IF4E_DROME
ID IF4E_DROME Reviewed; 259 AA.
AC P48598; A4V1Q6; Q95SV3; Q9VSX8; Q9VSX9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Eukaryotic translation initiation factor 4E1;
DE AltName: Full=eIF-4F 25 kDa subunit;
DE AltName: Full=mRNA cap-binding protein {ECO:0000303|PubMed:8663200};
GN Name=eIF4E1 {ECO:0000312|FlyBase:FBgn0015218};
GN Synonyms=eIF-4E {ECO:0000303|PubMed:7742371},
GN Eif4e {ECO:0000303|PubMed:14691132};
GN ORFNames=CG4035 {ECO:0000312|FlyBase:FBgn0015218};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), AND DEVELOPMENTAL STAGE.
RX PubMed=7742371; DOI=10.1016/0167-4781(95)00039-j;
RA Hernandez G., Sierra J.M.;
RT "Translation initiation factor eIF-4E from Drosophila: cDNA sequence and
RT expression of the gene.";
RL Biochim. Biophys. Acta 1261:427-431(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS I AND II), AND FUNCTION.
RX PubMed=8663200; DOI=10.1074/jbc.271.27.16393;
RA Lavoie C.A., Lachance P.E.D., Sonenberg N., Lasko P.;
RT "Alternatively spliced transcripts from the Drosophila eIF4E gene produce
RT two different Cap-binding proteins.";
RL J. Biol. Chem. 271:16393-16398(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS I AND II), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=9065696; DOI=10.1007/s004380050365;
RA Hernandez G., del Corral R., Santoyo J., Campuzano S., Sierra J.M.;
RT "Localization, structure and expression of the gene for translation
RT initiation factor eIF-4E from Drosophila melanogaster.";
RL Mol. Gen. Genet. 253:624-633(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS I AND II).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH THOR.
RX PubMed=11389445; DOI=10.1038/35078571;
RA Miron M., Verdu J., Lachance P.E., Birnbaum M.J., Lasko P.F., Sonenberg N.;
RT "The translational inhibitor 4E-BP is an effector of PI(3)K/Akt signalling
RT and cell growth in Drosophila.";
RL Nat. Cell Biol. 3:596-601(2001).
RN [9]
RP INTERACTION WITH CUP.
RX PubMed=14691132; DOI=10.1083/jcb.200309088;
RA Wilhelm J.E., Hilton M., Amos Q., Henzel W.J.;
RT "Cup is an eIF4E binding protein required for both the translational
RT repression of oskar and the recruitment of Barentsz.";
RL J. Cell Biol. 163:1197-1204(2003).
RN [10]
RP INTERACTION WITH THOR.
RX PubMed=14645523; DOI=10.1128/mcb.23.24.9117-9126.2003;
RA Miron M., Lasko P., Sonenberg N.;
RT "Signaling from Akt to FRAP/TOR targets both 4E-BP and S6K in Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 23:9117-9126(2003).
RN [11]
RP INTERACTION WITH CUP, AND MUTAGENESIS OF TRP-117.
RX PubMed=14723848; DOI=10.1016/s1534-5807(03)00400-3;
RA Nakamura A., Sato K., Hanyu-Nakamura K.;
RT "Drosophila Cup is an eIF4E binding protein that associates with Bruno and
RT regulates oskar mRNA translation in oogenesis.";
RL Dev. Cell 6:69-78(2004).
RN [12]
RP INTERACTION WITH CUP.
RX PubMed=14685270; DOI=10.1038/sj.emboj.7600026;
RA Nelson M.R., Leidal A.M., Smibert C.A.;
RT "Drosophila Cup is an eIF4E-binding protein that functions in Smaug-
RT mediated translational repression.";
RL EMBO J. 23:150-159(2004).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=17178403; DOI=10.1016/j.neuron.2006.10.028;
RA Barbee S.A., Estes P.S., Cziko A.M., Hillebrand J., Luedeman R.A.,
RA Coller J.M., Johnson N., Howlett I.C., Geng C., Ueda R., Brand A.H.,
RA Newbury S.F., Wilhelm J.E., Levine R.B., Nakamura A., Parker R.,
RA Ramaswami M.;
RT "Staufen- and FMRP-containing neuronal RNPs are structurally and
RT functionally related to somatic P bodies.";
RL Neuron 52:997-1009(2006).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=20869429; DOI=10.1016/j.gene.2010.09.003;
RA Ottone C., Galasso A., Gemei M., Pisa V., Gigliotti S., Piccioni F.,
RA Graziani F., Verrotti di Pianella A.;
RT "Diminution of eIF4E activity suppresses parkin mutant phenotypes.";
RL Gene 470:12-19(2011).
