IF4E4_ARATH
ID IF4E4_ARATH Reviewed; 198 AA.
AC O04663; Q3E8N6; Q546X5; Q9SAN8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4E;
DE Short=eIF(iso)4E;
DE AltName: Full=Protein LOSS OF SUSCEPTIBILITY TO POTYVIRUS 1;
DE AltName: Full=eIF-(iso)4F 25 kDa subunit;
DE AltName: Full=eIF-(iso)4F p28 subunit;
DE AltName: Full=eIF4Eiso protein;
DE AltName: Full=mRNA cap-binding protein;
GN Name=EIF(ISO)4E; Synonyms=LSP1; OrderedLocusNames=At5g35620;
GN ORFNames=MJE4.8;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9234949; DOI=10.1006/viro.1997.8634;
RA Wittmann S., Chatel H., Fortin M.G., Laliberte J.F.;
RT "Interaction of the viral protein genome linked of turnip mosaic potyvirus
RT with the translational eukaryotic initiation factor (iso) 4E of Arabidopsis
RT thaliana using the yeast two-hybrid system.";
RL Virology 234:84-92(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=12123581; DOI=10.1016/s0960-9822(02)00898-9;
RA Lellis A.D., Kasschau K.D., Whitham S.A., Carrington J.C.;
RT "Loss-of-susceptibility mutants of Arabidopsis thaliana reveal an essential
RT role for eIF(iso)4E during potyvirus infection.";
RL Curr. Biol. 12:1046-1051(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Rodriguez C.M., Freire M.A., Robaglia C.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH LOX2.
RX PubMed=11117257; DOI=10.1023/a:1006494628892;
RA Freire M.A., Tourneur C., Granier F., Camonis J., El Amrani A.,
RA Browning K.S., Robaglia C.;
RT "Plant lipoxygenase 2 is a translation initiation factor-4E-binding
RT protein.";
RL Plant Mol. Biol. 44:129-140(2000).
RN [10]
RP INTERACTION WITH BTF3.
RX PubMed=15716105; DOI=10.1016/j.gene.2004.11.030;
RA Freire M.A.;
RT "Translation initiation factor (iso) 4E interacts with BTF3, the beta
RT subunit of the nascent polypeptide-associated complex.";
RL Gene 345:271-277(2005).
RN [11]
RP REVIEW, AND SUBUNIT.
RX PubMed=16343979; DOI=10.1016/j.tplants.2005.11.004;
RA Robaglia C., Caranta C.;
RT "Translation initiation factors: a weak link in plant RNA virus
RT infection.";
RL Trends Plant Sci. 11:40-45(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Mediates susceptibility to Turnipmosaic potyvirus
CC (TuMV) and Tobacco etch potyvirus (TEV). {ECO:0000269|PubMed:12123581,
CC ECO:0000269|PubMed:9234949}.
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, EIF4E and EIF4G. EIF4E is also known to
CC interact with other partners. In higher plants two isoforms of EIF4F
CC have been identified, named isoform EIF4F and isoform EIF(iso)4F.
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28. This isoform interacts with the viral protein
CC genome linked (VPg)-proteinase of turnip mosaic potyvirus. Interacts
CC directly with LOX2. Interacts with BTF3 (PubMed:15716105).
CC {ECO:0000269|PubMed:11117257, ECO:0000269|PubMed:15716105,
CC ECO:0000269|PubMed:16343979}.
CC -!- INTERACTION:
CC O04663; Q9SMW7: BTF3; NbExp=2; IntAct=EBI-1770425, EBI-1770592;
CC O04663; P38418: LOX2; NbExp=7; IntAct=EBI-1770425, EBI-1770437;
CC O04663; Q03389; Xeno; NbExp=3; IntAct=EBI-1770425, EBI-1770460;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04663-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04663-2; Sequence=VSP_037805, VSP_037806;
CC -!- TISSUE SPECIFICITY: Abundant in floral organs and in young developing
CC tissues. {ECO:0000269|PubMed:9234949}.
CC -!- PTM: According to the redox status, the Cys-97-Cys-138 disulfide bridge
CC may have a role in regulating protein function by affecting its ability
CC to bind capped mRNA. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Decreased susceptibility to TuMV and TEV.
CC {ECO:0000269|PubMed:12123581}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB66906.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U62044; AAB66906.1; ALT_INIT; mRNA.
DR EMBL; AF538308; AAN06825.1; -; Genomic_DNA.
DR EMBL; Y10547; CAA71579.1; -; mRNA.
DR EMBL; AB013393; BAB09303.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93991.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93992.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70787.1; -; Genomic_DNA.
DR EMBL; AY054630; AAK96821.1; -; mRNA.
DR EMBL; AY081514; AAM10076.1; -; mRNA.
DR EMBL; BX831945; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY086315; AAM64386.1; -; mRNA.
DR RefSeq; NP_001332369.1; NM_001344112.1. [O04663-1]
DR RefSeq; NP_198412.1; NM_122953.3. [O04663-1]
DR RefSeq; NP_974852.1; NM_203123.1. [O04663-2]
DR AlphaFoldDB; O04663; -.
DR SMR; O04663; -.
DR BioGRID; 18787; 4.
DR IntAct; O04663; 6.
DR MINT; O04663; -.
DR STRING; 3702.AT5G35620.1; -.
DR iPTMnet; O04663; -.
DR PaxDb; O04663; -.
DR PRIDE; O04663; -.
DR ProteomicsDB; 250674; -. [O04663-1]
DR EnsemblPlants; AT5G35620.1; AT5G35620.1; AT5G35620. [O04663-1]
DR EnsemblPlants; AT5G35620.2; AT5G35620.2; AT5G35620. [O04663-2]
DR EnsemblPlants; AT5G35620.3; AT5G35620.3; AT5G35620. [O04663-1]
DR GeneID; 833534; -.
DR Gramene; AT5G35620.1; AT5G35620.1; AT5G35620. [O04663-1]
DR Gramene; AT5G35620.2; AT5G35620.2; AT5G35620. [O04663-2]
DR Gramene; AT5G35620.3; AT5G35620.3; AT5G35620. [O04663-1]
DR KEGG; ath:AT5G35620; -.
DR Araport; AT5G35620; -.
DR TAIR; locus:2165892; AT5G35620.
DR eggNOG; KOG1670; Eukaryota.
DR InParanoid; O04663; -.
DR OMA; LGYGCDY; -.
DR PhylomeDB; O04663; -.
DR PRO; PR:O04663; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O04663; baseline and differential.
DR Genevisible; O04663; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:TAIR.
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 Acetylation; Alternative splicing; Disulfide bond; Initiation factor;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..198
FT /note="Eukaryotic translation initiation factor isoform 4E"
FT /id="PRO_0000193655"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46..47
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"
FT BINDING 92..93
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"
FT BINDING 145..152
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 97..138
FT /evidence="ECO:0000250"
FT VAR_SEQ 167
FT /note="M -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_037805"
FT VAR_SEQ 168..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_037806"
FT CONFLICT 144
FT /note="V -> F (in Ref. 6; BX831945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 22514 MW; 71FEB309E073A9D2 CRC64;
MATDDVNEPL PAAAELPATE AEKQPHKLER KWSFWFDNQS KKGAAWGASL RKAYTFDTVE
DFWGLHETIF QTSKLTANAE IHLFKAGVEP KWEDPECANG GKWTWVVTAN RKEALDKGWL
ETLMALIGEQ FDEADEICGV VASVRPQSKQ DKLSLWTRTK SNEAVLMGIG KKWKEILDVT
DKITFNNHDD SRRSRFTV
