IF4E1_SOLHA
ID IF4E1_SOLHA Reviewed; 231 AA.
AC Q4VQY1; Q4VQY0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:15971038};
DE Short=eIF4E-1 {ECO:0000303|PubMed:15971038};
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:15971038};
OS Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
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=62890;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PHE-48; LYS-68; ASP-77 AND ILE-109,
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), SUBUNIT (MICROBIAL INFECTION),
RP AND POLYMORPHISM.
RC STRAIN=cv. PI 134417, and cv. PI 247087;
RX PubMed=15971038; DOI=10.1007/s00438-005-0003-x;
RA Ruffel S., Gallois J.L., Lesage M.L., Caranta C.;
RT "The recessive potyvirus resistance gene pot-1 is the tomato orthologue of
RT the pepper pvr2-eIF4E gene.";
RL Mol. Genet. Genomics 274:346-353(2005).
RN [2]
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 [3]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), VARIANTS PHE-48; LYS-68; ASP-77
RP AND ILE-109, SUBUNIT (MICROBIAL INFECTION), AND POLYMORPHISM.
RC STRAIN=cv. PI 247087;
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 [4]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), VARIANTS PHE-48; LYS-68; ASP-77
RP AND ILE-109, SUBUNIT (MICROBIAL INFECTION), AND POLYMORPHISM.
RC STRAIN=cv. PI 247087;
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
CC (PubMed:26850324). 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:26850324). Key component of
CC recessive resistance to potyviruses (PubMed:15971038, PubMed:27655175,
CC PubMed:26850324). {ECO:0000269|PubMed:15971038,
CC ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. pepper mottle virus (PepMoV), potato virus Y
CC (PVY) and tobacco etch virus (TEV)) by recruiting viral RNAs to the
CC host ribosomal complex via an interaction with viral genome-linked
CC protein (VPg). {ECO:0000269|PubMed:15971038,
CC ECO:0000269|PubMed:26850324, 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 (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 -!- SUBUNIT: (Microbial infection) Interacts with potyvirus viral genome-
CC linked protein (VPg); this interaction is possible in susceptible hosts
CC but impaired in resistant plants. {ECO:0000305|PubMed:15971038,
CC ECO:0000305|PubMed:26850324, ECO:0000305|PubMed:27655175}.
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 -!- POLYMORPHISM: Variant present in the strain cv. PI 247087, allele pot-
CC 1, exhibits a functionnal mRNA capping activity and an increased
CC resistance to potyviruses (e.g. pepper mottle virus (PepMoV), potato
CC virus Y (PVY) and tobacco etch virus (TEV)).
CC {ECO:0000269|PubMed:15971038, ECO:0000269|PubMed:26850324,
CC ECO:0000269|PubMed:27655175}.
CC -!- MISCELLANEOUS: Displayed sequence is cv. PI 134417 and confers
CC susceptibility to potyviruses (e.g. potato virus Y (PVY) and tobacco
CC etch virus (TEV)). {ECO:0000269|PubMed:15971038,
CC ECO:0000269|PubMed:27655175}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AY723735; AAV88612.1; -; mRNA.
DR EMBL; AY723736; AAV88613.1; -; mRNA.
DR SMR; Q4VQY1; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA: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; RNA-binding;
KW Translation regulation.
FT CHAIN 1..231
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454059"
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 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 48
FT /note="L -> F (in strain: PI 247087, allele pot-1)"
FT /evidence="ECO:0000269|PubMed:15971038,
FT ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175"
FT VARIANT 68
FT /note="N -> K (in strain: PI 247087, allele pot-1)"
FT /evidence="ECO:0000269|PubMed:15971038,
FT ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175"
FT VARIANT 77
FT /note="A -> D (in strain: PI 247087, allele pot-1)"
FT /evidence="ECO:0000269|PubMed:15971038,
FT ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175"
FT VARIANT 109
FT /note="M -> I (in strain: PI 247087, allele pot-1)"
FT /evidence="ECO:0000269|PubMed:15971038,
FT ECO:0000269|PubMed:26850324, ECO:0000269|PubMed:27655175"
SQ SEQUENCE 231 AA; 26019 MW; 17807B424279D5A1 CRC64;
MAAAEMERTM SFDAAEKLKA ADGGGGEVDD ELEEGEIVEE SNDTASYLGK EITVKHPLEH
SWTFWFDNST TKSRQTAWGS SLRNLYTFST VEDFWGAYNN IHHPSKLIMG ADFHCFKHKI
EPQWEDPVCA NGGTWKMSFS KGKSDTSWLY TLLAMIGHQF DHGDEICGAV VSVRAKGEKI
ALWTKNAANE TAQVSIGKQW KQFLDYSDSV GFIFHDDAKR LDRSAKNRYT V
