IFI4E_TOBAC
ID IFI4E_TOBAC Reviewed; 200 AA.
AC Q66WU1; A0A075QPA9; A0A075QVP6; A0A1J0FAS8; A0A7H1JMP5; D3UW25; U6BL55;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4E {ECO:0000303|PubMed:15988567, ECO:0000303|Ref.3, ECO:0000303|Ref.5};
DE Short=eIF(iso)-4E {ECO:0000303|PubMed:15988567, ECO:0000303|Ref.3};
DE Short=eIF(iso)4E {ECO:0000303|PubMed:15988567, ECO:0000303|Ref.3};
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:15988567, ECO:0000303|Ref.3};
GN Synonyms=eIF4E2a {ECO:0000303|Ref.5}, S10809 {ECO:0000303|Ref.4},
GN T024242 {ECO:0000303|Ref.4};
GN ORFNames=LOC107780685 {ECO:0000312|RefSeq:XP_016456737.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC STRAIN=cv. Samsun;
RX PubMed=15988567; DOI=10.1007/s11103-005-3098-x;
RA Combe J.P., Petracek M.E., van Eldik G., Meulewaeter F., Twell D.;
RT "Translation initiation factors eIF4E and eIFiso4E are required for
RT polysome formation and regulate plant growth in tobacco.";
RL Plant Mol. Biol. 57:749-760(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-7; 13-PRO--ALA-22 DELINS
RP LEU-PRO-ALA-PRO-ASP-THR-VAL-GLU; 38-ASN--SER-40 DEL; 47-ALA--SER-51 DELINS
RP VAL-TRP-ALA-SER-ALA AND ASN-101.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP SUBUNIT, AND VARIANTS GLY-8 AND ILE-107.
RC STRAIN=cv. Bright Yellow 2, cv. KF118, cv. KF120, cv. KY14,
RC cv. Petit Havana, cv. Samsun, cv. Virginia Bright, and cv. Xanthi;
RX DOI=10.1007/s13580-013-0045-7;
RA Yeam I., Jung J.;
RT "Exploring natural variations in eIF4E and screening for potyviral
RT resistance in diverse Nicotiana species.";
RL Horticult. Environ. Biotechnol. 54:430-440(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS 13-PRO--ALA-22 DELINS
RP LEU-PRO-ALA-PRO-ASP-THR-VAL-GLU; 38-ASN--SER-40 DEL; 47-ALA--SER-51 DELINS
RP VAL-TRP-ALA-SER-ALA; ASN-101; 149-ASP--GLU-178
RP DELINS ARG-ARG-TYR-VAL-GLU-TRP-LEU-PRO-VAL-TYR-VAL-GLY-VAL-ARG-ILE-ASN-PHE-
RP PRO-TYR-GLY-LEU-ARG-LEU-PRO-PRO-MET-LYS-GLN-PHE-ARG; ARG-156; ALA-163;
RP 179-LYS--VAL-200 DEL AND 190-ARG--ALA-194 DELINS LYS-GLU-ARG-SER-VAL, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Leaf, Root, and Stem;
RX DOI=10.1007/s11105-014-0775-4;
RA Julio E., Cotucheau J., Decorps C., Volpatti R., Sentenac C., Candresse T.,
RA Dorlhac de Borne F.;
RT "A Eukaryotic Translation Initiation Factor 4E (eIF4E) is Responsible for
RT the 'va' Tobacco Recessive Resistance to Potyviruses.";
RL Plant Mol. Biol. Rep. 33:609-623(2015).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS 13-PRO--ALA-22 DELINS
RP LEU-PRO-ALA-PRO-ASP-THR-VAL-GLU; 38-ASN--SER-40 DEL; 47-ALA--SER-51 DELINS
RP VAL-TRP-ALA-SER-ALA; ASN-101; ARG-156; ALA-163 AND LYS-190.
RA Yang D.-H.;
RT "TALEN-mediated mutagenesis of NteIF4E1a leads to Patato virus Y (PVY)
RT resistance in cultivated tobacco (Nicotana tobacum).";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-165, AND VARIANTS 13-PRO--ALA-22
RP DELINS LEU-PRO-ALA-PRO-ASP-THR-VAL-GLU; 38-ASN--SER-40 DEL; 47-ALA--SER-51
RP DELINS VAL-TRP-ALA-SER-ALA; ASN-101; ARG-156; ALA-163; VAL-165 AND
RP 190-ARG--ALA-194 DELINS LYS-GLU-ARG-SER-VAL.
RA Liu Y., Huang C., Li Z.;
RT "Simultaneous mutation of multiple eukaryotic translation-initiation factor
RT genes by CRISPR/Cas9 confers durable and broad resistance to potyviruses in
RT tobacco.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90;
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(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
CC (PubMed:15988567). Recognizes and binds the 7-methylguanosine-
CC containing mRNA cap during an early step in the initiation of protein
CC synthesis and facilitates ribosome binding by inducing the unwinding of
CC the mRNAs secondary structures (PubMed:15988567). Key component of
CC recessive resistance to potyviruses (Ref.3).
CC {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.3}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. potato virus Y (PVY) and pepper mottle virus
CC (PepMoV)) by recruiting viral RNAs to the host ribosomal complex via an
CC interaction with viral genome-linked protein (VPg).
CC {ECO:0000269|Ref.3}.
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 (By
CC similarity). In higher plants two isoforms of EIF4F have been
CC identified, named isoform EIF4F and isoform EIF(iso)4F (By similarity).
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28 (By similarity). {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.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}.
