MAF1_YEAST
ID MAF1_YEAST Reviewed; 395 AA.
AC P41910; D6VRZ3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Repressor of RNA polymerase III transcription MAF1;
GN Name=MAF1; OrderedLocusNames=YDR005C; ORFNames=YD8119.11C;
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=T8-1D;
RX PubMed=9055829; DOI=10.1016/s0378-1119(96)00669-5;
RA Boguta M., Czerska K., Zoladek T.;
RT "Mutation in a new gene MAF1 affects tRNA suppressor efficiency in
RT Saccharomyces cerevisiae.";
RL Gene 185:291-296(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION.
RX PubMed=12504022; DOI=10.1016/s1097-2765(02)00787-6;
RA Upadhya R., Lee J., Willis I.M.;
RT "Maf1 is an essential mediator of diverse signals that repress RNA
RT polymerase III transcription.";
RL Mol. Cell 10:1489-1494(2002).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-210, 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 [7]
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 [8]
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-347, AND
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).
RN [10]
RP PHOSPHORYLATION BY PKA.
RX PubMed=20702584; DOI=10.1091/mbc.e10-03-0182;
RA Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.;
RT "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein
RT kinase A toward some but not all substrates.";
RL Mol. Biol. Cell 21:3475-3486(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Mediator of diverse signals that repress RNA polymerase III
CC transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
CC {ECO:0000269|PubMed:12504022}.
CC -!- INTERACTION:
CC P41910; P32910: RPC34; NbExp=3; IntAct=EBI-10375, EBI-15835;
CC P41910; P04051: RPO31; NbExp=4; IntAct=EBI-10375, EBI-15810;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- PTM: Phosphorylated by PKA in a TORC1-dependent manner. Phosphorylation
CC at PKA consensus sites RRxS/T decreases upon rapamycin treatment.
CC {ECO:0000269|PubMed:20702584}.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MAF1 family. {ECO:0000305}.
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DR EMBL; U19492; AAB51655.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88065.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11853.1; -; Genomic_DNA.
DR PIR; S50986; S50986.
DR RefSeq; NP_010288.1; NM_001180313.1.
DR PDB; 6TUT; EM; 3.25 A; R=2-395.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P41910; -.
DR SMR; P41910; -.
DR BioGRID; 32058; 283.
DR DIP; DIP-5133N; -.
DR IntAct; P41910; 28.
DR MINT; P41910; -.
DR STRING; 4932.YDR005C; -.
DR iPTMnet; P41910; -.
DR MaxQB; P41910; -.
DR PaxDb; P41910; -.
DR PRIDE; P41910; -.
DR EnsemblFungi; YDR005C_mRNA; YDR005C; YDR005C.
DR GeneID; 851568; -.
DR KEGG; sce:YDR005C; -.
DR SGD; S000002412; MAF1.
DR VEuPathDB; FungiDB:YDR005C; -.
DR eggNOG; KOG3104; Eukaryota.
DR GeneTree; ENSGT00940000171523; -.
DR HOGENOM; CLU_037043_2_1_1; -.
DR InParanoid; P41910; -.
DR OMA; INIGPFG; -.
DR BioCyc; YEAST:G3O-29627-MON; -.
DR Reactome; R-SCE-8943724; Regulation of PTEN gene transcription.
DR PRO; PR:P41910; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41910; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000994; F:RNA polymerase III core binding; IDA:SGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR Gene3D; 3.40.1000.50; -; 1.
DR InterPro; IPR015257; Maf1.
DR InterPro; IPR038564; Maf1_sf.
DR PANTHER; PTHR22504; PTHR22504; 1.
DR Pfam; PF09174; Maf1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..395
FT /note="Repressor of RNA polymerase III transcription MAF1"
FT /id="PRO_0000213972"
FT REGION 69..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6TUT"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6TUT"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6TUT"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:6TUT"
SQ SEQUENCE 395 AA; 44733 MW; 1AE6262D0BEBBB1D CRC64;
MKFIDELDIE RVNQTLNFET NDCKIVGSCD IFTTKAVASD RKLYKTIDQH LDTILQENEN
YNATLQQQLA APETNQSPCS SPFYSNRRDS NSFWEQKRRI SFSEYNSNNN TNNSNGNSSN
NNNYSGPNGS SPATFPKSAK LNDQNLKELV SNYDSGSMSS SSLDSSSKND ERIRRRSSSS
ISSFKSGKSS NNNYSSGTAT NNVNKRRKSS INERPSNLSL GPFGPINEPS SRKIFAYLIA
ILNASYPDHD FSSVEPTDFV KTSLKTFISK FENTLYSLGR QPEEWVWEVI NSHMTLSDCV
LFQYSPSNSF LEDEPGYLWN LIGFLYNRKR KRVAYLYLIC SRLNSSTGEV EDALAKKPQG
KLIIDDGSNE YEGEYDFTYD ENVIDDKSDQ EESLQ