RN [15]
RP INTERACTION WITH MXT.
RX PubMed=23716590; DOI=10.1128/mcb.01354-12;
RA Hernandez G., Miron M., Han H., Liu N., Magescas J., Tettweiler G.,
RA Frank F., Siddiqui N., Sonenberg N., Lasko P.;
RT "Mextli is a novel eukaryotic translation initiation factor 4E-binding
RT protein that promotes translation in Drosophila melanogaster.";
RL Mol. Cell. Biol. 33:2854-2864(2013).
RN [16]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ME31B; CUP; TRAL AND PABP, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=28875934; DOI=10.7554/elife.27891;
RA Wang M., Ly M., Lugowski A., Laver J.D., Lipshitz H.D., Smibert C.A.,
RA Rissland O.S.;
RT "ME31B globally represses maternal mRNAs by two distinct mechanisms during
RT the Drosophila maternal-to-zygotic transition.";
RL Elife 6:0-0(2017).
RN [17] {ECO:0007744|PDB:4AXG}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 19-259 IN COMPLEX WITH CUP, AND
RP INTERACTION WITH CUP.
RX PubMed=22832024; DOI=10.1261/rna.033639.112;
RA Kinkelin K., Veith K., Grunwald M., Bono F.;
RT "Crystal structure of a minimal eIF4E-Cup complex reveals a general
RT mechanism of eIF4E regulation in translational repression.";
RL RNA 18:1624-1634(2012).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 80-259 IN COMPLEX WITH MXT,
RP INTERACTION WITH 4E-T; CUP; MXT AND THOR, AND MUTAGENESIS OF ILE-107;
RP 121-ASN-HIS-122 AND ILE-123.
RX PubMed=26294658; DOI=10.1101/gad.269068.115;
RA Peter D., Weber R., Kone C., Chung M.Y., Ebertsch L., Truffault V.,
RA Weichenrieder O., Igreja C., Izaurralde E.;
RT "Mextli proteins use both canonical bipartite and novel tripartite binding
RT modes to form eIF4E complexes that display differential sensitivity to 4E-
RT BP regulation.";
RL Genes Dev. 29:1835-1849(2015).
RN [19] {ECO:0007744|PDB:4UE8, ECO:0007744|PDB:4UE9, ECO:0007744|PDB:4UEA, ECO:0007744|PDB:4UEB, ECO:0007744|PDB:4UEC}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 80-259 IN COMPLEX WITH EIF4G1;
RP 4E-T AND THOR, AND INTERACTION WITH EIF4G1; 4E-T AND THOR.
RX PubMed=25702871; DOI=10.1016/j.molcel.2015.01.017;
RA Peter D., Igreja C., Weber R., Wohlbold L., Weiler C., Ebertsch L.,
RA Weichenrieder O., Izaurralde E.;
RT "Molecular architecture of 4E-BP translational inhibitors bound to eIF4E.";
RL Mol. Cell 57:1074-1087(2015).
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 (PubMed:8663200). In 0-1 hour embryos, forms a
CC complex with me31B, cup, tral and pAbp which binds to various mRNAs
CC including maternal mRNAs, and down-regulates their expression during
CC the maternal-to-zygotic transition (PubMed:28875934).
CC {ECO:0000269|PubMed:28875934, ECO:0000269|PubMed:8663200}.
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least eIF4A, eIF4E1 and eIF4G1 (PubMed:25702871).
CC Recruited by cup in oocytes and in early embryos, preventing the
CC interaction with eIF4G (PubMed:14691132, PubMed:14723848,
CC PubMed:14685270, PubMed:26294658, PubMed:22832024). The interaction
CC with cup therefore prevents the translation of key transcripts such as
CC oskar (osk) and nanos (nos) in some regions in the early embryo
CC (PubMed:14691132, PubMed:14723848, PubMed:14685270, PubMed:26294658,
CC PubMed:22832024). Interacts with mxt (PubMed:23716590,
CC PubMed:26294658). Interacts with 4E-T and Thor (PubMed:11389445,
CC PubMed:14645523, PubMed:26294658, PubMed:25702871). Forms a RNP
CC containing at least me31B, eIF4E1, cup, tral and pAbp; this interaction
CC is required for the translational silencing of maternal mRNAs during
CC the maternal-to-zygotic transition (PubMed:28875934).
CC {ECO:0000269|PubMed:11389445, ECO:0000269|PubMed:14645523,
CC ECO:0000269|PubMed:14685270, ECO:0000269|PubMed:14691132,
CC ECO:0000269|PubMed:14723848, ECO:0000269|PubMed:22832024,
CC ECO:0000269|PubMed:23716590, ECO:0000269|PubMed:25702871,
CC ECO:0000269|PubMed:26294658, ECO:0000269|PubMed:28875934}.
