IF4E1_SOLLC
ID IF4E1_SOLLC Reviewed; 231 AA.
AC Q4VQY3; A0A1D8EJF6; Q199B8; Q199B9; Q199C0; Q4VQY2; Q9M4R8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:15971038};
DE Short=eIF4E-1 {ECO:0000303|PubMed:15971038, ECO:0000303|PubMed:20593023};
DE AltName: Full=eIF-4F 25 kDa subunit {ECO:0000305};
DE AltName: Full=eIF-4F p26 subunit {ECO:0000305};
DE AltName: Full=mRNA cap-binding protein {ECO:0000305};
GN Name=eIF4E1 {ECO:0000303|PubMed:15971038, ECO:0000303|PubMed:20593023,
GN ECO:0000303|PubMed:27655175}; Synonyms=POT-1 {ECO:0000303|PubMed:15971038};
GN OrderedLocusNames=Solyc03g005870 {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. VF36;
RX PubMed=10915600; DOI=10.1006/viro.2000.0416;
RA Schaad M.C., Anderberg R.J., Carrington J.C.;
RT "Strain-specific interaction of the tobacco etch virus NIa protein with the
RT translation initiation factor eIF4E in the yeast two-hybrid system.";
RL Virology 273:300-306(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. MicroTom;
RA Ruffel S., Moretti A., Palloix A., Lesage M.-L., Caranta C.;
RT "Amino acid polymorphism in the eukaryotic translation initiation factor 4E
RT determines resistance against several potyviruses in tomato and pepper.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND FUNCTION (MICROBIAL INFECTION).
RC STRAIN=cv. Mospomorist;
RX PubMed=15971038; DOI=10.1007/s00438-005-0003-x;
RA Ruffel S., Gallois J.L., Lesage M.L., Caranta C.;
RT "The recessive potyvirus resistance gene pot-1 is the tomato orthologue of
RT the pepper pvr2-eIF4E gene.";
RL Mol. Genet. Genomics 274:346-353(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Zhongshu No5;
RA Zhang Y., Li H., Ye Z.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND FUNCTION (MICROBIAL
RP INFECTION).
RC STRAIN=cv. M82;
RX PubMed=20593023; DOI=10.1371/journal.pone.0011313;
RA Piron F., Nicolai M., Minoia S., Piednoir E., Moretti A., Salgues A.,
RA Zamir D., Caranta C., Bendahmane A.;
RT "An induced mutation in tomato eIF4E leads to immunity to two
RT potyviruses.";
RL PLoS ONE 5:e11313-e11313(2010).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP DISRUPTION PHENOTYPE, VARIANTS LYS-54; VAL-58; GLY-112 AND MET-151, AND
RP POLYMORPHISM.
RC STRAIN=cv. M82;
RX PubMed=27655175; DOI=10.1099/jgv.0.000609;
RA Lebaron C., Rosado A., Sauvage C., Gauffier C., German-Retana S., Moury B.,
RA Gallois J.-L.;
RT "A new eIF4E1 allele characterized by RNAseq data mining is associated with
RT resistance to potato virus Y in tomato albeit with a low durability.";
RL J. Gen. Virol. 97:3063-3072(2016).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [8]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, AND
RP INTERACTION WITH POTYVIRUS VPG (MICROBIAL INFECTION).
RC STRAIN=cv. WVA106;
RX PubMed=22242134; DOI=10.1371/journal.pone.0029595;
RA Mazier M., Flamain F., Nicolai M., Sarnette V., Caranta C.;
RT "Knock-down of both eIF4E1 and eIF4E2 genes confers broad-spectrum
RT resistance against potyviruses in tomato.";
RL PLoS ONE 6:e29595-e29595(2011).
RN [9]
RP GENE FAMILY, AND REVIEW.
RX PubMed=24309680; DOI=10.1016/j.meegid.2013.11.024;
RA Moury B., Charron C., Janzac B., Simon V., Gallois J.L., Palloix A.,
RA Caranta C.;
RT "Evolution of plant eukaryotic initiation factor 4E (eIF4E) and potyvirus
RT genome-linked protein (VPg): a game of mirrors impacting resistance
RT spectrum and durability.";
RL Infect. Genet. Evol. 27:472-480(2014).
RN [10]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE, VARIANTS
RP PHE-48; LYS-68; SER-69; ASP-77; LEU-85; ILE-109; GLN-123 AND SER-224, AND
RP POLYMORPHISM.
