IF4E1_WHEAT
ID IF4E1_WHEAT Reviewed; 215 AA.
AC P29557; A0A1W6I4N8; W5D237;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Eukaryotic translation initiation factor 4E-1 {ECO:0000303|PubMed:1508698};
DE Short=eIF-4E-1 {ECO:0000303|PubMed:1508698};
DE Short=eIF4E-1 {ECO:0000303|PubMed:1508698};
DE AltName: Full=eIF-4F 25 kDa subunit {ECO:0000303|PubMed:1508698};
DE AltName: Full=eIF-4F p26 subunit {ECO:0000303|PubMed:1508698};
DE AltName: Full=mRNA cap-binding protein {ECO:0000303|PubMed:1508698};
GN Name=eIF4E {ECO:0000303|PubMed:1508698};
GN ORFNames=TRAES_3BF151900060CFD_c1 {ECO:0000312|EMBL:CDJ26525.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Metz A.M.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. LM4, and cv. LY502;
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-215, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=1508698; DOI=10.1093/nar/20.15.4096;
RA Metz A.M., Timmer R.T., Browning K.S.;
RT "Isolation and sequence of a cDNA encoding the cap binding protein of wheat
RT eukaryotic protein synthesis initiation factor 4F.";
RL Nucleic Acids Res. 20:4096-4096(1992).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-215 IN COMPLEX WITH
RP 7-METHYLGUANOSINE, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=17322339; DOI=10.1104/pp.106.093146;
RA Monzingo A.F., Dhaliwal S., Dutt-Chaudhuri A., Lyon A., Sadow J.H.,
RA Hoffman D.W., Robertus J.D., Browning K.S.;
RT "The structure of eukaryotic translation initiation factor-4E from wheat
RT reveals a novel disulfide bond.";
RL Plant Physiol. 143:1504-1518(2007).
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:1508698). Recognizes and binds the 7-methylguanosine-containing
CC mRNA cap during an early step in the initiation of protein synthesis
CC and facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (PubMed:17322339, PubMed:1508698).
CC {ECO:0000269|PubMed:1508698, ECO:0000269|PubMed:17322339}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions (Probable).
CC It is composed of at least EIF4A, EIF4E and EIF4G (Probable). EIF4E is
CC also known to interact with other partners (Probable). In higher plants
CC two isoforms of EIF4F have been identified, named isoform EIF4F and
CC isoform EIF(iso)4F (Probable). Isoform EIF4F has subunits p220 and p26,
CC whereas isoform EIF(iso)4F has subunits p82 and p28 (Probable).
CC {ECO:0000305|PubMed:1508698}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm
CC {ECO:0000250|UniProtKB:K0P2S0}.
CC -!- PTM: According to the redox status, the Cys-113-Cys-151 disulfide
CC bridge may have a role in regulating protein function by affecting its
CC ability to bind capped mRNA. {ECO:0000269|PubMed:17322339}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z12616; CAA78262.2; -; mRNA.
DR EMBL; KX467330; ARM39030.1; -; mRNA.
DR EMBL; KX467331; ARM39031.1; -; mRNA.
DR EMBL; CBUC010000421; CDJ26525.1; -; Genomic_DNA.
DR PIR; S26493; S26493.
DR PDB; 2IDR; X-ray; 1.85 A; A/B=39-215.
DR PDB; 2IDV; X-ray; 2.30 A; A=39-215.
DR PDBsum; 2IDR; -.
DR PDBsum; 2IDV; -.
DR AlphaFoldDB; P29557; -.
DR SMR; P29557; -.
DR ELM; P29557; -.
DR IntAct; P29557; 1.
DR STRING; 4565.Traes_3B_B2BA7CF8B.1; -.
DR PRIDE; P29557; -.
DR EnsemblPlants; TraesCAD_scaffold_032410_01G000100.1; TraesCAD_scaffold_032410_01G000100.1; TraesCAD_scaffold_032410_01G000100.
DR EnsemblPlants; TraesCAD_scaffold_073395_01G000200.1; TraesCAD_scaffold_073395_01G000200.1; TraesCAD_scaffold_073395_01G000200.
DR EnsemblPlants; TraesCAD_scaffold_132297_01G000100.1; TraesCAD_scaffold_132297_01G000100.1; TraesCAD_scaffold_132297_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_027676_01G000200.1; TraesCLE_scaffold_027676_01G000200.1; TraesCLE_scaffold_027676_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_070372_01G000200.1; TraesCLE_scaffold_070372_01G000200.1; TraesCLE_scaffold_070372_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_112464_01G000200.1; TraesCLE_scaffold_112464_01G000200.1; TraesCLE_scaffold_112464_01G000200.
DR EnsemblPlants; TraesCS3A02G521500.1; TraesCS3A02G521500.1; TraesCS3A02G521500.
DR EnsemblPlants; TraesCS3D02G527800.1; TraesCS3D02G527800.1; TraesCS3D02G527800.
DR EnsemblPlants; TraesPAR_scaffold_029601_01G000200.1; TraesPAR_scaffold_029601_01G000200.1; TraesPAR_scaffold_029601_01G000200.
DR EnsemblPlants; TraesPAR_scaffold_072845_01G000200.1; TraesPAR_scaffold_072845_01G000200.1; TraesPAR_scaffold_072845_01G000200.
DR EnsemblPlants; TraesPAR_scaffold_136828_01G000100.1; TraesPAR_scaffold_136828_01G000100.1; TraesPAR_scaffold_136828_01G000100.
