EIF3E_DROME
ID EIF3E_DROME Reviewed; 435 AA.
AC O77410; Q9VVA2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000255|HAMAP-Rule:MF_03004};
GN Name=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
GN Synonyms=eIF-3p48 {ECO:0000303|PubMed:10375641},
GN eIF3-S6 {ECO:0000255|HAMAP-Rule:MF_03004},
GN Int6 {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000303|PubMed:10375641};
GN ORFNames=CG9677 {ECO:0000312|FlyBase:FBgn0025582};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10375641; DOI=10.1016/s0378-1119(99)00130-4;
RA Miyazaki S., Rasmussen S., Imatani A., Diella F., Sullivan D.T.,
RA Callahan R.;
RT "Characterization of the Drosophila ortholog of mouse eIF-3p48/INT-6.";
RL Gene 233:241-247(1999).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18493598; DOI=10.1371/journal.pone.0002239;
RA Rencus-Lazar S., Amir Y., Wu J., Chien C.T., Chamovitz D.A., Segal D.;
RT "The proto-oncogene Int6 is essential for neddylation of Cul1 and Cul3 in
RT Drosophila.";
RL PLoS ONE 3:E2239-E2239(2008).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28505193; DOI=10.1371/journal.pgen.1006784;
RA Renda F., Pellacani C., Strunov A., Bucciarelli E., Naim V., Bosso G.,
RA Kiseleva E., Bonaccorsi S., Sharp D.J., Khodjakov A., Gatti M., Somma M.P.;
RT "The Drosophila orthologue of the INT6 onco-protein regulates mitotic
RT microtubule growth and kinetochore structure.";
RL PLoS Genet. 13:E1006784-E1006784(2017).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation
CC (PubMed:18493598). In addition to its role in the eIF-3 complex, also
CC functions in protein ubiquitination and degradation (PubMed:18493598,
CC PubMed:28505193). During mitosis required for regulating mitotic
CC microtubule growth and kinetochore formation, and consequently is
CC required for satisfying the spindle assembly checkpoint (SAC) during
CC metaphase to prevent delays in mitotic progression (PubMed:28505193).
CC This is likely by promoting the ubiquitination and degradation of
CC Klp67A, a kinesin-like protein that suppresses microtubule
CC polymerization at plus ends (PubMed:28505193). Acts in the COP9
CC signalosome (CSN) mediated regulation of cullin neddylation by
CC promoting Cul1 and Cul3 neddylation and negatively regulating the CSN
CC complex subunit CSN5 (PubMed:18493598). {ECO:0000255|HAMAP-
CC Rule:MF_03004, ECO:0000269|PubMed:18493598,
CC ECO:0000269|PubMed:28505193}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. The eIF-3 complex interacts with pix. Interacts with
CC mxt (PubMed:23716590). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:23716590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:28505193}. Microsome {ECO:0000269|PubMed:10375641}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:10375641}. Note=Uniformly
CC distributed in interphase and mitotic cells.
CC {ECO:0000269|PubMed:28505193}.
CC -!- TISSUE SPECIFICITY: Expression levels in females and males are
CC relatively similar 10 days after oviposition, however by day 15
CC expression is higher in gravid females than in males (at protein
CC level). {ECO:0000269|PubMed:10375641}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adults (at
CC protein level). Expression peaks in early embryos (2 h after
CC oviposition), then steadily decreases over the embryonic and larval
CC stages (at protein level). Expression increases again 5 days after
CC oviposition and remains stable until day 10 (at protein level).
CC {ECO:0000269|PubMed:10375641}.
CC -!- DISRUPTION PHENOTYPE: Homozygous lethal at the first instar larval
CC stage. Larvae are smaller than wild-type and die 3-4 days after
CC hatching. {ECO:0000269|PubMed:18493598}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC Rule:MF_03004}.
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DR EMBL; U89162; AAC62307.1; -; mRNA.
DR EMBL; AE014296; AAF49412.1; -; Genomic_DNA.
DR EMBL; AF132551; AAD27850.1; -; mRNA.
DR RefSeq; NP_477385.1; NM_058037.5.
DR AlphaFoldDB; O77410; -.
DR SMR; O77410; -.
DR BioGRID; 65176; 17.
DR DIP; DIP-19544N; -.
DR IntAct; O77410; 3.
DR STRING; 7227.FBpp0075104; -.
DR PaxDb; O77410; -.
DR PRIDE; O77410; -.
DR DNASU; 39877; -.
DR EnsemblMetazoa; FBtr0075345; FBpp0075104; FBgn0025582.
DR GeneID; 39877; -.
DR KEGG; dme:Dmel_CG9677; -.
DR CTD; 3646; -.
DR FlyBase; FBgn0025582; eIF3e.
DR VEuPathDB; VectorBase:FBgn0025582; -.
DR eggNOG; KOG2758; Eukaryota.
DR GeneTree; ENSGT00390000002661; -.
DR HOGENOM; CLU_031132_0_0_1; -.
DR InParanoid; O77410; -.
DR OMA; TWGKLAC; -.
DR OrthoDB; 1151808at2759; -.
DR PhylomeDB; O77410; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; O77410; -.
DR BioGRID-ORCS; 39877; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 39877; -.
DR PRO; PR:O77410; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0025582; Expressed in ovary and 28 other tissues.
DR ExpressionAtlas; O77410; baseline and differential.
DR Genevisible; O77410; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:FlyBase.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:UniProtKB-UniRule.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR HAMAP; MF_03004; eIF3e; 1.
DR InterPro; IPR016650; eIF3e.
DR InterPro; IPR019010; eIF3e_N.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10317; PTHR10317; 1.
DR Pfam; PF09440; eIF3_N; 1.
DR Pfam; PF01399; PCI; 1.
DR PIRSF; PIRSF016255; eIF3e_su6; 1.
DR SMART; SM01186; eIF3_N; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Initiation factor; Microsome;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..435
FT /note="Eukaryotic translation initiation factor 3 subunit
FT E"
FT /id="PRO_0000123517"
FT DOMAIN 219..392
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ SEQUENCE 435 AA; 51162 MW; 6F79D32FBA3EA711 CRC64;
MANFDLTRIN CQFLDRHLTF PLLEFLCGKE IYNQQELLEY ILETVNKTNM IDYTMDTRKR
LNLSQEMPEE LVQRKAEVLA TLKQLQNEVA PIMKATDILK NGESMKDSKT FVNALQKDYN
FKVEHLESAY KLAKYLYECG NYQESTSYLY FCLIVMSPND KNYLNVLWGK LAAEILTLNW
NTALEDLTRL RDYIDNANFS TIQALQQRTW LIHWSVLVFF NHPKGRDLII EMFLYKPLYL
NAIQTMCPHI MRYLATAVVI NRTRRNALKD LIKVIQQESY TYRDPITEFL ECLYVNFDFE
GARLKLHECQ TVILNDFFIV ACLNEFVEDA RLMIFETFCR IHQCITISML ADKLNMKPNE
AECWIVNLIR NARLNAKIDS KLGHVVMGTQ PLSPYQQLVE KIDSLSMRSE HLAGLIERKS
KQKQNQESAD SWKYY
