IF4E1_CUCZE
ID IF4E1_CUCZE Reviewed; 235 AA.
AC A7KWF8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:17584936, ECO:0000303|PubMed:24309680};
DE Short=Cz-eIF4E-1 {ECO:0000303|PubMed:17584936};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:24309680};
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:17584936, ECO:0000303|PubMed:24309680};
OS Cucumis zeyherii (Wild cucumber) (Cucumis prophetarum subsp. zeyheri).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=61887;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION), AND
RP SUBUNIT (MICROBIAL INFECTION).
RC STRAIN=cv. C-277;
RX PubMed=17584936; DOI=10.1186/1471-2229-7-34;
RA Nieto C., Piron F., Dalmais M., Marco C.F., Moriones E.,
RA Gomez-Guillamon M.L., Truniger V., Gomez P., Garcia-Mas J., Aranda M.A.,
RA Bendahmane A.;
RT "EcoTILLING for the identification of allelic variants of melon eIF4E, a
RT factor that controls virus susceptibility.";
RL BMC Plant Biol. 7:34-34(2007).
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).
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:17584936).
CC {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:17584936}.
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:17584936}.
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:17584936}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm
CC {ECO:0000250|UniProtKB:C6ZJZ3}.
CC -!- PTM: According to the redox status, the Cys-133-Cys-171 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 -!- MISCELLANEOUS: Displayed sequence is from cv. C-277 and confers
CC resistance to melon necrotic spot virus (MNSV) isolates Malpha5 and
CC 264. {ECO:0000269|PubMed:17584936}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; EF595685; ABS18380.1; -; mRNA.
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 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..235
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454071"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..63
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 70..106
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 154..163
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..83
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 110
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 128..129
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 178..183
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 223..227
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 133..171
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
SQ SEQUENCE 235 AA; 26514 MW; D03CAF2EAA56D45B CRC64;
MVVEDTIKAT SAEDLSNSIA NQNPRGRGGE EDEELEEGEI VGDDDLDSSN LSAALVHQPN
PLEHSWTFWF DNPSAKSKQA TWGASIRPIY TFSTVEEFWS VYNNIHHPSK LAMRADLYCF
KHKIEPKWED PVCANGGKWT VNFPRGKSDN GWLYTLLAMI GEQFDCGDEI CGAVVNVRSG
QDKISIWTKN ASNEAAQASI GKQWKEFLDY NESIGFIFHD DAKKFDRHAK NKYMA
