DIG1_YEAST
ID DIG1_YEAST Reviewed; 452 AA.
AC Q03063; D6W3W5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Down-regulator of invasive growth 1;
DE AltName: Full=Regulator of STE12 protein 1;
DE AltName: Full=Regulator of sterile twelve 1;
GN Name=DIG1; Synonyms=RST1; OrderedLocusNames=YPL049C; ORFNames=P7102.02;
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 FUNCTION, INTERACTION WITH STE12 AND KSS1, AND PHOSPHORYLATION BY KSS1.
RX PubMed=8918885; DOI=10.1101/gad.10.22.2831;
RA Cook J.G., Bardwell L., Kron S.J., Thorner J.;
RT "Two novel targets of the MAP kinase Kss1 are negative regulators of
RT invasive growth in the yeast Saccharomyces cerevisiae.";
RL Genes Dev. 10:2831-2848(1996).
RN [4]
RP FUNCTION, COMPLEX WITH DIG2; FUS3 AND STE12, AND INTERACTION WITH CLN1 AND
RP CLN2.
RX PubMed=9094309; DOI=10.1016/s0960-9822(06)00118-7;
RA Tedford K., Kim S., Sa D., Stevens K., Tyers M.;
RT "Regulation of the mating pheromone and invasive growth responses in yeast
RT by two MAP kinase substrates.";
RL Curr. Biol. 7:228-238(1997).
RN [5]
RP FUNCTION, AND COMPLEX WITH DIG2; KSS1 AND STE12.
RX PubMed=9744865; DOI=10.1101/gad.12.18.2887;
RA Bardwell L., Cook J.G., Voora D., Baggott D.M., Martinez A.R., Thorner J.;
RT "Repression of yeast Ste12 transcription factor by direct binding of
RT unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK.";
RL Genes Dev. 12:2887-2898(1998).
RN [6]
RP FUNCTION.
RX PubMed=9860980; DOI=10.1073/pnas.95.26.15400;
RA Bardwell L., Cook J.G., Zhu-Shimoni J.X., Voora D., Thorner J.;
RT "Differential regulation of transcription: repression by unactivated
RT mitogen-activated protein kinase Kss1 requires the Dig1 and Dig2
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15400-15405(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH STE12.
RX PubMed=10825185; DOI=10.1128/mcb.20.12.4199-4209.2000;
RA Olson K.A., Nelson C., Tai G., Hung W., Yong C., Astell C., Sadowski I.;
RT "Two regulators of Ste12p inhibit pheromone-responsive transcription by
RT separate mechanisms.";
RL Mol. Cell. Biol. 20:4199-4209(2000).
RN [8]
RP FUNCTION, PHOSPHORYLATION BY FUS3, AND REPRESSION OF HAPLOID SPECIFIC AND
RP A-SPECIFIC GENES.
RX PubMed=12410840; DOI=10.1046/j.1365-2958.2002.03213.x;
RA Gelli A.;
RT "Rst1 and Rst2 are required for the a/alpha diploid cell type in yeast.";
RL Mol. Microbiol. 46:845-854(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH STE12.
RX PubMed=12732146; DOI=10.1016/s0092-8674(03)00301-5;
RA Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L.,
RA Fink G.R., Young R.A.;
RT "Program-specific distribution of a transcription factor dependent on
RT partner transcription factor and MAPK signaling.";
RL Cell 113:395-404(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-275, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-272; SER-330 AND
RP SER-428, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-126; SER-272 AND
RP THR-379, AND 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: DIG1 and DIG2 are negative regulators of the filamentation
CC and pheromone induced mating program. DIG1 and DIG2 inhibit the
CC transcriptional activity of STE12 by direct protein-protein
CC interaction. DIG1 colocalizes to promoters with STE12 and redistributes
CC with it during induction of filamentation (by butanol) or mating (by
CC pheromone) to program specific genes, but binding of DIG1 to STE12 is
CC reduced by pheromone treatment. {ECO:0000269|PubMed:10825185,
CC ECO:0000269|PubMed:12410840, ECO:0000269|PubMed:12732146,
CC ECO:0000269|PubMed:8918885, ECO:0000269|PubMed:9094309,
CC ECO:0000269|PubMed:9744865, ECO:0000269|PubMed:9860980}.
CC -!- SUBUNIT: Forms a complex with DIG2, STE12 and either FUS3 or KSS1. The
CC interaction of FUS3 with STE12 depends on the presence of both DIG1 and
CC DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after pheromone
CC treatment. DIG1 and DIG2 have also been reported to interact with CLN1
CC and CLN2.
CC -!- INTERACTION:
CC Q03063; Q03373: DIG2; NbExp=5; IntAct=EBI-29752, EBI-34019;
CC Q03063; P14681: KSS1; NbExp=5; IntAct=EBI-29752, EBI-9945;
CC Q03063; P13574: STE12; NbExp=6; IntAct=EBI-29752, EBI-18264;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by FUS3 and KSS1, in a pheromone-stimulated manner.
CC Phosphorylation reduces the affinity for STE12.
CC {ECO:0000269|PubMed:12410840, ECO:0000269|PubMed:8918885}.
CC -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD medium
CC (5480 according to TAP-tag study). {ECO:0000269|PubMed:14562106}.
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DR EMBL; U44030; AAB68172.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11381.1; -; Genomic_DNA.
DR PIR; S62027; S62027.
DR RefSeq; NP_015276.1; NM_001183863.1.
DR AlphaFoldDB; Q03063; -.
DR BioGRID; 36131; 235.
DR ComplexPortal; CPX-575; Ste12/Dig1/Dig2 transcription regulation complex.
DR ComplexPortal; CPX-576; Tec1/Ste12/Dig1 transcription regulation complex.
DR DIP; DIP-1291N; -.
DR IntAct; Q03063; 64.
DR MINT; Q03063; -.
DR STRING; 4932.YPL049C; -.
DR iPTMnet; Q03063; -.
DR MaxQB; Q03063; -.
DR PaxDb; Q03063; -.
DR PRIDE; Q03063; -.
DR EnsemblFungi; YPL049C_mRNA; YPL049C; YPL049C.
DR GeneID; 856058; -.
DR KEGG; sce:YPL049C; -.
DR SGD; S000005970; DIG1.
DR VEuPathDB; FungiDB:YPL049C; -.
DR eggNOG; ENOG502S5RS; Eukaryota.
DR HOGENOM; CLU_621344_0_0_1; -.
DR InParanoid; Q03063; -.
DR OMA; RSSWHEA; -.
DR BioCyc; YEAST:G3O-33962-MON; -.
DR PRO; PR:Q03063; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q03063; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990526; C:Ste12p-Dig1p-Dig2p complex; IDA:SGD.
DR GO; GO:1990527; C:Tec1p-Ste12p-Dig1p complex; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:2000218; P:negative regulation of invasive growth in response to glucose limitation; IGI:SGD.
DR GO; GO:0045894; P:negative regulation of mating-type specific transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:2000221; P:negative regulation of pseudohyphal growth; IGI:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0010570; P:regulation of filamentous growth; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..452
FT /note="Down-regulator of invasive growth 1"
FT /id="PRO_0000079897"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..452
FT /note="Interaction with FUS3 and KSS1"
FT /evidence="ECO:0000269|PubMed:8918885"
FT REGION 262..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 452 AA; 49356 MW; 2D27F9878BFADD30 CRC64;
MAVSARLRTT AEDTSIAKST QDPIGDTEIS VANAKGSSDS NIKNSPGGNS VGQESELEHV
PEEDDSGDKE ADHEDSETAT AKKRKAQPLK NPKKSLKRGR VPAPLNLSDS NTNTHGGNIK
DGNLASSNSA HFPPVANQNV KSAPAQVTQH SKFQPRVQYL GKASSRQSIQ VNNSSNSYGK
PHMPSAGIMS AMNPYMPMNR YIMSPYYNPY GIPPPHMLNK PIMTPYVSYP YPMGPRTSIP
YAMQGGNARP YEENEYSASN YRNKRVNDSY DSPLSGTAST GKTRRSEEGS RNSSVGSSAN
AGPTQQRADL RPADMIPAEE YHFERDALLS ANTKARSAST STSTSTSTNR DRSSWHEAEP
NKDEEEGTDL AIEDGAVPTP TFTTFQRTSQ PQQQSPSLLQ GEIRLSSHIF AFEFPLSSSN
VDKKMFMSIC NKVWNESKEL TKKSSSHHRT GK