DR EnsemblPlants; TraesROB_scaffold_077200_01G000300.1; TraesROB_scaffold_077200_01G000300.1; TraesROB_scaffold_077200_01G000300.
DR EnsemblPlants; TraesROB_scaffold_093481_01G000200.1; TraesROB_scaffold_093481_01G000200.1; TraesROB_scaffold_093481_01G000200.
DR EnsemblPlants; TraesROB_scaffold_115713_01G000200.1; TraesROB_scaffold_115713_01G000200.1; TraesROB_scaffold_115713_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_097257_01G000200.1; TraesWEE_scaffold_097257_01G000200.1; TraesWEE_scaffold_097257_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_104681_01G000100.1; TraesWEE_scaffold_104681_01G000100.1; TraesWEE_scaffold_104681_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_148986_01G000200.1; TraesWEE_scaffold_148986_01G000200.1; TraesWEE_scaffold_148986_01G000200.
DR Gramene; TraesCAD_scaffold_032410_01G000100.1; TraesCAD_scaffold_032410_01G000100.1; TraesCAD_scaffold_032410_01G000100.
DR Gramene; TraesCAD_scaffold_073395_01G000200.1; TraesCAD_scaffold_073395_01G000200.1; TraesCAD_scaffold_073395_01G000200.
DR Gramene; TraesCAD_scaffold_132297_01G000100.1; TraesCAD_scaffold_132297_01G000100.1; TraesCAD_scaffold_132297_01G000100.
DR Gramene; TraesCLE_scaffold_027676_01G000200.1; TraesCLE_scaffold_027676_01G000200.1; TraesCLE_scaffold_027676_01G000200.
DR Gramene; TraesCLE_scaffold_070372_01G000200.1; TraesCLE_scaffold_070372_01G000200.1; TraesCLE_scaffold_070372_01G000200.
DR Gramene; TraesCLE_scaffold_112464_01G000200.1; TraesCLE_scaffold_112464_01G000200.1; TraesCLE_scaffold_112464_01G000200.
DR Gramene; TraesCS3A02G521500.1; TraesCS3A02G521500.1; TraesCS3A02G521500.
DR Gramene; TraesCS3D02G527800.1; TraesCS3D02G527800.1; TraesCS3D02G527800.
DR Gramene; TraesPAR_scaffold_029601_01G000200.1; TraesPAR_scaffold_029601_01G000200.1; TraesPAR_scaffold_029601_01G000200.
DR Gramene; TraesPAR_scaffold_072845_01G000200.1; TraesPAR_scaffold_072845_01G000200.1; TraesPAR_scaffold_072845_01G000200.
DR Gramene; TraesPAR_scaffold_136828_01G000100.1; TraesPAR_scaffold_136828_01G000100.1; TraesPAR_scaffold_136828_01G000100.
DR Gramene; TraesROB_scaffold_077200_01G000300.1; TraesROB_scaffold_077200_01G000300.1; TraesROB_scaffold_077200_01G000300.
DR Gramene; TraesROB_scaffold_093481_01G000200.1; TraesROB_scaffold_093481_01G000200.1; TraesROB_scaffold_093481_01G000200.
DR Gramene; TraesROB_scaffold_115713_01G000200.1; TraesROB_scaffold_115713_01G000200.1; TraesROB_scaffold_115713_01G000200.
DR Gramene; TraesWEE_scaffold_097257_01G000200.1; TraesWEE_scaffold_097257_01G000200.1; TraesWEE_scaffold_097257_01G000200.
DR Gramene; TraesWEE_scaffold_104681_01G000100.1; TraesWEE_scaffold_104681_01G000100.1; TraesWEE_scaffold_104681_01G000100.
DR Gramene; TraesWEE_scaffold_148986_01G000200.1; TraesWEE_scaffold_148986_01G000200.1; TraesWEE_scaffold_148986_01G000200.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR OMA; WHDLLLC; -.
DR EvolutionaryTrace; P29557; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P29557; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
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 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Initiation factor; Nucleus; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..215
FT /note="Eukaryotic translation initiation factor 4E-1"
FT /id="PRO_0000193662"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..43
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 50..86
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 134..143
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..63
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:17322339,
FT ECO:0007744|PDB:2IDV"
FT BINDING 90
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:17322339,
FT ECO:0007744|PDB:2IDV"
FT BINDING 108..109
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:17322339,
FT ECO:0007744|PDB:2IDV"
FT BINDING 158..163
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:17322339,
FT ECO:0007744|PDB:2IDV"
FT BINDING 203..207
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 113..151
FT /evidence="ECO:0000269|PubMed:17322339,
FT ECO:0007744|PDB:2IDR"
FT CONFLICT 38
FT /note="T -> S (in Ref. 3; CDJ26525)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> R (in Ref. 3; CDJ26525)"
FT /evidence="ECO:0000305"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:2IDR"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2IDR"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2IDR"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2IDR"
SQ SEQUENCE 215 AA; 23991 MW; 80D148F5EAFF27EF CRC64;
MAEDTETRPA SAGAEEREEG EIADDGDGSS AAAAGRITAH PLENAWTFWF DNPQGKSRQV
AWGSTIHPIH TFSTVEDFWG LYNNIHNPSK LNVGADFHCF KNKIEPKWED PICANGGKWT
ISCGRGKSDT FWLHTLLAMI GEQFDFGDEI CGAVVSVRQK QERVAIWTKN AANEAAQISI
GKQWKEFLDY KDSIGFIVHE DAKRSDKGPK NRYTV