RC STRAIN=cv. M82;
RX PubMed=26850324; DOI=10.1111/tpj.13136;
RA Gauffier C., Lebaron C., Moretti A., Constant C., Moquet F., Bonnet G.,
RA Caranta C., Gallois J.-L.;
RT "A TILLING approach to generate broad-spectrum resistance to potyviruses in
RT tomato is hampered by eIF4E gene redundancy.";
RL Plant J. 85:717-729(2016).
RN [11]
RP FUNCTION, AND FUNCTION (MICROBIAL INFECTION).
RC STRAIN=cv. MicroTom;
RX PubMed=32849681; DOI=10.3389/fpls.2020.01098;
RA Yoon Y.-J., Venkatesh J., Lee J.-H., Kim J., Lee H.-E., Kim D.-S.,
RA Kang B.-C.;
RT "Genome editing of eIF4E1 in tomato confers resistance to pepper mottle
RT virus.";
RL Front. Plant Sci. 11:1098-1098(2020).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome
CC (PubMed:20593023, PubMed:26850324). Recognizes and binds the 7-
CC methylguanosine-containing mRNA cap during an early step in the
CC initiation of protein synthesis and facilitates ribosome binding by
CC inducing the unwinding of the mRNAs secondary structures
CC (PubMed:26850324). Key component of recessive resistance to potyviruses
CC (PubMed:15971038, PubMed:20593023, PubMed:27655175, PubMed:22242134,
CC PubMed:26850324, PubMed:32849681). {ECO:0000269|PubMed:15971038,
CC ECO:0000269|PubMed:20593023, ECO:0000269|PubMed:22242134,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175,
CC ECO:0000269|PubMed:32849681}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. potato virus Y (PVY), pepper mottle virus
CC (PepMoV) and tobacco etch virus (TEV)) by recruiting viral RNAs to the
CC host ribosomal complex via an interaction with viral genome-linked
CC protein (VPg). {ECO:0000269|PubMed:15971038,
CC ECO:0000269|PubMed:20593023, ECO:0000269|PubMed:22242134,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175,
CC ECO:0000269|PubMed:32849681}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions (By
CC similarity). It is composed of at least EIF4A, EIF4E and EIF4G. EIF4E
CC is also known to interact with other partners (By similarity). In
CC higher plants two isoforms of EIF4F have been identified, named isoform
CC EIF4F and isoform EIF(iso)4F (By similarity). Isoform EIF4F has
CC subunits p220 and p26, whereas isoform EIF(iso)4F has subunits p82 and
CC p28 (By similarity). {ECO:0000250|UniProtKB:P29557}.
CC -!- SUBUNIT: (Microbial infection) Interacts with potyvirus viral genome-
CC linked protein (VPg); mostly with tobacco etch virus (TEV-HAT) VPg and,
CC to a lower extent, with potato virus Y (PVY-LYE84 and PVY-LYE90) and
CC pepper mottle virus (PepMoV) VPg. {ECO:0000269|PubMed:22242134}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}.
CC -!- PTM: According to the redox status, the Cys-129-Cys-167 disulfide
CC bridge may have a role in regulating protein function by affecting its
CC ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
CC -!- POLYMORPHISM: Variant present in the allele pot1(2), haplotypes 1 and
CC 4, is associated with an increased resistance to potato virus Y (PVY)
CC isolate N605. {ECO:0000269|PubMed:27655175}.
CC -!- POLYMORPHISM: Variant present in the allele pot-1 is associated with a
CC functionnal mRNA capping activity and normal susceptibility to
CC potyviruses (e.g. pepper mottle virus (PepMoV), potato virus Y (PVY)
CC and tobacco etch virus (TEV)). {ECO:0000269|PubMed:26850324}.
CC -!- DISRUPTION PHENOTYPE: Impaired mRNA capping activity (PubMed:26850324).
CC Slightly impaired growth and fertility (PubMed:22242134). Increased
CC resistance to pepper mottle virus (PepMoV) and potato virus Y (PVY)
CC strain LYE90 but not to PVY strains N605, LYE72, SON41 and LYE84 and to
CC tobacco etch virus (TEV) strains HAT, CAA10 and S103 (PubMed:26850324).
