CET1_YEAST
ID CET1_YEAST Reviewed; 549 AA.
AC O13297; D6W3E2; Q12197;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=mRNA-capping enzyme subunit beta;
DE EC=3.6.1.74 {ECO:0000269|PubMed:6094533};
DE AltName: Full=mRNA 5'-phosphatase;
DE AltName: Full=mRNA 5'-triphosphate monophosphatase;
GN Name=CET1; OrderedLocusNames=YPL228W; ORFNames=P1433;
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 26109 / X2180;
RX PubMed=9345280; DOI=10.1006/bbrc.1997.7439;
RA Tsukamoto T., Shibagaki Y., Imajoh-Ohmi S., Murakoshi T., Suzuki M.,
RA Nakamura A., Gotoh H., Mizumoto K.;
RT "Isolation and characterization of the yeast mRNA capping enzyme beta
RT subunit gene encoding RNA 5'-triphosphatase, which is essential for cell
RT viability.";
RL Biochem. Biophys. Res. Commun. 239:116-122(1997).
RN [2]
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 [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 SUBUNIT.
RX PubMed=6389537; DOI=10.1016/s0021-9258(18)89833-7;
RA Itoh N., Mizumoto K., Kaziro Y.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I.
RT Purification and subunit structure.";
RL J. Biol. Chem. 259:13923-13929(1984).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6094533; DOI=10.1016/s0021-9258(18)89834-9;
RA Itoh N., Mizumoto K., Kaziro Y.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II.
RT Catalytic properties.";
RL J. Biol. Chem. 259:13930-13936(1984).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=3029058; DOI=10.1016/s0021-9258(18)61609-6;
RA Itoh N., Yamada H., Kaziro Y., Mizumoto K.;
RT "Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large
RT scale purification, subunit functions, and subcellular localization.";
RL J. Biol. Chem. 262:1989-1995(1987).
RN [7]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-280; ILE-520; PHE-523 AND
RP LEU-524.
RX PubMed=12788946; DOI=10.1074/jbc.m303060200;
RA Hausmann S., Pei Y., Shuman S.;
RT "Homodimeric quaternary structure is required for the in vivo function and
RT thermal stability of Saccharomyces cerevisiae and Schizosaccharomyces pombe
RT RNA triphosphatases.";
RL J. Biol. Chem. 278:30487-30496(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-124, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-124, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 241-549.
RX PubMed=10589681; DOI=10.1016/s0092-8674(00)81541-x;
RA Lima C.D., Wang L.K., Shuman S.;
RT "Structure and mechanism of yeast RNA triphosphatase: an essential
RT component of the mRNA capping apparatus.";
RL Cell 99:533-543(1999).
CC -!- FUNCTION: First step of mRNA capping. Converts the 5'-triphosphate end
CC of a nascent mRNA chain into a diphosphate end.
CC {ECO:0000269|PubMed:12788946, ECO:0000269|PubMed:3029058,
CC ECO:0000269|PubMed:6094533}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC diphospho-ribonucleoside in mRNA + H(+) + phosphate;
CC Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC Evidence={ECO:0000269|PubMed:6094533};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC Evidence={ECO:0000269|PubMed:6094533};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:6094533};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for pppA-poly(A) {ECO:0000269|PubMed:6094533};
CC pH dependence:
CC Optimum pH is 6.5-8.5. {ECO:0000269|PubMed:6094533};
CC -!- SUBUNIT: Heterodimer (PubMed:6389537, PubMed:3029058). The mRNA-capping
CC enzyme is composed of two separate chains alpha and beta, respectively
CC a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase
CC (PubMed:6389537, PubMed:3029058, PubMed:12788946).
CC {ECO:0000269|PubMed:12788946, ECO:0000269|PubMed:3029058,
CC ECO:0000269|PubMed:6389537}.
CC -!- INTERACTION:
CC O13297; Q01159: CEG1; NbExp=9; IntAct=EBI-4473, EBI-10503;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 3900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the fungal TPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB008799; BAA23522.1; -; Genomic_DNA.
DR EMBL; Z73584; CAA97944.1; -; Genomic_DNA.
DR EMBL; Z73583; CAA97943.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64259.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11208.1; -; Genomic_DNA.
DR PIR; S61706; S61706.
DR RefSeq; NP_015096.1; NM_001184042.1.
DR PDB; 1D8H; X-ray; 2.00 A; A/B/C=241-549.
DR PDB; 1D8I; X-ray; 2.05 A; A/B/C=241-549.
DR PDB; 3KYH; X-ray; 3.00 A; A/B=241-549.
DR PDBsum; 1D8H; -.
DR PDBsum; 1D8I; -.
DR PDBsum; 3KYH; -.
DR AlphaFoldDB; O13297; -.
DR SMR; O13297; -.
DR BioGRID; 35957; 512.