CC Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=NteIFiso4E1 {ECO:0000303|PubMed:15988567};
CC IsoId=Q66WU1-1; Sequence=Displayed;
CC Name=2; Synonyms=NteIFiso4E2 {ECO:0000303|PubMed:15988567};
CC IsoId=Q66WU1-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in seedlings, roots, leaves,
CC sepals, petals, anthers and dehisced pollen, with highest levels in
CC pollen, maturing anthers and roots (PubMed:15988567). Strongly
CC expressed in susceptible plants but not in resistant ones (Ref.4).
CC {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.4}.
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 -!- DISRUPTION PHENOTYPE: Plants lacking both eIF4E and eIFiso4E are semi-
CC dwarf and exhibit an overall reduction in polyribosome loading.
CC {ECO:0000269|PubMed:15988567}.
CC -!- MISCELLANEOUS: Displayed sequence is allele 2 / eIF4E2a.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AY699609; AAU06579.1; -; mRNA.
DR EMBL; FN666434; CBJ34333.1; -; mRNA.
DR EMBL; KC625587; AHA36694.1; -; mRNA.
DR EMBL; KC625588; AHA36695.1; -; mRNA.
DR EMBL; KC625589; AHA36696.1; -; mRNA.
DR EMBL; KC625590; AHA36697.1; -; mRNA.
DR EMBL; KC625591; AHA36698.1; -; mRNA.
DR EMBL; KC625592; AHA36699.1; -; mRNA.
DR EMBL; KC625593; AHA36700.1; -; mRNA.
DR EMBL; KC625594; AHA36701.1; -; mRNA.
DR EMBL; KC625595; AHA36702.1; -; mRNA.
DR EMBL; KM202065; AIG20718.1; -; mRNA.
DR EMBL; KM202066; AIG20719.1; -; mRNA.
DR EMBL; KX000389; APC26091.1; -; mRNA.
DR EMBL; KX000390; APC26092.1; -; mRNA.
DR EMBL; MN897004; QNT12791.1; -; mRNA.
DR EMBL; MN897005; QNT12792.1; -; mRNA.
DR RefSeq; XP_016456737.1; XM_016601251.1.
DR SMR; Q66WU1; -.
DR STRING; 4097.A0A075QPA9; -.
DR GeneID; 107780685; -.
DR KEGG; nta:107780685; -.
DR OMA; LGYGCDY; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; Q66WU1; -.
DR Proteomes; UP000084051; Unplaced.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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 Alternative splicing; Cytoplasm; Disulfide bond; Host-virus interaction;
KW Initiation factor; Nucleus; Plant defense; Protein biosynthesis;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..200
FT /note="Eukaryotic translation initiation factor isoform 4E"
FT /id="PRO_0000454075"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 7
FT /note="I -> V (in allele A)"
FT /evidence="ECO:0000269|PubMed:21525344"
FT VARIANT 8
FT /note="E -> G (in strain: Xanthi; allele 1)"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 13..22
FT /note="PPASATETVA -> LPAPDTVE (in strain: T024242; alleles
FT A, eIF4E2b and eIFiso4E-T)"
FT /evidence="ECO:0000269|PubMed:21525344, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT VARIANT 38..40
FT /note="Missing (in strain: T024242; alleles A, eIF4E2b and
FT eIFiso4E-T)"
FT /evidence="ECO:0000269|PubMed:21525344, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT VARIANT 47..51
FT /note="AWGSS -> VWASA (in strain: T024242; alleles A,
FT eIF4E2b and eIFiso4E-T)"
FT /evidence="ECO:0000269|PubMed:21525344, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT VARIANT 101
FT /note="S -> N (in strain: T024242; alleles A, eIF4E2b and
FT eIFiso4E-T)"
FT /evidence="ECO:0000269|PubMed:21525344, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.6"
FT VARIANT 107
FT /note="V -> I (in strain: Xanthi; allele 1)"
FT /evidence="ECO:0000269|Ref.3"
FT VARIANT 149..178
FT /note="DKLSLWTKTASNEAIQMSIGRKWKEIIDAE -> RRYVEWLPVYVGVRINFP
FT YGLRLPPMKQFR (in strain: S10809)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 156
FT /note="K -> R (in strain: T024242; alleles eIF4E2b and
FT eIFiso4E-T)"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT VARIANT 163
FT /note="I -> A (in strain: T024242; alleles eIF4E2b and
FT eIFiso4E-T)"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5,
FT ECO:0000269|Ref.6"
FT VARIANT 165
FT /note="M -> V (in eIFiso4E-S)"
FT /evidence="ECO:0000269|Ref.6"
FT VARIANT 179..200
FT /note="Missing (in strain: S10809)"
FT /evidence="ECO:0000269|Ref.4"
FT VARIANT 190..194
FT /note="RERSA -> KERSV (in strain: T024242; allele eIFiso4E-
FT T)"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT VARIANT 190
FT /note="R -> K (in allele eIF4E2b)"
FT /evidence="ECO:0000269|Ref.5"
SQ SEQUENCE 200 AA; 22852 MW; 6578EC79FD418F60 CRC64;
MATEAPIEAT EVPPASATET VAKQPHKLER RWTFWFDNQS KPKQGAAWGS SLRKAYTFET
VEEFWSLYDQ IFKPSKLTAN ADFHLFKAGI EPKWEDPECA SGGKWTVTSS RKANLETMWL
ETLMALVGEQ FDESEEICGV VASVRRSQDK LSLWTKTASN EAIQMSIGRK WKEIIDAEKI
SYSFHDDSKR ERSAKSRYTV
