IF4E_BOVIN
ID IF4E_BOVIN Reviewed; 217 AA.
AC Q9N0T5; Q2NL02;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Eukaryotic translation initiation factor 4E;
DE Short=eIF-4E;
DE Short=eIF4E;
DE AltName: Full=mRNA cap-binding protein;
GN Name=EIF4E;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11913777; DOI=10.3109/10425170109084455;
RA Long E., Capuco A.V., Zhao X.;
RT "Cloning of bovine eukaryotic translation initiation factor 4E (eIF-4E) and
RT its expression in the bovine mammary gland at different physiological
RT stages.";
RL DNA Seq. 12:319-329(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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. It is
CC composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also
CC known to interact with other partners. Interacts with EIF4ENIF1/4E-T;
CC promotes recruitment to P-bodies and import into the nucleus.
CC Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with
CC EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase
CC (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of
CC the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of
CC translation. Interacts mutually exclusive with EIF4A1 or EIF4A2 (By
CC similarity). Interacts with NGDN and PIWIL2. Component of the CYFIP1-
CC EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts
CC directly with CYFIP1. Interacts with CLOCK (By similarity). Binds to
CC MKNK2 in nucleus. Interacts with LIMD1, WTIP and AJUBA. Interacts with
CC APOBEC3G in an RNA-dependent manner. Interacts with LARP1. Interacts
CC with METTL3. Interacts with RBM24; this interaction prevents EIF4E from
CC binding to p53/TP53 mRNA and inhibits the assembly of translation
CC initiation complex. Interacts with DDX3X; interaction is direct and in
CC an RNA-independent manner; this interaction enhances EIF4E cap-binding
CC ability and is required for the repression of cap-dependent translation
CC and the increase of IRES-mediated translation. DDX3X competes with
CC EIF4G1 for interaction with EIF4E (By similarity). Interacts with BTG4
CC and CNOT7 (By similarity). {ECO:0000250|UniProtKB:P06730,
CC ECO:0000250|UniProtKB:P63073}.
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; AF257235; AAF66991.1; -; mRNA.
DR EMBL; BC111272; AAI11273.1; -; mRNA.
DR RefSeq; NP_776735.2; NM_174310.3.
DR AlphaFoldDB; Q9N0T5; -.
DR BMRB; Q9N0T5; -.
DR SMR; Q9N0T5; -.
DR STRING; 9913.ENSBTAP00000012530; -.
DR iPTMnet; Q9N0T5; -.
DR PaxDb; Q9N0T5; -.
DR PRIDE; Q9N0T5; -.
DR GeneID; 281751; -.
DR KEGG; bta:281751; -.
DR CTD; 1977; -.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_1_1_1; -.
DR InParanoid; Q9N0T5; -.
DR OrthoDB; 1394271at2759; -.
DR TreeFam; TF101526; -.
DR Proteomes; UP000009136; 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 2: Evidence at transcript 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_0000193633"
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"
FT CONFLICT 124
FT /note="S -> G (in Ref. 1; AAF66991)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="V -> L (in Ref. 1; AAF66991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 25079 MW; 44BC0418D54BA583 CRC64;
MATVEPETTP TPNPPPTEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN DKSKTWQANL
RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP MWEDEKNKRG GRWLITLNKQ
QRRSDLDRFW LETVLCLIGE SFDDYSDDVC GAVVNVRAKG DKIAIWTTEC ENREAVTHIG
RVYKERLGLP PKIVIGYQSH ADTATKSGST TKNRFVV
