IF4E5_CAEEL
ID IF4E5_CAEEL Reviewed; 201 AA.
AC P56570; Q9NIF2;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Eukaryotic translation initiation factor 4E-5;
DE Short=eIF-4E-5;
DE Short=eIF4E-5;
DE AltName: Full=eIF-4F 25 kDa subunit;
DE AltName: Full=mRNA cap-binding protein;
GN Name=ife-5; ORFNames=Y57A10A.30;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Bristol N2;
RX PubMed=10744754; DOI=10.1074/jbc.275.14.10590;
RA Keiper B.D., Lamphear B.J., Deshpande A.M., Jankowska-Anyszka M.,
RA Aamodt E.J., Blumenthal T., Rhoads R.E.;
RT "Functional characterization of five eIF4E isoforms in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 275:10590-10596(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=11641215; DOI=10.1242/dev.128.20.3899;
RA Amiri A., Keiper B.D., Kawasaki I., Fan Y., Kohara Y., Rhoads R.E.,
RA Strome S.;
RT "An isoform of eIF4E is a component of germ granules and is required for
RT spermatogenesis in C. elegans.";
RL Development 128:3899-3912(2001).
RN [4]
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS.
RX PubMed=12422237;
RA Stachelska A., Wieczorek Z., Ruszczynska K., Stolarski R., Pietrzak M.,
RA Lamphear B.J., Rhoads R.E., Darzynkiewicz E., Jankowska-Anyszka M.;
RT "Interaction of three Caenorhabditis elegans isoforms of translation
RT initiation factor eIF4E with mono- and trimethylated mRNA 5' cap
RT analogues.";
RL Acta Biochim. Pol. 49:671-682(2002).
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. All 5 eIF4E proteins bind monomethyl cap
CC structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures
CC which result from trans-splicing. Translation of trimethyl cap
CC structure mRNAs may be regulated by intracellular redox state;
CC disulfide bonds change the width and depth of the cap-binding cavity
CC determining selectivity to mRNA caps. {ECO:0000269|PubMed:10744754,
CC ECO:0000269|PubMed:12422237}.
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.
CC -!- TISSUE SPECIFICITY: Enriched in the germline.
CC {ECO:0000269|PubMed:11641215}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AF214652; AAF62415.1; -; mRNA.
DR EMBL; AL117195; CAB55035.1; -; Genomic_DNA.
DR PIR; T31652; T31652.
DR RefSeq; NP_001022479.1; NM_001027308.6.
DR AlphaFoldDB; P56570; -.
DR SMR; P56570; -.
DR BioGRID; 40172; 1.
DR STRING; 6239.Y57A10A.30.2; -.
DR PaxDb; P56570; -.
DR PeptideAtlas; P56570; -.
DR EnsemblMetazoa; Y57A10A.30.1; Y57A10A.30.1; WBGene00002063.
DR EnsemblMetazoa; Y57A10A.30.2; Y57A10A.30.2; WBGene00002063.
DR UCSC; Y57A10A.30.2; c. elegans.
DR WormBase; Y57A10A.30; CE22608; WBGene00002063; ife-5.
DR eggNOG; KOG1670; Eukaryota.
DR GeneTree; ENSGT00940000173082; -.
DR HOGENOM; CLU_043552_1_0_1; -.
DR InParanoid; P56570; -.
DR OMA; PEHYITH; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; P56570; -.
DR PRO; PR:P56570; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002063; Expressed in adult organism and 4 other tissues.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:WormBase.
DR GO; GO:0000341; F:RNA trimethylguanosine cap binding; IDA:WormBase.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
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 Disulfide bond; Initiation factor; Protein biosynthesis;
KW Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1..201
FT /note="Eukaryotic translation initiation factor 4E-5"
FT /id="PRO_0000193647"
FT DISULFID 122..126
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 21..29
FT /note="NDDRNASWQ->KADRNKEWE: No change in selectivity for
FT monomethyl cap structures. Selectivity slightly decreased;
FT when associated with N-64--73-K."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 64..73
FT /note="NVFRDDIQPK->YLFKEGIKPM: High selectivity for
FT monomethyl cap structures. Selectivity slightly decreased;
FT when associated with N-21--29-Q."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 64
FT /note="N->Y: High selectivity for monomethyl cap
FT structures. Increased selectivity; when associated with L-
FT 65."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 65
FT /note="V->L: High selectivity for monomethyl cap
FT structures. Increased selectivity; when associated with Y-
FT 64."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 68..73
FT /note="DDIQPK->EGIKPM: No change in selectivity for
FT monomethyl cap structures."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 71..73
FT /note="QPK->KPM: Small increase in selectivity for
FT monomethyl cap structures."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 73..81
FT /note="KWEAPENWD->WEDVNNVQM: Low selectivity for monomethyl
FT cap structures. Selectivity slightly increased; when
FT associated with mutagenesis with N-21--29-Q."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 122
FT /note="C->S: Unfolded protein."
FT /evidence="ECO:0000269|PubMed:12422237"
FT MUTAGEN 126
FT /note="C->S: Unfolded protein."
FT /evidence="ECO:0000269|PubMed:12422237"
SQ SEQUENCE 201 AA; 23278 MW; DD4820658F5655FA CRC64;
MTELTTPIYP LQRNWSWWFL NDDRNASWQD RLKKVYTFNT VPEFWAFYEA ILPPSGLNDL
CDYNVFRDDI QPKWEAPENW DGGRWLIIIN KGKTPEVLDA VWLEILLALI GEQFGKDMES
ICGLVCNVRG QGSKISVWTK NCNDDDTNMR IGVVLKEKLM AAASKAHSKP LFDVIHYQTH
RNCVKKTTSA LKYKFSLKSI V