CC -!- INTERACTION:
CC P48598; Q9VMA3: cup; NbExp=6; IntAct=EBI-198574, EBI-95398;
CC P48598; O61380: eIF4G1; NbExp=4; IntAct=EBI-198574, EBI-182219;
CC P48598; P21187: pAbp; NbExp=2; IntAct=EBI-198574, EBI-103658;
CC P48598-2; Q9VY20: Dmel\CG5347; NbExp=4; IntAct=EBI-15128446, EBI-15128468;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:17178403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I {ECO:0000303|PubMed:8663200}; Synonyms=A, B, D, E, F, G;
CC IsoId=P48598-1; Sequence=Displayed;
CC Name=II {ECO:0000303|PubMed:8663200}; Synonyms=C;
CC IsoId=P48598-2; Sequence=VSP_001437;
CC -!- TISSUE SPECIFICITY: Expressed at the posterior end of developing
CC oocytes (at protein level) (PubMed:20869429). Preferential expression
CC in the pole cells, at different developmental stages (PubMed:9065696).
CC {ECO:0000269|PubMed:20869429, ECO:0000269|PubMed:9065696}.
CC -!- DEVELOPMENTAL STAGE: High levels of expression in early embryos, with
CC levels decreasing slightly over the first 5 hours of embryogenesis (at
CC protein level) (PubMed:28875934). Throughout development
CC (PubMed:7742371, PubMed:9065696). {ECO:0000269|PubMed:28875934,
CC ECO:0000269|PubMed:7742371, ECO:0000269|PubMed:9065696}.
CC -!- PTM: Phosphorylation increases the ability of the protein to bind to
CC mRNA caps and to form the eIF4F complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U16139; AAC46603.1; -; mRNA.
DR EMBL; U54469; AAC03525.1; -; Genomic_DNA.
DR EMBL; U54469; AAC03524.1; -; Genomic_DNA.
DR EMBL; U63033; AAC47480.1; -; Genomic_DNA.
DR EMBL; U63033; AAC47479.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50281.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50282.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50283.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11963.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11964.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11965.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11966.1; -; Genomic_DNA.
DR EMBL; AY060470; AAL25509.1; ALT_FRAME; mRNA.
DR EMBL; BT012467; AAS93738.1; -; mRNA.
DR EMBL; BT044219; ACH92284.1; -; mRNA.
DR PIR; S55936; S55936.
DR RefSeq; NP_001261626.1; NM_001274697.1. [P48598-1]
DR RefSeq; NP_001261627.1; NM_001274698.1. [P48598-1]
DR RefSeq; NP_524829.1; NM_080090.3. [P48598-1]
DR RefSeq; NP_729480.1; NM_168333.2. [P48598-2]
DR RefSeq; NP_729481.1; NM_168334.1. [P48598-1]
DR RefSeq; NP_729482.1; NM_168335.2. [P48598-1]
DR RefSeq; NP_729483.1; NM_168336.2. [P48598-1]
DR RefSeq; NP_729484.1; NM_168337.2. [P48598-1]
DR RefSeq; NP_729485.1; NM_168338.2. [P48598-1]
DR PDB; 4AXG; X-ray; 2.80 A; A/B=19-259.
DR PDB; 4UE8; X-ray; 1.10 A; A=80-259.
DR PDB; 4UE9; X-ray; 2.15 A; A=80-259.
DR PDB; 4UEA; X-ray; 2.62 A; A/C/E=80-259.
DR PDB; 4UEB; X-ray; 2.52 A; A/C/E=80-259.
DR PDB; 4UEC; X-ray; 2.40 A; A/C=80-259.
DR PDB; 5ABU; X-ray; 2.16 A; A=80-259.
DR PDB; 5ABV; X-ray; 2.13 A; A/C/E/G=80-259.
DR PDB; 5T47; X-ray; 2.20 A; A/C=80-259.
DR PDB; 5T48; X-ray; 2.19 A; A=80-259.
DR PDBsum; 4AXG; -.
DR PDBsum; 4UE8; -.
DR PDBsum; 4UE9; -.
DR PDBsum; 4UEA; -.
DR PDBsum; 4UEB; -.
DR PDBsum; 4UEC; -.
DR PDBsum; 5ABU; -.
DR PDBsum; 5ABV; -.
DR PDBsum; 5T47; -.
DR PDBsum; 5T48; -.
DR AlphaFoldDB; P48598; -.
DR SMR; P48598; -.
