IF4E1_TOBAC
ID IF4E1_TOBAC Reviewed; 222 AA.
AC A0A075QQ08; A0A7H1JMP3; D3UW24;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:21525344, ECO:0000303|Ref.2};
DE Short=NteIF4E1 {ECO:0000303|PubMed:15988567};
DE Short=eIF4E-1 {ECO:0000303|PubMed:21525344};
DE AltName: Full=Eukaryotic translation initiation factor 4E2-T {ECO:0000303|Ref.3};
DE Short=eIF4E2-T {ECO:0000303|Ref.3};
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=eIF4E {ECO:0000303|PubMed:21525344, ECO:0000303|Ref.2};
GN Synonyms=EIF4E2-T {ECO:0000303|Ref.3}, T015277 {ECO:0000303|Ref.2};
GN ORFNames=LOC107829212 {ECO:0000312|RefSeq:XP_016512167.1};
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].
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), 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
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 [6]
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
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.2).
CC {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.2}.
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.2}.
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:P29557}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm
CC {ECO:0000250|UniProtKB:K0P2S0}.
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.2).
CC {ECO:0000269|PubMed:15988567, ECO:0000269|Ref.2}.
CC -!- PTM: According to the redox status, the Cys-120-Cys-158 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: Plants lacking both eIF4E and eIFiso4E are semi-
CC dwarf and exhibit an overall reduction in polyribosome loading.
CC {ECO:0000269|PubMed:15988567}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; FN666433; CBJ34332.1; -; mRNA.
DR EMBL; KM202067; AIG20720.1; -; mRNA.
DR EMBL; MN897003; QNT12790.1; -; mRNA.
DR RefSeq; NP_001313148.1; NM_001326219.1.
DR RefSeq; XP_016512167.1; XM_016656681.1.
DR SMR; A0A075QQ08; -.
DR STRING; 4097.A0A075QQ08; -.
DR GeneID; 107829212; -.
DR KEGG; nta:107829212; -.
DR OMA; NKFGGRW; -.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000084051; Unplaced.
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; 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 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 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Initiation factor; Nucleus; Plant defense;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..222
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454055"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..50
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 57..93
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 141..150
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 65..70
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 97
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 115..116
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 165..170
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 210..214
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 120..158
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT CONFLICT 186
FT /note="S -> C (in Ref. 3; QNT12790)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="I -> V (in Ref. 1; CBJ34332)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25217 MW; AC9D47C1ECA0BD28 CRC64;
MVDEVEKPAS LEESKTNTRE VEEGAEEVIE SDDTMSSLGN PCKAMKHPLE HSWTFWFDNP
SGKSKQAAWG SSIRPIYTFS TVEDFWSVYN NIHHPSKLAV GADFHCFKNK IEPKWEDPVC
ASGGKWTMSF SRGKSDTCWL YTLLAMIGEQ FDCGDEICGA VINVRVRQEK IALWTRNAAN
ETAQVSIGKQ WKEFLDYNDS IGFIFHDDAK KLDRAAKNRY SV
