IF4EA_SOLTU
ID IF4EA_SOLTU Reviewed; 231 AA.
AC D3UW26; A0A6G5S7W0; G9JJS1; G9JJS2; G9JJS3; M1B1I1; R4HZ52;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Eukaryotic translation initiation factor 4E allele A {ECO:0000303|PubMed:21525344, ECO:0000303|PubMed:31906869};
DE Short=eIF4E-A {ECO:0000303|PubMed:21525344, ECO:0000303|PubMed:31906869};
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=eIF4Ea {ECO:0000303|PubMed:21525344, ECO:0000303|PubMed:21668622,
GN ECO:0000303|PubMed:31906869}; Synonyms=P4Ea {ECO:0000303|PubMed:21525344};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=21525344; DOI=10.1128/jvi.00485-11;
RA Ala-Poikela M.S., Goytia E., Haikonen T., Rajamaeki M.L., Valkonen J.P.T.;
RT "Helper component proteinase of the genus Potyvirus is an interaction
RT partner of translation initiation factors eIF(iso)4E and eIF4E and contains
RT a 4E binding motif.";
RL J. Virol. 85:6784-6794(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP VARIANTS THR-3; ASN-138 AND TYR-206, MUTAGENESIS OF LEU-48; SER-68; PRO-69;
RP ILE-70; ALA-77; LEU-82; MET-109; GLY-110 AND ASP-112, AND SUBUNIT
RP (MICROBIAL INFECTION).
RC STRAIN=cv. Russet Burbank-0;
RX PubMed=21668622; DOI=10.1111/j.1467-7652.2011.00622.x;
RA Cavatorta J., Perez K.W., Gray S.M., Van Eck J., Yeam I., Jahn M.;
RT "Engineering virus resistance using a modified potato gene.";
RL Plant Biotechnol. J. 9:1014-1021(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP VARIANTS ASN-138 AND TYR-206, AND SUBUNIT (MICROBIAL INFECTION).
RC STRAIN=cv. Russet Burbank-0;
RX PubMed=22146867; DOI=10.1007/s11248-011-9576-9;
RA Duan H., Richael C., Rommens C.M.;
RT "Overexpression of the wild potato eIF4E-1 variant Eva1 elicits Potato
RT virus Y resistance in plants silenced for native eIF4E-1.";
RL Transgenic Res. 21:929-938(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lebedeva M.V., Taranov V.V., Babakov A.V.;
RT "Solanum tuberosum cultivar Zhukovskiy ranniy eukaryotic translation
RT initiation factor eIF4E-1 (eIF4E-1) mRNA, eIF4E-1-2 allele.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44;
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-231, FUNCTION, FUNCTION (MICROBIAL
RP INFECTION), AND SUBUNIT (MICROBIAL INFECTION).
RC STRAIN=cv. ATLWT;
RX PubMed=31906869; DOI=10.1186/s12864-019-6423-5;
RA Gutierrez Sanchez P.A., Babujee L., Jaramillo Mesa H., Arcibal E.,
RA Gannon M., Halterman D., Jahn M., Jiang J., Rakotondrafara A.M.;
RT "Overexpression of a modified eIF4E regulates potato virus Y resistance at
RT the transcriptional level in potato.";
RL BMC Genomics 21:18-18(2020).
RN [7]
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).
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:21668622, PubMed:22146867,
CC PubMed:31906869). {ECO:0000250|UniProtKB:P29557,
CC ECO:0000269|PubMed:21668622, ECO:0000269|PubMed:22146867,
CC ECO:0000269|PubMed:31906869}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. Potato virus Y (PVY)) by recruiting viral RNAs to
CC the host ribosomal complex via an interaction with viral genome-linked
CC protein (VPg). {ECO:0000269|PubMed:21668622,
CC ECO:0000269|PubMed:22146867, ECO:0000269|PubMed:31906869}.
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 (By
CC similarity). EIF4E is also known to interact with other partners. 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 viral genome-linked
CC protein (VPg); this interaction is possible in susceptible hosts but
CC impaired in resistant plants. {ECO:0000305|PubMed:21668622,
CC ECO:0000305|PubMed:22146867, ECO:0000305|PubMed:31906869}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm
CC {ECO:0000250|UniProtKB:K0P2S0}.
