IF4E1_CUCME
ID IF4E1_CUCME Reviewed; 235 AA.
AC Q00LS8; A0A5A7UUA1; Q00LT0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:17026540};
DE Short=Cm-eIF4E {ECO:0000303|PubMed:17026540};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:17026540};
DE Short=eIF4E-1 {ECO:0000303|PubMed:17026540};
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:0000303|PubMed:17026540};
GN Name=eIF4E {ECO:0000303|PubMed:17026540};
GN ORFNames=E6C27_scaffold96G002720 {ECO:0000312|EMBL:KAA0057081.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FUNCTION (MICROBIAL INFECTION),
RP VARIANT LEU-228, SUBUNIT (MICROBIAL INFECTION), AND POLYMORPHISM.
RC STRAIN=cv. PI 161375, cv. Vedrantais, and cv. WMR-29;
RX PubMed=17026540; DOI=10.1111/j.1365-313x.2006.02885.x;
RA Nieto C., Morales M., Orjeda G., Clepet C., Monfort A., Sturbois B.,
RA Puigdomenech P., Pitrat M., Caboche M., Dogimont C., Garcia-Mas J.,
RA Aranda M.A., Bendahmane A.;
RT "An eIF4E allele confers resistance to an uncapped and non-polyadenylated
RT RNA virus in melon.";
RL Plant J. 48:452-462(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92;
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SW 3; TISSUE=Leaf;
RA Kwon S.-Y.;
RT "Draft genome sequences of two oriental melons (Cucumis melo L. var
RT makuwa).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-235 IN COMPLEX WITH
RP 7-METHYLGUANOSINE AND EIF4G, FUNCTION, DISULFIDE BONDS, INTERACTION WITH
RP EIF4G, MUTAGENESIS OF PHE-70; ILE-89; TRP-99 AND TYR-154, AND VARIANT
RP LEU-228.
RC STRAIN=cv. C46;
RX PubMed=28522457; DOI=10.1104/pp.17.00193;
RA Miras M., Truniger V., Silva C., Verdaguer N., Aranda M.A., Querol-Audi J.;
RT "Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal
RT Bipartite Binding Mode for Protein Translation.";
RL Plant Physiol. 174:1476-1491(2017).
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:17026540, PubMed:28522457). Recognizes and binds the 7-
CC methylguanosine-containing mRNA cap during an early step in the
CC initiation of protein synthesis and facilitates ribosome binding by
CC inducing the unwinding of the mRNAs secondary structures
CC (PubMed:17026540, PubMed:28522457). Key component of recessive
CC resistance to potyviruses and Tombusviridae genus Carmovirus such as
CC melon necrotic spot virus (MNSV) (PubMed:17026540).
CC {ECO:0000269|PubMed:17026540, ECO:0000269|PubMed:28522457}.
CC -!- FUNCTION: (Microbial infection) Susceptibility host factor required for
CC viral infection by recruiting viral RNAs, including uncapped and non-
CC polyadenylated RNA, to the host ribosomal complex via an interaction
CC with viral genome-linked protein (VPg). {ECO:0000269|PubMed:17026540}.
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 (By similarity). Interacts directly with
CC eIF4G (PubMed:28522457). In higher plants two isoforms of EIF4F have
CC been identified, named isoform EIF4F and isoform EIF(iso)4F. Isoform
CC EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28 (By similarity). {ECO:0000250|UniProtKB:P29557,
CC ECO:0000269|PubMed:28522457}.
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:17026540}.
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 -!- POLYMORPHISM: Variant present in the strain cv. PI 161375, allele nsv,
CC confers an increased resistance to Tombusviridae genus Carmovirus such
CC as melon necrotic spot virus (MNSV) strain Malpha5 but not to the
CC strain 264, associated with a normal mRNA cap-binding activity, but an
CC impaired ability to support cap-independent translation of mRNAs.
CC {ECO:0000269|PubMed:17026540}.
CC -!- MISCELLANEOUS: Displayed sequence is cv. WMR-29 and cv. Vedrantais.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; DQ393830; ABD57969.1; -; mRNA.
DR EMBL; DQ393831; ABD57970.1; -; mRNA.
DR EMBL; DQ393832; ABD57971.1; -; mRNA.
DR EMBL; EF188258; ABQ53636.1; -; Genomic_DNA.
DR EMBL; SSTE01007279; KAA0057081.1; -; Genomic_DNA.
DR RefSeq; NP_001284409.1; NM_001297480.1.
DR PDB; 5ME5; X-ray; 1.90 A; A=2-235.
