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Protein

Eukaryotic translation initiation factor 4E

Gene

Eif4e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit mediates the binding to the mRNA cap (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. May play an important role in spermatogenesis through translational regulation of stage-specific mRNAs during germ cell development.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-1169408. ISG15 antiviral mechanism.
R-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-166208. mTORC1-mediated signalling.
R-RNO-429947. Deadenylation of mRNA.
R-RNO-72649. Translation initiation complex formation.
R-RNO-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 4E
Short name:
eIF-4E
Short name:
eIF4E
Alternative name(s):
eIF-4F 25 kDa subunit
mRNA cap-binding protein
Gene namesi
Name:Eif4e
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi69647. Eif4e.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 217216Eukaryotic translation initiation factor 4EPRO_0000193637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei22 – 221PhosphothreonineBy similarity
Modified residuei209 – 2091Phosphoserine; by PKC and MKNK2By similarity

Post-translational modificationi

Phosphorylation increases the ability of the protein to bind to mRNA caps and to form the eIF4F complex.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63074.
PRIDEiP63074.

PTM databases

iPTMnetiP63074.
PhosphoSiteiP63074.

Expressioni

Tissue specificityi

Very high levels in post-meiotic testicular germ cells of rats of reproductive age.1 Publication

Gene expression databases

GenevisibleiP63074. RN.

Interactioni

Subunit structurei

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4E is also known to interact with other partners. The interaction with EIF4ENIF1 mediates the import into the nucleus. Hypophosphorylated EIF4EBP1, EIF4EBP2 and EIF4EBP3 compete with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. Rapamycin can attenuate insulin stimulation, mediated by FKBPs. Interacts mutually exclusive with EIF4A1 or EIF4A2. Component of the CYFIP1-EIF4E-FMR1 complex composed of CYFIP, EIF4E and FMR1. Interacts directly with CYFIP1. Interacts with NGDN and PIWIL2. Binds to MKNK2 in nucleus (By similarity). Interacts with LIMD1, WTIP and AJUBA (By similarity). Interacts with APOBEC3G in an RNA-dependent manner. Interacts with CLOCK and LARP1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi250643. 2 interactions.
IntActiP63074. 1 interaction.
STRINGi10116.ENSRNOP00000063699.

Structurei

3D structure databases

ProteinModelPortaliP63074.
SMRiP63074. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 404EIF4EBP1/2/3 bindingBy similarity
Regioni56 – 5727-methylguanosine-containing mRNA cap bindingBy similarity
Regioni73 – 775EIF4EBP1/2/3 bindingBy similarity
Regioni102 – 10327-methylguanosine-containing mRNA cap bindingBy similarity
Regioni132 – 1398EIF4EBP1/2/3 bindingBy similarity
Regioni157 – 16267-methylguanosine-containing mRNA cap bindingBy similarity
Regioni205 – 20737-methylguanosine-containing mRNA cap bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1670. Eukaryota.
COG5053. LUCA.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000186751.
HOVERGENiHBG006130.
InParanoidiP63074.
KOiK03259.
OMAiWTLWYYE.
OrthoDBiEOG7QRQVM.
PhylomeDBiP63074.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.
PROSITEiPS00813. IF4E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVEPETTP TTNPPPAEEE KTESNQEVAN PEHYIKHPLQ NRWALWFFKN
60 70 80 90 100
DKSKTWQANL RLISKFDTVE DFWALYNHIQ LSSNLMPGCD YSLFKDGIEP
110 120 130 140 150
MWEDEKNKRG GRWLITLNKQ QRRSDLDRFW LETLLCLIGE SFDDYSDDVC
160 170 180 190 200
GAVVNVRAKG DKIAIWTTEC ENRDAVTHIG RVYKERLGLP PKIVIGYQSH
210
ADTATKSGST TKNRFVV
Length:217
Mass (Da):25,053
Last modified:September 13, 2004 - v1
Checksum:iFC61D0FB337BCD8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83399 mRNA. Translation: CAA58316.1.
BC087001 mRNA. Translation: AAH87001.1.
RefSeqiNP_446426.1. NM_053974.2.
XP_008759710.1. XM_008761488.1.
UniGeneiRn.11275.

Genome annotation databases

EnsembliENSRNOT00000090526; ENSRNOP00000073799; ENSRNOG00000052343.
GeneIDi117045.
KEGGirno:117045.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83399 mRNA. Translation: CAA58316.1.
BC087001 mRNA. Translation: AAH87001.1.
RefSeqiNP_446426.1. NM_053974.2.
XP_008759710.1. XM_008761488.1.
UniGeneiRn.11275.

3D structure databases

ProteinModelPortaliP63074.
SMRiP63074. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250643. 2 interactions.
IntActiP63074. 1 interaction.
STRINGi10116.ENSRNOP00000063699.

PTM databases

iPTMnetiP63074.
PhosphoSiteiP63074.

Proteomic databases

PaxDbiP63074.
PRIDEiP63074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000090526; ENSRNOP00000073799; ENSRNOG00000052343.
GeneIDi117045.
KEGGirno:117045.

Organism-specific databases

CTDi1977.
RGDi69647. Eif4e.

Phylogenomic databases

eggNOGiKOG1670. Eukaryota.
COG5053. LUCA.
GeneTreeiENSGT00520000055549.
HOGENOMiHOG000186751.
HOVERGENiHBG006130.
InParanoidiP63074.
KOiK03259.
OMAiWTLWYYE.
OrthoDBiEOG7QRQVM.
PhylomeDBiP63074.

Enzyme and pathway databases

ReactomeiR-RNO-1169408. ISG15 antiviral mechanism.
R-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-166208. mTORC1-mediated signalling.
R-RNO-429947. Deadenylation of mRNA.
R-RNO-72649. Translation initiation complex formation.
R-RNO-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

PROiP63074.

Gene expression databases

GenevisibleiP63074. RN.

Family and domain databases

Gene3Di3.30.760.10. 1 hit.
InterProiIPR023398. TIF_eIF4e-like.
IPR001040. TIF_eIF_4E.
IPR019770. TIF_eIF_4E_CS.
[Graphical view]
PANTHERiPTHR11960. PTHR11960. 1 hit.
PfamiPF01652. IF4E. 1 hit.
[Graphical view]
SUPFAMiSSF55418. SSF55418. 1 hit.
PROSITEiPS00813. IF4E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Abundant expression of translation initiation factor EIF-4E in post-meiotic germ cells of the rat testis."
    Miyagi Y., Kerr S., Sugiyama A., Asai A., Shibuya M., Fujimoto H., Kuchino Y.
    Lab. Invest. 73:890-898(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. "PHAS-I as a link between mitogen-activated protein kinase and translation initiation."
    Lin T.-A., Kong X., Haystead T.A.J., Pause A., Belsham G.J., Sonenberg N., Lawrence J.C. Jr.
    Science 266:653-656(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4EBP1.

Entry informationi

Entry nameiIF4E_RAT
AccessioniPrimary (citable) accession number: P63074
Secondary accession number(s): P20415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 6, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.