IFI4E_PRUDO
ID IFI4E_PRUDO Reviewed; 213 AA.
AC M1J8U6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4E {ECO:0000303|PubMed:23382802};
DE Short=eIF(iso)-4E {ECO:0000303|PubMed:23382802};
DE Short=eIF(iso)4E {ECO:0000303|PubMed:23382802};
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=eIF(iso)4E {ECO:0000303|PubMed:23382802};
OS Prunus domestica (Garden plum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3758;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP DISRUPTION PHENOTYPE (MICROBIAL INFECTION), TISSUE SPECIFICITY, INTERACTION
RP WITH POTYVIRUS VPG (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION
RP (MICROBIAL INFECTION).
RX PubMed=23382802; DOI=10.1371/journal.pone.0050627;
RA Wang X., Kohalmi S.E., Svircev A., Wang A., Sanfacon H., Tian L.;
RT "Silencing of the host factor eIF(iso)4E gene confers plum pox virus
RT resistance in plum.";
RL PLoS ONE 8:e50627-e50627(2013).
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 such as the plum pox virus (PPV) strain D
CC (PubMed:23382802). {ECO:0000250|UniProtKB:Q66WU1,
CC ECO:0000269|PubMed:23382802}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection by recruiting viral RNAs to the host ribosomal complex
CC via an interaction with viral genome-linked protein (VPg).
CC {ECO:0000269|PubMed:23382802}.
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:O04663}.
CC -!- SUBUNIT: (Microbial infection) Interacts with potyvirus viral genome-
CC linked protein (VPg) of plum pox virus (PPV) strain D both in nucleus
CC and cytoplasm; this interaction is possible in susceptible hosts but is
CC impaired in resistant plants. {ECO:0000269|PubMed:23382802}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23382802}. Nucleus
CC {ECO:0000269|PubMed:23382802}. Note=(Microbial infection) Binds to
CC potyvirus viral genome-linked protein (VPg) in cytoplasm and nucleus.
CC {ECO:0000269|PubMed:23382802}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, flower buds, leaf buds
CC and anthers, to a lower extent in roots, stems and green immature
CC fruit, and, at low levels, in petals. {ECO:0000269|PubMed:23382802}.
CC -!- PTM: According to the redox status, the Cys-111-Cys-150 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: (Microbial infection) Increased resistance to
CC plum pox virus (PPV) strain D. {ECO:0000269|PubMed:23382802}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; JX137117; AGE81988.1; -; mRNA.
DR SMR; M1J8U6; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP: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 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..213
FT /note="Eukaryotic translation initiation factor isoform 4E"
FT /id="PRO_0000454074"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 56..61
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 88
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..107
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 157..162
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 202..205
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 111..150
FT /evidence="ECO:0000250|UniProtKB:P29557"
SQ SEQUENCE 213 AA; 24074 MW; BD30434D86BE4EF4 CRC64;
MATEVAAAVP PPQLDAEENS GLEAAAAEAK IQPSSGPHKL ERKWTFWFDN QSKPKQGAAW
GSSLRKAYTF ETVQEFWCLY DQVFKPSKFP PNADFHLFRA GVEPKWEDPE CANGGKWTVT
SRSKASLDTM WLETLMALIG EQFDEADEIC GVVASVRQRQ DKLALWTRNA ANEAAQMGIG
RKWKEIIDVT DKITYSFHDD SKRERSAKPR YNV
