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IFI4E_SOLLC
ID   IFI4E_SOLLC             Reviewed;         200 AA.
AC   A0A3Q7I7R4; A7Y4C8; C9E258;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Eukaryotic translation initiation factor isoform 4E {ECO:0000303|PubMed:20593023, ECO:0000303|Ref.1};
DE            Short=SleIF(iso)4E {ECO:0000303|PubMed:20593023, ECO:0000303|Ref.1};
DE            Short=eIF(iso)-4E {ECO:0000303|PubMed:20593023, ECO:0000303|Ref.1};
DE   AltName: Full=eIF-(iso)4F 25 kDa subunit {ECO:0000305};
DE   AltName: Full=eIF-(iso)4F p28 subunit {ECO:0000305};
DE   AltName: Full=mRNA cap-binding protein {ECO:0000305};
GN   Name=eIFiso4E {ECO:0000303|PubMed:20593023, ECO:0000303|Ref.1};
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], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP   VARIANT ARG-87, TISSUE SPECIFICITY, SUBUNIT (MICROBIAL INFECTION), AND
RP   POLYMORPHISM.
RC   STRAIN=cv. Ailsa Craig, and cv. Zhongshu 5;
RX   DOI=10.1007/s11105-009-0090-7;
RA   Zhang Y.-Y., Qi M.-F., Sun J., Zhang X.-H., Shi H.-L., Li H.-X., Ye Z.-B.;
RT   "Molecular Cloning and Characterization of a Gene Encoding Eukaryotic
RT   Initiation Factor iso4E in Tomato (Solanum lycopersicum).";
RL   Plant Mol. Biol. Rep. 27:400-406(2009).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-164.
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   [4]
RP   DISRUPTION PHENOTYPE.
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).
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 (Ref.1). {ECO:0000250|UniProtKB:O04663,
CC       ECO:0000250|UniProtKB:P29557, ECO:0000269|Ref.1}.
CC   -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC       viral infection by recruiting viral RNAs to the host ribosomal complex
CC       via an interaction with viral genome-linked protein (VPg).
CC       {ECO:0000269|Ref.1}.
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. {ECO:0000250|UniProtKB:O04663}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with viral genome-linked
CC       protein (VPg); this interaction is possible in susceptible hosts but
CC       impaired in resistant plants. {ECO:0000305|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}.
CC       Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in roots and leaves, and, to a
CC       lower extent, in stems, flowers and immature green fruits.
CC       {ECO:0000269|Ref.1}.
CC   -!- PTM: According to the redox status, the Cys-99-Cys-138 disulfide bridge
CC       may have a role in regulating protein function by affecting its ability
CC       to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
CC   -!- POLYMORPHISM: Variant present in strain cv. Zhongshu 5, confers an
CC       increased resistance to potyvirus cucumber mosaic virus (CMV) and
CC       tobacco mosaic virus (TMV) and tolerance to plum pox virus (PPV).
CC       {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: No obvious growth defects (PubMed:22242134).
CC       Plants lacking eIFiso4E, eIF4E1 and eIF4E2 exhibit a semi-dwarf
CC       phenotype (PubMed:22242134). {ECO:0000269|PubMed:22242134}.
CC   -!- MISCELLANEOUS: Displayed sequence is from cv. Heinz 1706 and cv. Ailsa
CC       Craig, and is associated with susceptibility to cucumber mosaic virus
CC       (CMV), tobacco mosaic virus (TMV) and plum pox virus (PPV).
CC       {ECO:0000305|Ref.1}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; EU119958; ABV23495.1; -; mRNA.
DR   EMBL; GQ451832; ACV74553.1; -; Genomic_DNA.
DR   RefSeq; NP_001234772.2; NM_001247843.2.
DR   STRING; 4081.Solyc09g090580.2.1; -.
DR   EnsemblPlants; Solyc09g090580.3.1; Solyc09g090580.3.1; Solyc09g090580.3.
DR   GeneID; 100134893; -.
DR   Gramene; Solyc09g090580.3.1; Solyc09g090580.3.1; Solyc09g090580.3.
DR   KEGG; sly:100134893; -.
DR   OMA; LGYGCDY; -.
DR   Proteomes; UP000004994; Chromosome 9.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009615; P:response to virus; IEA:UniProt.
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; Initiation factor; Nucleus;
KW   Protein biosynthesis; Reference proteome; RNA-binding;
KW   Translation regulation.
FT   CHAIN           1..200
FT                   /note="Eukaryotic translation initiation factor isoform 4E"
FT                   /id="PRO_0000454076"
FT   BINDING         44..49
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         76
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         94..95
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         145..150
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         189..192
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        99..138
FT                   /evidence="ECO:0000250|UniProtKB:P29557"
FT   VARIANT         87
FT                   /note="K -> R (in strain: cv. Zhongshu 5)"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   200 AA;  22823 MW;  A07EDAF821588876 CRC64;
     MATEAPVEAT EIPSVAAAET VEKQPHKLER KWTFWFDNQS KPKQGVAWGS SLRKAYTFET
     VEEFWSLYDQ IFKPSKVTVN ADFHLFKAGI EPKWEDPECA NGGKWTATSS RKANLETMWL
     ETLMALVGEQ FDESEDICGV VASVRRSQDK LSLWTKTATN EAAQMGIGRK WKEIIDAEKI
     SYSFHDDSKR ERSAKSRYTV
 
 
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