DR PDB; 5ME6; X-ray; 2.90 A; A/B/C/D=53-235.
DR PDB; 5ME7; X-ray; 2.20 A; A/B/C/D=53-235.
DR PDBsum; 5ME5; -.
DR PDBsum; 5ME6; -.
DR PDBsum; 5ME7; -.
DR SMR; Q00LS8; -.
DR STRING; 1194695.A0A5A7UUA1; -.
DR EnsemblPlants; MELO3C002698.2.1; maker-chr12-exonerate_est2genome-gene-206.0-mRNA-1:cds; MELO3C002698.2.
DR GeneID; 103487284; -.
DR Gramene; MELO3C002698.2.1; maker-chr12-exonerate_est2genome-gene-206.0-mRNA-1:cds; MELO3C002698.2.
DR KEGG; cmo:103487284; -.
DR eggNOG; KOG1670; Eukaryota.
DR OrthoDB; 1394271at2759; -.
DR Proteomes; UP000089565; Unplaced.
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 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 3D-structure; Cytoplasm; Disulfide bond; Host-virus interaction;
KW Initiation factor; Nucleus; Plant defense; Protein biosynthesis;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..235
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000454068"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..63
FT /note="EIF4G-binding"
FT /evidence="ECO:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME5"
FT REGION 70..106
FT /note="EIF4G-binding"
FT /evidence="ECO:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME5"
FT REGION 154..163
FT /note="EIF4G-binding"
FT /evidence="ECO:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME5"
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:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME6"
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:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME6"
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:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME6"
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:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME6"
FT DISULFID 133..171
FT /evidence="ECO:0000269|PubMed:28522457,
FT ECO:0007744|PDB:5ME5"
FT VARIANT 228
FT /note="H -> L (in strain: PI 161375, allele nsv)"
FT /evidence="ECO:0000269|PubMed:17026540"
FT MUTAGEN 70
FT /note="F->A: Reduced eIF4G binding and impaired ability to
FT support cap-independent translation of mRNAs. Strongly
FT reduced eIF4G binding and impaired ability to support cap-
FT independent translation of mRNAs; when associated with A-
FT 89. Strongly reduced eIF4G binding and impaired ability to
FT support cap-independent translation of mRNAs; when
FT associated with A-99 and H-154. Strongly reduced eIF4G
FT binding and impaired ability to support cap-independent
FT translation of mRNAs; when associated with A-89 and H-154."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 89
FT /note="I->A: Strongly reduced eIF4G binding and impaired
FT ability to support cap-independent translation of mRNAs;
FT when associated with A-70. Strongly reduced eIF4G binding
FT and impaired ability to support cap-independent translation
FT of mRNAs; when associated with A-70 and H-154."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 99
FT /note="W->A: Reduced eIF4G binding and impaired ability to
FT support cap-independent translation of mRNAs. Strongly
FT reduced eIF4G binding and impaired ability to support cap-
FT independent translation of mRNAs; when associated with H-
FT 154. Strongly reduced eIF4G binding and impaired ability to
FT support cap-independent translation of mRNAs; when
FT associated with A-70 and H-154."
FT /evidence="ECO:0000269|PubMed:28522457"
FT MUTAGEN 154
FT /note="Y->H: Strongly reduced eIF4G binding and impaired
FT ability to support cap-independent translation of mRNAs;
FT when associated with A-99. Strongly reduced eIF4G binding
FT and impaired ability to support cap-independent translation
FT of mRNAs; when associated with A-70 and A-89. Strongly
FT reduced eIF4G binding and impaired ability to support cap-
FT independent translation of mRNAs; when associated with A-70
FT and A-99."
FT /evidence="ECO:0000269|PubMed:28522457"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:5ME6"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:5ME5"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5ME5"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:5ME7"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5ME6"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5ME7"
SQ SEQUENCE 235 AA; 26571 MW; A98E3C6591D0F00F CRC64;
MVVEDSMKAT SAEDLSNSIA NQNPRGRGGD EDEELEEGEI VGDDDLDSSN LSASLVHQPH
PLEHSWTFWF DNPSAKSKQA TWGASIRPIY TFSTVEEFWS VYNNIHHPSK LAMRADLYCF
KHKIEPKWED PVCANGGKWT VNFPRGKSDN GWLYTLLAMI GEQFDCGDEI CGAVVNVRSG
QDKISIWTKN ASNEAAQASI GKQWKEFLDY NESIGFIFHD DAKKFDRHAK NKYMV