DR ComplexPortal; CPX-580; mRNA cap methyltransferase complex.
DR DIP; DIP-2299N; -.
DR IntAct; O13297; 5.
DR MINT; O13297; -.
DR STRING; 4932.YPL228W; -.
DR iPTMnet; O13297; -.
DR MaxQB; O13297; -.
DR PaxDb; O13297; -.
DR PRIDE; O13297; -.
DR EnsemblFungi; YPL228W_mRNA; YPL228W; YPL228W.
DR GeneID; 855873; -.
DR KEGG; sce:YPL228W; -.
DR SGD; S000006149; CET1.
DR VEuPathDB; FungiDB:YPL228W; -.
DR eggNOG; ENOG502RZAX; Eukaryota.
DR HOGENOM; CLU_037653_0_0_1; -.
DR InParanoid; O13297; -.
DR OMA; DWVYATI; -.
DR BioCyc; MetaCyc:G3O-34116-MON; -.
DR BioCyc; YEAST:G3O-34116-MON; -.
DR BRENDA; 3.6.1.74; 984.
DR EvolutionaryTrace; O13297; -.
DR PRO; PR:O13297; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; O13297; protein.
DR GO; GO:0031533; C:mRNA cap methyltransferase complex; IGI:SGD.
DR GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IDA:SGD.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:ComplexPortal.
DR GO; GO:0098507; P:polynucleotide 5' dephosphorylation; IBA:GO_Central.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR CDD; cd07470; CYTH-like_mRNA_RTPase; 1.
DR Gene3D; 3.20.100.10; -; 1.
DR InterPro; IPR040343; Cet1/Ctl1.
DR InterPro; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004206; mRNA_triPase_Cet1.
DR InterPro; IPR037009; mRNA_triPase_Cet1_sf.
DR PANTHER; PTHR28118; PTHR28118; 1.
DR Pfam; PF02940; mRNA_triPase; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; mRNA capping; mRNA processing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..549
FT /note="mRNA-capping enzyme subunit beta"
FT /id="PRO_0000210119"
FT REGION 30..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="N6-GMP-lysine intermediate"
FT SITE 280
FT /note="Essential for dimer formation"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 280
FT /note="D->A: Significant growth defects."
FT /evidence="ECO:0000269|PubMed:12788946"
FT MUTAGEN 520
FT /note="I->A: No growth."
FT /evidence="ECO:0000269|PubMed:12788946"
FT MUTAGEN 523
FT /note="F->A: Temperature sensitive growth phenotype."
FT /evidence="ECO:0000269|PubMed:12788946"
FT MUTAGEN 524
FT /note="L->A: Temperature sensitive growth phenotype."
FT /evidence="ECO:0000269|PubMed:12788946"
FT CONFLICT 242
FT /note="R -> K (in Ref. 1; BAA23522)"
FT /evidence="ECO:0000305"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1D8H"
FT TURN 254..258
FT /evidence="ECO:0007829|PDB:3KYH"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:1D8H"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1D8H"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 368..381
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 391..400
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 405..418
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 425..435
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:3KYH"
FT HELIX 441..445
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:1D8I"
FT STRAND 453..463
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 468..477
FT /evidence="ECO:0007829|PDB:1D8H"
FT STRAND 488..497
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:1D8H"
FT TURN 508..511
FT /evidence="ECO:0007829|PDB:1D8H"
FT HELIX 514..536
FT /evidence="ECO:0007829|PDB:1D8H"
SQ SEQUENCE 549 AA; 61850 MW; 2B946CC53D66F824 CRC64;
MSYTDNPPQT KRALSLDDLV NHDENEKVKL QKLSEAANGS RPFAENLESD INQTETGQAA
PIDNYKESTG HGSHSQKPKS RKSSNDDEET DTDDEMGASG EINFDSEMDF DYDKQHRNLL
SNGSPPMNDG SDANAKLEKP SDDSIHQNSK SDEEQRIPKQ GNEGNIASNY ITQVPLQKQK
QTEKKIAGNA VGSVVKKEEE ANAAVDNIFE EKATLQSKKN NIKRDLEVLN EISASSKPSK
YRNVPIWAQK WKPTIKALQS INVKDLKIDP SFLNIIPDDD LTKSVQDWVY ATIYSIAPEL
RSFIELEMKF GVIIDAKGPD RVNPPVSSQC VFTELDAHLT PNIDASLFKE LSKYIRGISE
VTENTGKFSI IESQTRDSVY RVGLSTQRPR FLRMSTDIKT GRVGQFIEKR HVAQLLLYSP
KDSYDVKISL NLELPVPDND PPEKYKSQSP ISERTKDRVS YIHNDSCTRI DITKVENHNQ
NSKSRQSETT HEVELEINTP ALLNAFDNIT NDSKEYASLI RTFLNNGTII RRKLSSLSYE
IFEGSKKVM
