENSPI VALPLLSESQ GIRMPSNPAL PKKLLNVPYE
LLAPTGDYFG FNIIIGGFHP NYQSSNFHCF IYDINSGKWS RVATACPDCD INKHRFWRVF
VWKSHHQTIL LGTKTDDYYS PSVQRFDHLS TFGLPLVNIF NKTIQLPHHK ISASSLPIPI
ENFAKHKDTP LKKVSFTSSA TSQFENYIRY IAPPLEMSSI QSVFPPYAMV LGKDALEIYG
KPLSDFEFIT SEGDSIGIPC YLLRKRWGRY FDMLLSQSYT KVCADYETTD TQSTLIKFSP
HSSRNSSKAV RQEGRLSSSG SLDNYFEKNF PIFARTSVSE AQNTQPQVAN ADAKAPNTPS
TSDEPSSSSS SDLYSTPHYQ RNNDEEDDED PVSPKPVSKS NSIYRPIRKT ESSSTTSSSN
GMIFRVPFKE KAAVTSNTEA LLESNLSLQE LSRRRSSLMS IPSGELLRSS ISEAEHQRRA
SHPLTSSPLF EDSGTPCGKQ LQQLQQHTIQ NPHNHLSPRR FSRSARSSIS YVSSSSDRRG
NSISSRSTSD SFGTPPVLGV LNVPLPPQTR EPNEPPPPCP AMSTGSNTRR SNTLTDYMHS
NKASPFSSRR SSHIGRRSST PETENAFSAT PRASLDGQML GKSLKEGSTS QYTQPRMNSF
PKANETIQTP TSSNNEWSRQ SVTSNTDSFD SLQSNFALEL EPLLTPRSLY MPWPTSTVRA
FAEFFYTGQV NSKWLLAPVA LDLLVMAKIY EIPLLYKLIL EVLYSILAKK EESLSLICTS
LMETFRTKTL NSYKGDEEKT NTYLTSNDNY QELLKLKVSL ENIDNGYYDP DLLRKQSRAQ
SSSTQESSGS ANGEKTATGA GSLETSSTNV PTVFAGGPRD SHNSVGSIGF PNSMNIQGSR
RSTSGFSPRV KMKSSLSKEI DPKTFYEEYE PKEGKSFDDN DDQQTNIGSF NLHLFDMNYG
SISSSSTNSI SSSDLEEKEE QEQLQDLLEI EREDSAEILD ARFRNKEDDK VTKDISNDKK
RNYLPHEKNN LKAKEGKETR DVREEEEEFD FGLGMLSLNK IKREAKHVDK VDDSVDPLFK
SSAFPQSPIR AYGSTTRTSS ASGKPFRDNR SFNAFSVLTL ENMASANALP PVDYVIKSIY
RTTVLVNDIR LMVRCMDCIE LSKNLRALKK KTMEDISKLK GISKPSP
