IF4E1_SOLPI
ID IF4E1_SOLPI Reviewed; 231 AA.
AC A0A1D8EJF9; A0A1D8EJG6; A0A1D8EJG7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:27655175};
DE Short=eIF4E-1 {ECO:0000303|PubMed:27655175};
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=eIF4E1 {ECO:0000303|PubMed:27655175};
OS Solanum pimpinellifolium (Currant tomato) (Lycopersicon pimpinellifolium).
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=4084;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP VARIANTS LYS-54; VAL-58; GLY-112 AND MET-151, SUBUNIT (MICROBIAL
RP INFECTION), AND POLYMORPHISM.
RC STRAIN=cv. LA0409, cv. LA0411, cv. LA1245, cv. LA1420, cv. LA1478,
RC cv. LA1582, and cv. LA1593;
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).
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:27655175).
CC {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:27655175}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection (e.g. potato virus Y (PVY) and tobacco etch virus
CC (TEV)) by recruiting viral RNAs to the host ribosomal complex via an
CC interaction with viral genome-linked protein (VPg).
CC {ECO:0000269|PubMed:27655175}.
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: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:27655175}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}. Note=Binds to potyvirus viral genome-
CC linked protein (VPg) in the nucleus and with potyvirus nuclear
CC inclusion protein A (NIa-Pro) and nuclear inclusion protein B (NIb) in
CC the cytoplasm. {ECO:0000250|UniProtKB:C6ZJZ3}.
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 strains cv. LA0411, cv. LA1420 and
CC cv. LA0409, allele pot1(2), haplotypes 1 and 4, is associated with an
CC increased resistance to potato virus Y (PVY) isolates LYE90 and N605
CC but not to PVY isolate SON41g and to tobacco etch virus (TEV) isolates
CC CAA10. {ECO:0000269|PubMed:27655175}.
CC -!- MISCELLANEOUS: Displayed sequence confers sensistivity to potyviruses
CC (e.g. potato virus Y (PVY) and tobacco etch virus (TEV)).
CC {ECO:0000305|PubMed:27655175}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; KX855954; AOT21125.1; -; mRNA.
DR EMBL; KX855955; AOT21126.1; -; mRNA.
DR EMBL; KX855956; AOT21127.1; -; mRNA.
DR SMR; A0A1D8EJF9; -.
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; RNA-binding;
KW Translation regulation.
FT CHAIN 1..231
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454062"
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 54
FT /note="V -> K (in strain: LA0411, LA1420 and LA0409, allele
FT pot1(2), haplotypes 1 and 4)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 58
FT /note="L -> V (in strain: LA1478, LA1582 and LA1593,
FT haplotype 2)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 112
FT /note="D -> G (in strain: LA0411, allele pot1(2), haplotype
FT 4)"
FT /evidence="ECO:0000269|PubMed:27655175"
FT VARIANT 151
FT /note="T -> M (in strain: LA1245, haplotype 3)"
FT /evidence="ECO:0000269|PubMed:27655175"
SQ SEQUENCE 231 AA; 26042 MW; 0DBFA3141790555C CRC64;
MAAAEMERTM SFDAAEKLKA ADGGGGEVDD ELEEGEIVEE SNDTASYLGK EITVKHPLEH
SWTFWFDNPT TKSRQTAWGS SLRNVYTFST VEDFWGAYNN IHHPSKLIMG ADFHCFKHKI
EPKWEDPVCA NGGTWKMSFS KGKSDTSWLY TLLAMIGHQF DHGDEICGAV VSVRAKGEKI
ALWTKNAANE TAQVSIGKQW KQFLDYSDSV GFIFHDDAKR LDRNAKNRYT V
