IF4A_CAEEL
ID IF4A_CAEEL Reviewed; 402 AA.
AC P27639; Q4TTC4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Eukaryotic initiation factor 4A;
DE Short=eIF-4A;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A;
DE AltName: Full=Initiation factor 1;
GN Name=inf-1; ORFNames=F57B9.6;
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] (ISOFORM A).
RC STRAIN=Bristol N2;
RX PubMed=1641346; DOI=10.1093/nar/20.14.3783;
RA Roussell D.L., Bennett K.L.;
RT "Caenorhabditis cDNA encodes an eIF-4A-like protein.";
RL Nucleic Acids Res. 20:3783-3783(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F
CC complex involved in cap recognition and is required for mRNA binding to
CC ribosome. In the current model of translation initiation, eIF4A unwinds
CC RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC allow efficient binding of the small ribosomal subunit, and subsequent
CC scanning for the initiator codon.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P27639-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P27639-2; Sequence=VSP_020640;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; Z12116; CAA78102.1; -; mRNA.
DR EMBL; FO081266; CCD70313.1; -; Genomic_DNA.
DR EMBL; FO081266; CCD70314.1; -; Genomic_DNA.
DR PIR; S26281; S26281.
DR RefSeq; NP_001022623.1; NM_001027452.2. [P27639-1]
DR RefSeq; NP_001022624.1; NM_001027453.2. [P27639-2]
DR AlphaFoldDB; P27639; -.
DR SMR; P27639; -.
DR BioGRID; 41180; 15.
DR DIP; DIP-27102N; -.
DR IntAct; P27639; 1.
DR STRING; 6239.F57B9.6a.2; -.
DR EPD; P27639; -.
DR PaxDb; P27639; -.
DR PeptideAtlas; P27639; -.
DR PRIDE; P27639; -.
DR EnsemblMetazoa; F57B9.6a.1; F57B9.6a.1; WBGene00002083. [P27639-1]
DR EnsemblMetazoa; F57B9.6b.1; F57B9.6b.1; WBGene00002083. [P27639-2]
DR GeneID; 175966; -.
DR KEGG; cel:CELE_F57B9.6; -.
DR UCSC; F57B9.6a.1; c. elegans. [P27639-1]
DR CTD; 175966; -.
DR WormBase; F57B9.6a; CE01341; WBGene00002083; inf-1. [P27639-1]
DR WormBase; F57B9.6b; CE38524; WBGene00002083; inf-1. [P27639-2]
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000153889; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; P27639; -.
DR OMA; EHKDGQR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; P27639; -.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:P27639; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002083; Expressed in germ line (C elegans) and 5 other tissues.
DR GO; GO:0043186; C:P granule; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044728; EIF4A_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..402
FT /note="Eukaryotic initiation factor 4A"
FT /id="PRO_0000054945"
FT DOMAIN 60..230
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 241..402
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 29..57
FT /note="Q motif"
FT MOTIF 178..181
FT /note="DEAD box"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_020640"
SQ SEQUENCE 402 AA; 45408 MW; AB1CE281F9FC8881 CRC64;
MTDVKNDVNV SSVVDADGLI EGNYDQVVES FDDMELKEEL LRGIYGFGFE KPSAIQKRAI
VPCTTGKDVI AQAQSGTGKT ATFSVSILQR IDHEDPHVQA LVMAPTRELA QQIQKVMSAL
GEYLNVNILP CIGGTSVRDD QRKLEAGIHV VVGTPGRVGD MINRNALDTS RIKMFVLDEA
DEMLSRGFKD QIYEVFRSMP QDVQVVLLSA TMPSEVLDVT NRFMRNPIRI LVKKDELTLE
GIRQFYINVQ KDEWKFDCLC DLYNVVNVTQ AVIFCNTRRK VDTLTEKMTE NQFTVSCLHG
DMDQAERDTI MREFRSGSSR VLITTDILAR GIDVQQVSLV INYDLPSNRE NYIHRIGRSG
RFGRKGVAIN FVTENDARQL KEIESYYTTQ IEEMPESIAD LI
