IF4E2_SOLLC
ID IF4E2_SOLLC Reviewed; 221 AA.
AC A0A3Q7FGP1;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Eukaryotic translation initiation factor 4E-2 {ECO:0000303|PubMed:27655175};
DE Short=eIF4E-2 {ECO:0000303|PubMed:27655175};
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=eIF4E2 {ECO:0000303|PubMed:27655175};
GN OrderedLocusNames=Solyc02g021550 {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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
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 [5]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), AND DISRUPTION PHENOTYPE.
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).
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 (By
CC similarity). 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 (By similarity). Key component of recessive
CC resistance to potyviruses (PubMed:27655175, PubMed:22242134,
CC PubMed:26850324). {ECO:0000250|UniProtKB:P29557,
CC ECO:0000250|UniProtKB:Q4VQY3, ECO:0000269|PubMed:22242134,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. potato virus Y (PVY) and tobacco etch virus
CC (TEV)) by recruiting viral RNAs to the host ribosomal complex via an
CC interaction with viral genome-linked protein (VPg).
CC {ECO:0000269|PubMed:22242134, ECO:0000269|PubMed:26850324,
CC ECO:0000269|PubMed:27655175}.
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) in the nucleus; mostly potato virus Y (PVY-LYE84)
CC and tobacco etch virus (TEV-HAT) VPg, but not with PVY-LYE90 and pepper
CC mottle virus (PepMoV) VPg; these interactions are possible in
CC susceptible hosts but impaired in resistant plants.
CC {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-119-Cys-157 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 -!- DISRUPTION PHENOTYPE: Slightly impaired growth and fertility
CC (PubMed:22242134). Plants lacking both eIF4E1 and eIF4E2 display
CC pleiotropic effect on plant development but are resistant specifically
CC to several potyviruses including potato virus Y (PVY, strains N605,
CC LYE72, LYE90 and LYE84), tobacco etch virus (TEV, strains HAT, CAA10
CC and S103), pepper mottle virus (PepMoV), Ecuadorian rocotto virus
CC (ERV), pepper severe mosaic virus (PepSMV), pepper yellow mosaic virus
CC (PepYMV), and potato virus V (PVV) (PubMed:27655175, PubMed:22242134,
CC PubMed:26850324). Plants lacking eIFiso4E, eIF4E1 and eIF4E2 exhibit a
CC semi-dwarf phenotype (PubMed:22242134). {ECO:0000269|PubMed:22242134,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR RefSeq; NP_001307578.1; NM_001320649.1.
DR SMR; A0A3Q7FGP1; -.
DR STRING; 4081.Solyc02g021550.2.1; -.
DR EnsemblPlants; Solyc02g021550.3.1; Solyc02g021550.3.1; Solyc02g021550.3.
DR GeneID; 101261276; -.
DR Gramene; Solyc02g021550.3.1; Solyc02g021550.3.1; Solyc02g021550.3.
DR KEGG; sly:101261276; -.
DR OMA; NKFGGRW; -.
DR Proteomes; UP000004994; Chromosome 2.
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:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
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 Cytoplasm; Disulfide bond; Host-virus interaction; Initiation factor;
KW Nucleus; Plant defense; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..221
FT /note="Eukaryotic translation initiation factor 4E-2"
FT /id="PRO_0000454061"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..49
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 56..92
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 140..149
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64..69
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 96
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 114..115
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 164..169
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 209..213
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 119..157
FT /evidence="ECO:0000250|UniProtKB:P29557"
SQ SEQUENCE 221 AA; 25104 MW; 85C53D9914662FD2 CRC64;
MADELNKAAL EEYKSSSVED RGEEGEIVGE SDDTASSLGK QITMKHPLEH SWTFWFDNPS
GKSKQAAWGS SIRPIYTFST AEDFWSVYNN IHHPSKLAVG ADFHCFKNKI EPKWEDPVCA
NGGKWTMNFS RGKSDTCWLY TLLALIGEQF DYGDEICGAV INVRVRQEKI ALWTRNAANE
TAQVSIGKQW KEFLDYNDTI GFIFHDDAKK LDRAAKNRYS V
