IF4E2_WHEAT
ID IF4E2_WHEAT Reviewed; 209 AA.
AC Q03389;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Eukaryotic translation initiation factor isoform 4E-2;
DE Short=eIF(iso)-4E-2;
DE Short=eIF(iso)4E-2;
DE AltName: Full=eIF-(iso)4F 25 kDa subunit;
DE AltName: Full=eIF-(iso)4F p28 subunit;
DE AltName: Full=mRNA cap-binding protein;
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].
RX PubMed=1385417; DOI=10.1016/s0021-9258(18)50081-8;
RA Allen M.L., Metz A.M., Timmer R.T., Rhoads R.E., Browning K.S.;
RT "Isolation and sequence of the cDNAs encoding the subunits of the isozyme
RT form of wheat protein synthesis initiation factor 4F.";
RL J. Biol. Chem. 267:23232-23236(1992).
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). {ECO:0000250|UniProtKB:Q66WU1}.
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:O04663}.
CC -!- INTERACTION:
CC Q03389; O04663: EIF(ISO)4E; Xeno; NbExp=3; IntAct=EBI-1770460, EBI-1770425;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}.
CC Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.
CC -!- PTM: According to the redox status, the Cys-106-Cys-145 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 -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; M95818; AAA34295.1; -; mRNA.
DR EMBL; M95819; AAA34296.1; -; mRNA.
DR AlphaFoldDB; Q03389; -.
DR SMR; Q03389; -.
DR IntAct; Q03389; 2.
DR STRING; 4565.Traes_1BL_7103BF3C6.1; -.
DR PRIDE; Q03389; -.
DR EnsemblPlants; TraesCAD_scaffold_020754_01G000300.1; TraesCAD_scaffold_020754_01G000300.1; TraesCAD_scaffold_020754_01G000300.
DR EnsemblPlants; TraesCLE_scaffold_070407_01G000200.1; TraesCLE_scaffold_070407_01G000200.1; TraesCLE_scaffold_070407_01G000200.
DR EnsemblPlants; TraesCS1D02G146500.1; TraesCS1D02G146500.1; TraesCS1D02G146500.
DR EnsemblPlants; TraesPAR_scaffold_066195_01G000200.1; TraesPAR_scaffold_066195_01G000200.1; TraesPAR_scaffold_066195_01G000200.
DR EnsemblPlants; TraesROB_scaffold_066899_01G000300.1; TraesROB_scaffold_066899_01G000300.1; TraesROB_scaffold_066899_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_070878_01G000200.1; TraesWEE_scaffold_070878_01G000200.1; TraesWEE_scaffold_070878_01G000200.
DR Gramene; TraesCAD_scaffold_020754_01G000300.1; TraesCAD_scaffold_020754_01G000300.1; TraesCAD_scaffold_020754_01G000300.
DR Gramene; TraesCLE_scaffold_070407_01G000200.1; TraesCLE_scaffold_070407_01G000200.1; TraesCLE_scaffold_070407_01G000200.
DR Gramene; TraesCS1D02G146500.1; TraesCS1D02G146500.1; TraesCS1D02G146500.
DR Gramene; TraesPAR_scaffold_066195_01G000200.1; TraesPAR_scaffold_066195_01G000200.1; TraesPAR_scaffold_066195_01G000200.
DR Gramene; TraesROB_scaffold_066899_01G000300.1; TraesROB_scaffold_066899_01G000300.1; TraesROB_scaffold_066899_01G000300.
DR Gramene; TraesWEE_scaffold_070878_01G000200.1; TraesWEE_scaffold_070878_01G000200.1; TraesWEE_scaffold_070878_01G000200.
DR eggNOG; KOG1670; Eukaryota.
DR OMA; LGYGCDY; -.
DR Proteomes; UP000019116; Unplaced.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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; Initiation factor; Nucleus;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..209
FT /note="Eukaryotic translation initiation factor isoform 4E-
FT 2"
FT /id="PRO_0000193663"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51..56
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 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 101..102
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 152..157
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 197..200
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 106..145
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT VARIANT 22
FT /note="G -> S"
SQ SEQUENCE 209 AA; 23522 MW; E6EC9E8557AB2BED CRC64;
MAEVEAALPV AATETPEVAA EGDAGAAEAK GPHKLQRQWT FWYDIQTKPK PGAAWGTSLK
KGYTFDTVEE FWCLYDQIFR PSKLVGSADF HLFKAGVEPK WEDPECANGG KWTVISSRKT
NLDTMWLETC MALIGEQFDE SQEICGVVAS VRQRQDKLSL WTKTASNEAV QVDIGKKWKE
VIDYNDKMVY SFHDDSRSQK PSRGGRYTV
