EIF3E_ARATH
ID EIF3E_ARATH Reviewed; 441 AA.
AC Q9C5Z3; Q9M2L8; Q9M4T7;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000303|PubMed:11029466};
DE Short=AtEIF3E-1 {ECO:0000303|PubMed:11029466};
DE Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000303|PubMed:11029466};
DE Short=p48 {ECO:0000303|PubMed:11029466};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6 {ECO:0000255|HAMAP-Rule:MF_03004};
DE Short=AtINT6 {ECO:0000303|PubMed:11029466};
DE Short=INT-6 {ECO:0000303|PubMed:11029466};
GN Name=TIF3E1 {ECO:0000303|PubMed:11029466};
GN Synonyms=INT6 {ECO:0000303|PubMed:11029466};
GN OrderedLocusNames=At3g57290 {ECO:0000312|EMBL:AEE79636.1};
GN ORFNames=F28O9.140 {ECO:0000312|EMBL:CAB68135.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAG53613.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH CSN7 AND TIF3C1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11029466; DOI=10.1074/jbc.m006721200;
RA Yahalom A., Kim T.-H., Winter E., Karniol B., von Arnim A.G.,
RA Chamovitz D.A.;
RT "Arabidopsis eIF3e (INT-6) associates with both eIF3c and the COP9
RT signalosome subunit CSN7.";
RL J. Biol. Chem. 276:334-340(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11042177; DOI=10.1074/jbc.m007236200;
RA Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.;
RT "Plant initiation factor 3 subunit composition resembles mammalian
RT initiation factor 3 and has a novel subunit.";
RL J. Biol. Chem. 276:2122-2131(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [7]
RP PROTEASE-RESISTANCE.
RX PubMed=16679540; DOI=10.1385/cbb:44:3:522;
RA Murai M.J., Carneiro F.R.G., Gozzo F.C., Ierardi D.F., Pertinhez T.A.,
RA Zanchin N.I.T.;
RT "Identification and characterization of a proteolysis-resistant fragment
RT containing the PCI domain in the Arabidopsis thaliana INT6/eIF3e
RT translation factor.";
RL Cell Biochem. Biophys. 44:522-529(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=18067529; DOI=10.1111/j.1365-313x.2007.03347.x;
RA Yahalom A., Kim T.-H., Roy B., Singer R., von Arnim A.G., Chamovitz D.A.;
RT "Arabidopsis eIF3e is regulated by the COP9 signalosome and has an impact
RT on development and protein translation.";
RL Plant J. 53:300-311(2008).
RN [9]
RP INTERACTION WITH AT1G27930; AT4G30620; CSN1; CSN4; CSN6A; CSN6B; CSN7;
RP CSN8; RPN12A; RPS9B AND RPS9C, AND SUBUNIT.
RX PubMed=19704582; DOI=10.4161/psb.3.6.5434;
RA Paz-Aviram T., Yahalom A., Chamovitz D.A.;
RT "Arabidopsis eIF3e interacts with subunits of the ribosome, Cop9
RT signalosome and proteasome.";
RL Plant Signal. Behav. 3:409-411(2008).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TIF3F1.
RX PubMed=20444226; DOI=10.1111/j.1365-313x.2010.04237.x;
RA Xia C., Wang Y.-J., Li W.-Q., Chen Y.-R., Deng Y., Zhang X.-Q., Chen L.-Q.,
RA Ye D.;
RT "The Arabidopsis eukaryotic translation initiation factor 3, subunit F
RT (AteIF3f), is required for pollen germination and embryogenesis.";
RL Plant J. 63:189-202(2010).
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 (Potential). Regulates negatively translation during flower development
CC (PubMed:18067529, PubMed:20444226). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:18067529, ECO:0000269|PubMed:20444226}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex (Potential). Binds to the translation initiation
CC factors TIF3F1 and TIF3H1 (PubMed:20444226, PubMed:15548739).
CC Associates with the CSN (COP9 signalosome) complex. Interacts directly
CC with CSN1, CSN4, CSN6A, CSN6B, CSN7, CSN8 and TIF3C1 (PubMed:11029466,
CC PubMed:19704582). Binds to 40S small ribosomal subunit S9 (RPS9B and
CC RPS9C) via its N-terminal part. Interacts with the 26S proteasome
CC subunit RPN12a via its C-terminal part. Binds also with At1g27930 and
CC At4g30620 (PubMed:19704582). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:11029466, ECO:0000269|PubMed:15548739,
CC ECO:0000269|PubMed:19704582, ECO:0000269|PubMed:20444226}.
