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IF4E2_CAEEL
ID   IF4E2_CAEEL             Reviewed;         228 AA.
AC   Q21693;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Eukaryotic translation initiation factor 4E-2;
DE            Short=eIF-4E-2;
DE            Short=eIF4E-2;
DE   AltName: Full=eIF-4F 25 kDa subunit;
DE   AltName: Full=mRNA cap-binding protein;
GN   Name=ife-2; ORFNames=R04A9.4;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Bristol N2;
RX   PubMed=9553113; DOI=10.1074/jbc.273.17.10538;
RA   Jankowska-Anyszka M., Lamphear B.J., Aamodt E.J., Harrington T.,
RA   Darzynkiewicz E., Stolarski R., Rhoads R.E.;
RT   "Multiple isoforms of eukaryotic protein synthesis initiation factor 4E in
RT   Caenorhabditis elegans can distinguish between mono- and trimethylated mRNA
RT   cap structures.";
RL   J. Biol. Chem. 273:10538-10542(1998).
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   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   [4]
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   [5]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17277769; DOI=10.1038/nature05603;
RA   Syntichaki P., Troulinaki K., Tavernarakis N.;
RT   "eIF4E function in somatic cells modulates ageing in Caenorhabditis
RT   elegans.";
RL   Nature 445:922-926(2007).
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 (PubMed:10744754, PubMed:9553113).
CC       Probably by regulating mRNA translation in somatic cells, negatively
CC       regulates lifespan independently of daf-2/insulin and let-363/TOR
CC       pathways (PubMed:17277769). Negatively regulates resistance to
CC       oxidative stress (PubMed:17277769). May play a role in embryonic
CC       development (PubMed:17277769). {ECO:0000269|PubMed:10744754,
CC       ECO:0000269|PubMed:17277769, ECO:0000269|PubMed:9553113}.
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   -!- INTERACTION:
CC       Q21693; Q9XW13: mxt-1; NbExp=5; IntAct=EBI-330154, EBI-330111;
CC   -!- TISSUE SPECIFICITY: Highly expressed in all somatic tissues.
CC       {ECO:0000269|PubMed:11641215, ECO:0000269|PubMed:17277769}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at the 2-fold embryonic stage and
CC       throughout larval stages and adulthood. {ECO:0000269|PubMed:17277769}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases lifespan.
CC       Lifespan is further increased in an age-1 hx546, daf-2 e1370, clk-1
CC       qm30 or eat-2 ad465 mutant background. {ECO:0000269|PubMed:17277769}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC       {ECO:0000305}.
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DR   EMBL; FO080331; CCD62912.1; -; Genomic_DNA.
DR   PIR; T16678; T16678.
DR   RefSeq; NP_508094.1; NM_075693.4.
DR   AlphaFoldDB; Q21693; -.
DR   SMR; Q21693; -.
DR   BioGRID; 45346; 4.
DR   DIP; DIP-25396N; -.
DR   IntAct; Q21693; 1.
DR   STRING; 6239.R04A9.4; -.
DR   iPTMnet; Q21693; -.
DR   EPD; Q21693; -.
DR   PaxDb; Q21693; -.
DR   PeptideAtlas; Q21693; -.
DR   EnsemblMetazoa; R04A9.4.1; R04A9.4.1; WBGene00002060.
DR   GeneID; 180393; -.
DR   KEGG; cel:CELE_R04A9.4; -.
DR   UCSC; R04A9.4; c. elegans.
DR   CTD; 180393; -.
DR   WormBase; R04A9.4; CE04791; WBGene00002060; ife-2.
DR   eggNOG; KOG1670; Eukaryota.
DR   HOGENOM; CLU_043552_1_0_1; -.
DR   InParanoid; Q21693; -.
DR   OMA; FWFDTPS; -.
DR   OrthoDB; 1394271at2759; -.
DR   PhylomeDB; Q21693; -.
DR   PRO; PR:Q21693; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00002060; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:WormBase.
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:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR   GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IMP: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   Disulfide bond; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding; Translation regulation.
FT   CHAIN           1..228
FT                   /note="Eukaryotic translation initiation factor 4E-2"
FT                   /id="PRO_0000193644"
FT   DISULFID        130..134
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   228 AA;  25727 MW;  BAC8DB2B01CEDE41 CRC64;
     MSEEPVAAPG TISHPVYKLK RNWTWWYLND ERNKSWEERL KNVKTFSSVG EFWALHDSIK
     PPSGLNPPSD YNVFRDGIEP MWEVPQNQNG GRWLITIEKG RTPEIMDTIW TEILMAMIGE
     QFSDDIESLC GIVCNVRGKG SKISVWTTNS ADDGANLRIG GVLKQVLNNA SMIHQRPLYD
     VLRYEDHESC QKKTSSGVKA KHAIYAVEPR EEKAPVPVST ETPATPAT
 
 
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