IF4A_DROME
ID IF4A_DROME Reviewed; 403 AA.
AC Q02748; A4UZV9; Q9U9Y6; Q9VMJ8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Eukaryotic initiation factor 4A;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A;
GN Name=eIF4A {ECO:0000303|PubMed:18590813, ECO:0000312|FlyBase:FBgn0001942};
GN Synonyms=eIF-4a {ECO:0000303|PubMed:8455559}, l(2L)162;
GN ORFNames=CG9075 {ECO:0000312|FlyBase:FBgn0001942};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8455559; DOI=10.1007/bf00282805;
RA Dorn R., Morawietz H., Reuter G., Saumweber H.;
RT "Identification of an essential Drosophila gene that is homologous to the
RT translation initiation factor eIF-4A of yeast and mouse.";
RL Mol. Gen. Genet. 237:233-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, INTERACTION WITH TUD AND VAS, AND SUBCELLULAR LOCATION.
RX PubMed=18590813; DOI=10.1016/j.mod.2008.06.005;
RA Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.;
RT "Isolation of new polar granule components in Drosophila reveals P body and
RT ER associated proteins.";
RL Mech. Dev. 125:865-873(2008).
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. Involved in germ cell formation.
CC {ECO:0000269|PubMed:18590813}.
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, eIF4E1 and eIF4G1. Interacts with tud and
CC vas. {ECO:0000269|PubMed:18590813}.
CC -!- INTERACTION:
CC Q02748; P22745: bam; NbExp=4; IntAct=EBI-85570, EBI-88504;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18590813}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
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DR EMBL; X69045; CAA48790.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52317.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10566.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10567.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10568.1; -; Genomic_DNA.
DR EMBL; AF145621; AAD38596.1; -; mRNA.
DR EMBL; AY069283; AAL39428.1; -; mRNA.
DR EMBL; AY121623; AAM51950.1; -; mRNA.
DR PIR; S30278; S30278.
DR RefSeq; NP_001245907.1; NM_001258978.3.
DR RefSeq; NP_001260117.1; NM_001273188.1.
DR RefSeq; NP_476595.1; NM_057247.5.
DR RefSeq; NP_723137.1; NM_164668.3.
DR RefSeq; NP_723138.1; NM_164669.3.
DR RefSeq; NP_723139.1; NM_164670.4.
DR AlphaFoldDB; Q02748; -.
DR SMR; Q02748; -.
DR BioGRID; 60000; 61.
DR DIP; DIP-18113N; -.
DR IntAct; Q02748; 24.
DR MINT; Q02748; -.
DR STRING; 7227.FBpp0297911; -.
DR PaxDb; Q02748; -.
DR PRIDE; Q02748; -.
DR ABCD; Q02748; 1 sequenced antibody.
DR DNASU; 33835; -.
DR EnsemblMetazoa; FBtr0079175; FBpp0078806; FBgn0001942.
DR EnsemblMetazoa; FBtr0079176; FBpp0078807; FBgn0001942.
DR EnsemblMetazoa; FBtr0079177; FBpp0078808; FBgn0001942.
DR EnsemblMetazoa; FBtr0079178; FBpp0078809; FBgn0001942.
DR EnsemblMetazoa; FBtr0307068; FBpp0297911; FBgn0001942.
DR EnsemblMetazoa; FBtr0331201; FBpp0303628; FBgn0001942.
DR GeneID; 33835; -.
DR KEGG; dme:Dmel_CG9075; -.
DR CTD; 33835; -.
DR FlyBase; FBgn0001942; eIF4A.
DR VEuPathDB; VectorBase:FBgn0001942; -.
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000153889; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q02748; -.
DR OMA; EHKDGQR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q02748; -.
DR Reactome; R-DME-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-429947; Deadenylation of mRNA.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; Q02748; -.
DR BioGRID-ORCS; 33835; 1 hit in 3 CRISPR screens.
DR ChiTaRS; eIF-4a; fly.
DR GenomeRNAi; 33835; -.
DR PRO; PR:Q02748; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001942; Expressed in second segment of antenna (Drosophila) and 22 other tissues.
DR ExpressionAtlas; Q02748; baseline and differential.
DR Genevisible; Q02748; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0046332; F:SMAD binding; IPI:FlyBase.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IGI:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..403
FT /note="Eukaryotic initiation factor 4A"
FT /id="PRO_0000054947"
FT DOMAIN 61..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 242..403
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 30..58
FT /note="Q motif"
FT MOTIF 179..182
FT /note="DEAD box"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 167
FT /note="Missing (in Ref. 1; CAA48790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 45879 MW; B870FF8C420CC4F2 CRC64;
MDDRNEIPQD GPASMEPEGV IESTWHEVYD NFDDMNLREE LLRGIYGYGF EKPSAIQQRA
IIPCVRGRDV IAQAQSGTGK TATFSIAILQ QIDTSIRECQ ALILAPTREL ATQIQRVVMA
LGEYMKVHSH ACIGGTNVRE DARILESGCH VVVGTPGRVY DMINRKVLRT QYIKLFVLDE
ADEMLSRGFK DQIQDVFKML PPDVQVILLS ATMPPDVLEV SRCFMRDPVS ILVKKEELTL
EGIKQFYVNV KQENWKLGTL CDLYDTLSIT QSVIFCNTRR KVDQLTQEMS IHNFTVSAMH
GDMEQRDREV IMKQFRSGSS RVLITTDLLA RGIDVQQVSL VINYDLPSNR ENYIHRIGRG
GRFGRKGVAI NFITDDDRRI LKDIEQFYHT TIEEMPANIA DLI