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 -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; FN666435; CBJ34334.1; -; mRNA.
DR EMBL; JN831440; AEX01233.1; -; mRNA.
DR EMBL; JN831441; AEX01234.1; -; mRNA.
DR EMBL; JN831442; AEX01235.1; -; mRNA.
DR EMBL; JF927213; AEW07371.1; -; mRNA.
DR EMBL; MT828880; QQP16450.1; -; mRNA.
DR EMBL; MK572846; QCI62445.1; -; mRNA.
DR RefSeq; NP_001275360.1; NM_001288431.1.
DR STRING; 4113.PGSC0003DMT400034911; -.
DR GeneID; 102580433; -.
DR KEGG; sot:102580433; -.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR OMA; WHDLLLC; -.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; D3UW26; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; ISS: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 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 allele
FT A"
FT /id="PRO_0000454057"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 3
FT /note="A -> T (in strain: Russet Burbank-0, alleles 1, 2
FT and 3)"
FT /evidence="ECO:0000269|PubMed:21668622"
FT VARIANT 138
FT /note="S -> N (in strain: Russet Burbank-0, allele 1)"
FT /evidence="ECO:0000269|PubMed:21668622,
FT ECO:0000269|PubMed:22146867"
FT VARIANT 206
FT /note="H -> Y (in strain: Russet Burbank-0, allele 1)"
FT /evidence="ECO:0000269|PubMed:21668622,
FT ECO:0000269|PubMed:22146867"
FT MUTAGEN 48
FT /note="L->F: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with K-68, D-77 and I-109."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 68
FT /note="S->K: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with F-48, D-77 and I-109."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 69
FT /note="P->T: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with N-70, R-82, R-110 and
FT N-112."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 70
FT /note="I->E,N: Increased resistance to potyviruses (e.g.
FT potato virus Y (PVY)); when associated with R-82 and N-112.
FT No resistance to potyviruses (e.g. potato virus Y (PVY));
FT when associated with T-69, R-82, R-110 and N-112."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 77
FT /note="A->D: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with F-48, K-68 and I-109."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 82
FT /note="L->R: Increased resistance to potyviruses (e.g.
FT potato virus Y (PVY)); when associated with N-70 or E-70
FT and N-112. No resistance to potyviruses (e.g. potato virus
FT Y (PVY)); when associated with T-69, N-70, R-110 and N-
FT 112."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 109
FT /note="M->I: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with F-48, K-68 and D-77."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 110
FT /note="G->R: No resistance to potyviruses (e.g. potato
FT virus Y (PVY)). No resistance to potyviruses (e.g. potato
FT virus Y (PVY)); when associated with T-69, N-70, R-82 and
FT N-112."
FT /evidence="ECO:0000269|PubMed:21668622"
FT MUTAGEN 112
FT /note="D->N: Increased resistance to potyviruses (e.g.
FT potato virus Y (PVY)); when associated with N-70 or E-70
FT and R-82. No resistance to potyviruses (e.g. potato virus Y
FT (PVY)); when associated with T-69, N-70, R-82 and R-110."
FT /evidence="ECO:0000269|PubMed:21668622"
FT CONFLICT 23
FT /note="A -> G (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="D -> E (in Ref. 1; CBJ34334)"
FT CONFLICT 224
FT /note="S -> N (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25956 MW; C2EDC6BC507CDC6C CRC64;
MAAAEMERTT SFDAAEKLKA ADAGGGEVDD ELEEGEIVEE SNDTASYLGK EITVKHPLEH
SWTFWFDSPI AKSRQTAWGS SLRNVYTFST VEDFWGAYNN IHHPSKLVMG ADFHCFKHKI
EPKWEDPVCA NGGTWKMSFL KGKSDTSWLY TLLAMIGHQF DHGDEICGAV VSVRSKGEKI
ALWTKNAANE TAQVSIGKQW KQFLDHSDSV GFIFHDDAKR LDRSAKNRYT V