CC Plants lacking both eIF4E1 and eIF4E2 display pleiotropic effect on
CC plant development but are resistant specifically to several potyviruses
CC including potato virus Y (PVY, strains N605, LYE72, LYE90 and LYE84),
CC tobacco etch virus (TEV, strains HAT, CAA10 and S103), pepper mottle
CC virus (PepMoV), Ecuadorian rocotto virus (ERV), pepper severe mosaic
CC virus (PepSMV), pepper yellow mosaic virus (PepYMV), and potato virus V
CC (PVV) (PubMed:27655175, PubMed:22242134, PubMed:26850324). Plants
CC lacking eIFiso4E, eIF4E1 and eIF4E2 exhibit a semi-dwarf phenotype
CC (PubMed:22242134). {ECO:0000269|PubMed:22242134,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.
CC -!- MISCELLANEOUS: Displayed sequence is cv. Mospomorist and cv. M82, and
CC confers susceptibility to potyviruses (e.g. potato virus Y (PVY) and
CC tobacco etch virus (TEV)). {ECO:0000269|PubMed:15971038}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AF259801; AAF70507.1; -; mRNA.
DR EMBL; AY723734; AAV88611.1; -; mRNA.
DR EMBL; AY723733; AAV88610.1; -; mRNA.
DR EMBL; DQ537341; ABF83562.1; -; mRNA.
DR EMBL; DQ537342; ABF83563.1; -; mRNA.
DR EMBL; DQ537343; ABF83564.1; -; mRNA.
DR EMBL; KX855953; AOT21124.1; -; mRNA.
DR EMBL; GQ451830; ACV74551.1; -; Genomic_DNA.
DR RefSeq; NP_001234459.2; NM_001247530.2.
DR SMR; Q4VQY3; -.
DR STRING; 4081.Solyc03g005870.2.1; -.
DR PaxDb; Q4VQY3; -.
DR PRIDE; Q4VQY3; -.
DR EnsemblPlants; Solyc03g005870.3.1; Solyc03g005870.3.1; Solyc03g005870.3.
DR GeneID; 543653; -.
DR Gramene; Solyc03g005870.3.1; Solyc03g005870.3.1; Solyc03g005870.3.
DR KEGG; sly:543653; -.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR InParanoid; Q4VQY3; -.
DR OMA; WHDLLLC; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; Q4VQY3; -.
DR Proteomes; UP000004994; Chromosome 3.
DR ExpressionAtlas; Q4VQY3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0051607; P:defense response to virus; ISS:UniProtKB.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Host-virus interaction; Initiation factor;
KW Nucleus; Plant defense; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..231
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454060"
FT REGION 56..59
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 66..102
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 150..159
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT BINDING 74..79
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:P29557"
FT BINDING 106
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:P29557"
FT BINDING 124..125
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:P29557"
FT BINDING 174..179
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:P29557"
FT BINDING 219..223
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:Q00LS8"
FT DISULFID 129..167
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT VARIANT 48
FT /note="L -> F (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 54
FT /note="V -> K (in allele pot1(2), haplotypes 1 and 4)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 58
FT /note="L -> V (in haplotype 2)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 68
FT /note="N -> K (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 69
FT /note="P -> S (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 77
FT /note="A -> D (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 85
FT /note="V -> L (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 109
FT /note="M -> I (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 112
FT /note="D -> G (in allele pot1(2), haplotype 4)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 123
FT /note="K -> Q (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT VARIANT 151
FT /note="T -> M (in haplotype 3)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 224
FT /note="N -> S (in allele pot-1)"
FT /evidence="ECO:0000269|PubMed:26850324"
FT CONFLICT 13
FT /note="D -> N (in Ref. 4; ABF83563)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="E -> G (in Ref. 4; ABF83562)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="G -> E (in Ref. 4; ABF83564)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="D -> N (in Ref. 1; AAF70507)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> N (in Ref. 2; AAV88611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 26042 MW; 0DBFA3141790555C CRC64;
MAAAEMERTM SFDAAEKLKA ADGGGGEVDD ELEEGEIVEE SNDTASYLGK EITVKHPLEH
SWTFWFDNPT TKSRQTAWGS SLRNVYTFST VEDFWGAYNN IHHPSKLIMG ADFHCFKHKI
EPKWEDPVCA NGGTWKMSFS KGKSDTSWLY TLLAMIGHQF DHGDEICGAV VSVRAKGEKI
ALWTKNAANE TAQVSIGKQW KQFLDYSDSV GFIFHDDAKR LDRNAKNRYT V