DR BioGRID; 69740; 50.
DR ComplexPortal; CPX-3177; eIF4E-cup complex.
DR DIP; DIP-17448N; -.
DR ELM; P48598; -.
DR IntAct; P48598; 14.
DR STRING; 7227.FBpp0076215; -.
DR iPTMnet; P48598; -.
DR PaxDb; P48598; -.
DR PRIDE; P48598; -.
DR DNASU; 45525; -.
DR EnsemblMetazoa; FBtr0076487; FBpp0076215; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0076488; FBpp0076216; FBgn0015218. [P48598-2]
DR EnsemblMetazoa; FBtr0076489; FBpp0076217; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0076490; FBpp0076218; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0076491; FBpp0076219; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0076492; FBpp0076220; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0076493; FBpp0076221; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0333884; FBpp0306016; FBgn0015218. [P48598-1]
DR EnsemblMetazoa; FBtr0333885; FBpp0306017; FBgn0015218. [P48598-1]
DR GeneID; 45525; -.
DR KEGG; dme:Dmel_CG4035; -.
DR UCSC; CG4035-RB; d. melanogaster.
DR CTD; 45525; -.
DR FlyBase; FBgn0015218; eIF4E1.
DR VEuPathDB; VectorBase:FBgn0015218; -.
DR eggNOG; KOG1670; Eukaryota.
DR GeneTree; ENSGT00940000167792; -.
DR InParanoid; P48598; -.
DR OMA; EEFWAIV; -.
DR PhylomeDB; P48598; -.
DR Reactome; R-DME-110523; TOR signaling pathway.
DR Reactome; R-DME-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-166208; mTORC1-mediated signalling.
DR Reactome; R-DME-429947; Deadenylation of mRNA.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; P48598; -.
DR BioGRID-ORCS; 45525; 1 hit in 3 CRISPR screens.
DR ChiTaRS; eIF-4E; fly.
DR GenomeRNAi; 45525; -.
DR PRO; PR:P48598; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0015218; Expressed in egg chamber and 42 other tissues.
DR ExpressionAtlas; P48598; baseline and differential.
DR Genevisible; P48598; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IDA:FlyBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0097482; C:muscle cell postsynaptic specialization; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IPI:FlyBase.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:FlyBase.
DR GO; GO:0000339; F:RNA cap binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IDA:SynGO.
DR GO; GO:0099578; P:regulation of translation at postsynapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0016070; P:RNA metabolic process; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IDA:FlyBase.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR DisProt; DP02400; -.
DR Gene3D; 3.30.760.10; -; 1.
DR IDEAL; IID50283; -.
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; Alternative splicing; Cytoplasm; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..259
FT /note="Eukaryotic translation initiation factor 4E1"
FT /id="PRO_0000193642"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..101
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 146..147
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 199..204
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT VAR_SEQ 1..18
FT /note="MQSDFHRMKNFANPKSMF -> MVVLETE (in isoform II)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_001437"
FT MUTAGEN 107
FT /note="I->A: Abolishes interaction with cup and mxt; when
FT associated with A-123."
FT /evidence="ECO:0000269|PubMed:26294658"
FT MUTAGEN 117
FT /note="W->A: Disrupts interaction with cup, eIF4G and mxt."
FT /evidence="ECO:0000269|PubMed:14723848,
FT ECO:0000269|PubMed:26294658"
FT MUTAGEN 121..122
FT /note="NH->EE: Abolishes interaction with mxt, reduces
FT binding to Thor and 4E-T, and does not affect interaction
FT with cup."
FT /evidence="ECO:0000269|PubMed:26294658"
FT MUTAGEN 123
FT /note="I->A: Abolishes interaction with cup and mxt; when
FT associated with A-107."
FT /evidence="ECO:0000269|PubMed:26294658"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5ABV"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 113..122
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4UEB"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 215..229
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:4UE8"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4UE8"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:5ABV"
SQ SEQUENCE 259 AA; 29224 MW; B844B2DD5738758E CRC64;
MQSDFHRMKN FANPKSMFKT SAPSTEQGRP EPPTSAAAPA EAKDVKPKED PQETGEPAGN
TATTTAPAGD DAVRTEHLYK HPLMNVWTLW YLENDRSKSW EDMQNEITSF DTVEDFWSLY
NHIKPPSEIK LGSDYSLFKK NIRPMWEDAA NKQGGRWVIT LNKSSKTDLD NLWLDVLLCL
IGEAFDHSDQ ICGAVINIRG KSNKISIWTA DGNNEEAALE IGHKLRDALR LGRNNSLQYQ
LHKDTMVKQG SNVKSIYTL
