IF4E_YEAST
ID IF4E_YEAST Reviewed; 213 AA.
AC P07260; D6W1T0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Eukaryotic translation initiation factor 4E;
DE Short=eIF-4E;
DE Short=eIF4E;
DE AltName: Full=eIF-4F 25 kDa subunit;
DE AltName: Full=mRNA cap-binding protein;
GN Name=CDC33; Synonyms=TIF45; OrderedLocusNames=YOL139C;
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=3550438; DOI=10.1128/mcb.7.3.998-1003.1987;
RA Altmann M., Handschin C., Trachsel H.;
RT "mRNA cap-binding protein: cloning of the gene encoding protein synthesis
RT initiation factor eIF-4E from Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:998-1003(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062383; DOI=10.1128/mcb.8.8.3556-3559.1988;
RA Brenner C., Nakayama N., Goebl M., Tanaka K., Toh-e A., Matsumoto K.;
RT "CDC33 encodes mRNA cap-binding protein eIF-4E of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 8:3556-3559(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2685552; DOI=10.1128/mcb.9.10.4467-4472.1989;
RA Altmann M., Sonenberg N., Trachsel H.;
RT "Translation in Saccharomyces cerevisiae: initiation factor 4E-dependent
RT cell-free system.";
RL Mol. Cell. Biol. 9:4467-4472(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7502581; DOI=10.1002/yea.320111107;
RA Casas C., Aldea M., Casamayor A., Lafuente M.J., Gamo F.J., Gancedo C.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 9873 bp fragment of the left arm of yeast
RT chromosome XV that contains the ARG8 and CDC33 genes, a putative riboflavin
RT synthase beta chain gene, and four new open reading frames.";
RL Yeast 11:1061-1067(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [8]
RP PHOSPHORYLATION AT SER-2 AND SER-15.
RX PubMed=7592868; DOI=10.1074/jbc.270.44.26505;
RA Zanchin N.I.T., McCarthy J.E.G.;
RT "Characterization of the in vivo phosphorylation sites of the mRNA.cap-
RT binding complex proteins eukaryotic initiation factor-4E and p20 in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:26505-26510(1995).
RN [9]
RP INTERACTION WITH PAT1.
RX PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1;
RA Tharun S., Parker R.;
RT "Targeting an mRNA for decapping: displacement of translation factors and
RT association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
RL Mol. Cell 8:1075-1083(2001).
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-15, 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-15; THR-22 AND SER-30, 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-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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-22 AND SER-30, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-22; SER-28 AND
RP SER-30, 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).
RN [16]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=9302999; DOI=10.1038/nsb0997-717;
RA Matsuo H., Li H., McGuire A.M., Fletcher C.M., Gingras A.-C., Sonenberg N.,
RA Wagner G.;
RT "Structure of translation factor eIF4E bound to m7GDP and interaction with
RT 4E-binding protein.";
RL Nat. Struct. Biol. 4:717-724(1997).
CC -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures.
CC -!- SUBUNIT: Component of the eIF4F complex, which composition varies with
CC external and internal environmental conditions. It is composed of at
CC least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632)
CC (By similarity). Interacts with PAT1 in a RNA-dependent manner. eIF4E
CC is also known to interact with other partners. {ECO:0000250,
CC ECO:0000269|PubMed:11741542}.
CC -!- INTERACTION:
CC P07260; P12962: CAF20; NbExp=7; IntAct=EBI-150, EBI-9010;
CC P07260; P39935: TIF4631; NbExp=14; IntAct=EBI-150, EBI-9002;
CC -!- MISCELLANEOUS: Present with 14200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; M15436; AAA34587.1; -; Genomic_DNA.
DR EMBL; M21620; AAA34480.1; -; Genomic_DNA.
DR EMBL; M29251; AAA34588.1; -; Genomic_DNA.
DR EMBL; X84036; CAA58854.1; -; Genomic_DNA.
DR EMBL; Z74881; CAA99160.1; -; Genomic_DNA.
DR EMBL; AY692936; AAT92955.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10646.1; -; Genomic_DNA.
DR PIR; A26130; A26130.
DR RefSeq; NP_014502.1; NM_001183393.1.
DR PDB; 1AP8; NMR; -; A=1-213.
DR PDB; 1RF8; NMR; -; A=1-213.
DR PDB; 6FC1; X-ray; 1.35 A; A/C=25-213.
DR PDB; 6FC2; X-ray; 1.92 A; A/C=35-213.
DR PDB; 6FC3; X-ray; 1.75 A; A=35-213.
DR PDBsum; 1AP8; -.
DR PDBsum; 1RF8; -.
DR PDBsum; 6FC1; -.
DR PDBsum; 6FC2; -.
DR PDBsum; 6FC3; -.
DR AlphaFoldDB; P07260; -.
DR SMR; P07260; -.
DR BioGRID; 34278; 168.
DR ComplexPortal; CPX-430; Eukaryotic translation initiation factor 4F complex, variant TIF4631.
DR ComplexPortal; CPX-431; Eukaryotic translation initiation factor 4F complex, variant TIF4632.
DR DIP; DIP-1223N; -.
DR ELM; P07260; -.
DR IntAct; P07260; 84.
DR MINT; P07260; -.
DR STRING; 4932.YOL139C; -.
DR iPTMnet; P07260; -.
DR MaxQB; P07260; -.
DR PaxDb; P07260; -.
DR PRIDE; P07260; -.
DR TopDownProteomics; P07260; -.
DR EnsemblFungi; YOL139C_mRNA; YOL139C; YOL139C.
DR GeneID; 854026; -.
DR KEGG; sce:YOL139C; -.
DR SGD; S000005499; CDC33.
DR VEuPathDB; FungiDB:YOL139C; -.
DR eggNOG; KOG1670; Eukaryota.
DR GeneTree; ENSGT00940000167792; -.
DR HOGENOM; CLU_043552_2_2_1; -.
DR InParanoid; P07260; -.
DR OMA; EEFWAIV; -.
DR BioCyc; YEAST:G3O-33532-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR EvolutionaryTrace; P07260; -.
DR PRO; PR:P07260; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07260; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IC:ComplexPortal.
DR GO; GO:0098808; F:mRNA cap binding; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:SGD.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:SGD.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; ISS:SGD.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..213
FT /note="Eukaryotic translation initiation factor 4E"
FT /id="PRO_0000193653"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:7592868"
FT MOD_RES 15
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:7592868,
FT ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1RF8"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1AP8"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:6FC1"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1RF8"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:6FC3"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6FC1"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:1AP8"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6FC1"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:6FC1"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:6FC3"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6FC1"
SQ SEQUENCE 213 AA; 24254 MW; 5B9162E1BD0B1BDE CRC64;
MSVEEVSKKF EENVSVDDTT ATPKTVLSDS AHFDVKHPLN TKWTLWYTKP AVDKSESWSD
LLRPVTSFQT VEEFWAIIQN IPEPHELPLK SDYHVFRNDV RPEWEDEANA KGGKWSFQLR
GKGADIDELW LRTLLAVIGE TIDEDDSQIN GVVLSIRKGG NKFALWTKSE DKEPLLRIGG
KFKQVLKLTD DGHLEFFPHS SANGRHPQPS ITL