CC -!- INTERACTION:
CC Q9C5Z3; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-1635572, EBI-617095;
CC Q9C5Z3; Q94JU3: CSN7; NbExp=6; IntAct=EBI-1635572, EBI-531152;
CC Q9C5Z3; O49160: TIF3C1; NbExp=3; IntAct=EBI-1635572, EBI-1635551;
CC Q9C5Z3; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1635572, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:11029466}. Nucleus {ECO:0000269|PubMed:11029466}.
CC -!- INDUCTION: Targeted by the COP9 signalosome to proteasome-dependent
CC degradation. {ECO:0000269|PubMed:18067529}.
CC -!- DISRUPTION PHENOTYPE: Several floral development defects, including
CC delayed flowering, reduced sepaloid petals and short stamens. Male
CC gametophytic lethal. {ECO:0000269|PubMed:18067529,
CC ECO:0000269|PubMed:20444226}.
CC -!- MISCELLANEOUS: The PCI domain is protease-resistant.
CC {ECO:0000269|PubMed:16679540}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC Rule:MF_03004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB68135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF255679; AAF67757.1; -; mRNA.
DR EMBL; AF285832; AAG53613.1; -; mRNA.
DR EMBL; AL137080; CAB68135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79636.1; -; Genomic_DNA.
DR EMBL; AY039913; AAK64017.1; -; mRNA.
DR EMBL; AY079357; AAL85088.1; -; mRNA.
DR PIR; T45807; T45807.
DR RefSeq; NP_567047.1; NM_115589.5.
DR AlphaFoldDB; Q9C5Z3; -.
DR SMR; Q9C5Z3; -.
DR IntAct; Q9C5Z3; 4.
DR STRING; 3702.AT3G57290.1; -.
DR PaxDb; Q9C5Z3; -.
DR PRIDE; Q9C5Z3; -.
DR ProteomicsDB; 222285; -.
DR EnsemblPlants; AT3G57290.1; AT3G57290.1; AT3G57290.
DR GeneID; 824896; -.
DR Gramene; AT3G57290.1; AT3G57290.1; AT3G57290.
DR KEGG; ath:AT3G57290; -.
DR Araport; AT3G57290; -.
DR TAIR; locus:2082593; AT3G57290.
DR eggNOG; KOG2758; Eukaryota.
DR HOGENOM; CLU_031132_0_0_1; -.
DR InParanoid; Q9C5Z3; -.
DR OMA; TWGKLAC; -.
DR OrthoDB; 1151808at2759; -.
DR PhylomeDB; Q9C5Z3; -.
DR PRO; PR:Q9C5Z3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C5Z3; baseline and differential.
DR Genevisible; Q9C5Z3; AT.
DR GO; GO:0008180; C:COP9 signalosome; IPI:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031597; C:cytosolic proteasome complex; IDA:UniProtKB.
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; IPI:TAIR.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; TAS:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0006412; P:translation; IMP:TAIR.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Developmental protein; Initiation factor; Nucleus;
KW Protein biosynthesis; Reference proteome; Repressor;
KW Translation regulation.
FT CHAIN 1..441
FT /note="Eukaryotic translation initiation factor 3 subunit
FT E"
FT /id="PRO_0000434569"
FT DOMAIN 223..407
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT CONFLICT 274
FT /note="E -> D (in Ref. 1; AAF67757)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="L -> F (in Ref. 1; AAF67757)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="Y -> F (in Ref. 1; AAF67757)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> R (in Ref. 1; AAF67757)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="E -> V (in Ref. 1; AAF67757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 51750 MW; A9E6656E51AA1483 CRC64;
MEESKQNYDL TPLIAPNLDR HLVFPIFEFL QERQLYPDEQ ILKSKIQLLN QTNMVDYAMD
IHKSLYHTED APQEMVERRT EVVARLKSLE EAAAPLVSFL LNPNAVQELR ADKQYNLQML
KERYQIGPDQ IEALYQYAKF QFECGNYSGA ADYLYQYRTL CSNLERSLSA LWGKLASEIL
MQNWDIALEE LNRLKEIIDS KSFSSPLNQV QNRIWLMHWG LYIFFNHDNG RTQIIDLFNQ
DKYLNAIQTS APHLLRYLAT AFIVNKRRRP QLKEFIKVIQ QEHYSYKDPI IEFLACVFVN
YDFDGAQKKM KECEEVIVND PFLGKRVEDG NFSTVPLRDE FLENARLFVF ETYCKIHQRI
DMGVLAEKLN LNYEEAERWI VNLIRTSKLD AKIDSESGTV IMEPTQPNVH EQLINHTKGL
SGRTYKLVNQ LLEHTQAQAT R
