IF4E_DICDI
ID IF4E_DICDI Reviewed; 250 AA.
AC Q55FE0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Eukaryotic translation initiation factor 4E;
DE Short=eIF-4E;
DE Short=eIF4E;
GN Name=eif4e; ORFNames=DDB_G0268574;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {ECO:0000250|UniProtKB:P06730}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P06730}.
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; AAFI02000003; EAL73740.1; -; Genomic_DNA.
DR RefSeq; XP_647593.1; XM_642501.1.
DR AlphaFoldDB; Q55FE0; -.
DR SMR; Q55FE0; -.
DR STRING; 44689.DDB0234247; -.
DR PaxDb; Q55FE0; -.
DR EnsemblProtists; EAL73740; EAL73740; DDB_G0268574.
DR GeneID; 8616405; -.
DR KEGG; ddi:DDB_G0268574; -.
DR dictyBase; DDB_G0268574; eIF4e.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_2_1; -.
DR InParanoid; Q55FE0; -.
DR OMA; EEFWAIV; -.
DR PhylomeDB; Q55FE0; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-166208; mTORC1-mediated signalling.
DR Reactome; R-DDI-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q55FE0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
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:0006972; P:hyperosmotic response; IEP:dictyBase.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
PE 3: Inferred from homology;
KW Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..250
FT /note="Eukaryotic translation initiation factor 4E"
FT /id="PRO_0000328013"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 96..97
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 142..143
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 193..198
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 239..241
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"
SQ SEQUENCE 250 AA; 29023 MW; A751A25577B0C39A CRC64;
MTTNKDVECL VEPTSNISIT EENKNVTSET TTTTNNTQNK ETETTDNINK EETADKENKE
EQQQEENPEN LIKHPLQNRW SLWYDYQSGK INPEHWVDSL KKVISFDSVE DFWCVFNNLP
NVSNLKQGSS YHLFKDDIEP KWEHESNKRG GKWFVMVKDK SRCDNQWLQS VMACVGETFD
SSDEICGIVY NSRKNGDKIS VWTKTAQDEK ATRDVGNCLK KILEIDQTIQ YTPHEDFIRS
SKGSKNLYEC
