IF4E_RABIT
ID IF4E_RABIT Reviewed; 217 AA.
AC P29338;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Eukaryotic translation initiation factor 4E;
DE Short=eIF-4E;
DE Short=eIF4E;
DE AltName: Full=eIF-4F 25 kDa subunit;
DE AltName: Full=mRNA cap-binding protein;
GN Name=EIF4E;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1475206; DOI=10.1093/nar/20.23.6415;
RA Rychlik W., Rhoads R.E.;
RT "Nucleotide sequence of rabbit eIF-4E cDNA.";
RL Nucleic Acids Res. 20:6415-6415(1992).
RN [2]
RP INTERACTION WITH EIF4A.
RX PubMed=6853548; DOI=10.1016/s0021-9258(20)81965-6;
RA Grifo J.A., Tahara S.M., Morgan M.A., Shatkin A.J., Merrick W.C.;
RT "New initiation factor activity required for globin mRNA translation.";
RL J. Biol. Chem. 258:5804-5810(1983).
CC -!- FUNCTION: 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. In addition to its role in translation
CC initiation, also acts as a regulator of translation and stability in
CC the cytoplasm (By similarity). Component of the CYFIP1-EIF4E-FMR1
CC complex which binds to the mRNA cap and mediates translational
CC repression: in the complex, EIF4E mediates the binding to the mRNA cap.
CC Component of a multiprotein complex that sequesters and represses
CC translation of proneurogenic factors during neurogenesis (By
CC similarity). In P-bodies, component of a complex that mediates the
CC storage of translationally inactive mRNAs in the cytoplasm and prevents
CC their degradation (By similarity). May play an important role in
CC spermatogenesis through translational regulation of stage-specific
CC mRNAs during germ cell development (By similarity).
CC {ECO:0000250|UniProtKB:P06730, ECO:0000250|UniProtKB:P63073,
CC ECO:0000250|UniProtKB:P63074}.
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 EIF4G1/EIF4G3
CC (PubMed:6853548). EIF4E is also known to interact with other partners.
CC Interacts with EIF4ENIF1/4E-T; promotes recruitment to P-bodies and
CC import into the nucleus. Hypophosphorylated EIF4EBP1, EIF4EBP2 and
CC EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin
CC stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1
CC causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and
CC consequent initiation of translation. Interacts mutually exclusive with
CC EIF4A1 or EIF4A2 (By similarity). Interacts with NGDN and PIWIL2.
CC Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and
CC FMR1. Interacts directly with CYFIP1. Interacts with CLOCK (By
CC similarity). Binds to MKNK2 in nucleus. Interacts with LIMD1, WTIP and
CC AJUBA. Interacts with APOBEC3G in an RNA-dependent manner. Interacts
CC with LARP1. Interacts with METTL3. Interacts with RBM24; this
CC interaction prevents EIF4E from binding to p53/TP53 mRNA and inhibits
CC the assembly of translation initiation complex. Interacts with DDX3X;
CC interaction is direct and in an RNA-independent manner; this
CC interaction enhances EIF4E cap-binding ability and is required for the
CC repression of cap-dependent translation and the increase of IRES-
CC mediated translation. DDX3X competes with EIF4G1 for interaction with
CC EIF4E (By similarity). Interacts with BTG4 and CNOT7 (By similarity).
CC {ECO:0000250|UniProtKB:P06730, ECO:0000250|UniProtKB:P63073,
CC ECO:0000269|PubMed:6853548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:P06730}.
CC Cytoplasm {ECO:0000250|UniProtKB:P06730}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P06730}. Nucleus {ECO:0000250|UniProtKB:P06730}.
CC Note=Interaction with EIF4ENIF1/4E-T is required for localization to
CC processing bodies (P-bodies). Imported in the nucleus via interaction
CC with EIF4ENIF1/4E-T via a piggy-back mechanism.
CC {ECO:0000250|UniProtKB:P06730}.
CC -!- PTM: Phosphorylation increases the ability of the protein to bind to
CC mRNA caps and to form the eIF4F complex.
CC {ECO:0000250|UniProtKB:P06730}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; X61939; CAA43943.1; -; mRNA.
DR PIR; S30248; B26411.
DR RefSeq; NP_001095180.1; NM_001101710.1.
DR AlphaFoldDB; P29338; -.
DR BMRB; P29338; -.
DR SMR; P29338; -.
DR STRING; 9986.ENSOCUP00000024878; -.
DR BindingDB; P29338; -.
DR ChEMBL; CHEMBL5636; -.
DR iPTMnet; P29338; -.
DR GeneID; 100009338; -.
DR KEGG; ocu:100009338; -.
DR CTD; 1977; -.
DR eggNOG; KOG1670; Eukaryota.
DR InParanoid; P29338; -.
DR OrthoDB; 1394271at2759; -.
DR TreeFam; TF101526; -.
DR PRO; PR:P29338; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:AgBase.
DR GO; GO:0019899; F:enzyme binding; ISS:AgBase.
DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; ISS:AgBase.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; 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 Acetylation; Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT CHAIN 2..217
FT /note="Eukaryotic translation initiation factor 4E"
FT /id="PRO_0000193636"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..40
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT REGION 73..77
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT REGION 132..139
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 56..57
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:P06730"
FT BINDING 102..103
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:P06730"
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:P06730"
FT BINDING 205..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:P06730"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT MOD_RES 209
FT /note="Phosphoserine; by PKC and MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P06730"
SQ SEQUENCE 217 AA; 25049 MW; B5A6BE12F4147159 CRC64;
MATVEPETTP TPNPPPAEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL
RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ
QRRSDLDRFW LETLLCLIGE SFDDYSDDVC GAVVNVRAKG DKIAIWTTEC ENRDAVTHIG
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV
