IF4A3_DROME
ID IF4A3_DROME Reviewed; 399 AA.
AC Q9VHS8; Q8SXH3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Eukaryotic initiation factor 4A-III {ECO:0000303|PubMed:22961380};
DE Short=eIF-4A-III {ECO:0000303|PubMed:14973490};
DE Short=eIF4A-III {ECO:0000303|PubMed:14973490};
DE EC=3.6.4.13 {ECO:0000303|PubMed:22961380};
GN ORFNames=CG7483 {ECO:0000312|FlyBase:FBgn0037573};
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 {ECO:0000312|EMBL:AAF54221.1};
RN [1] {ECO:0000312|EMBL:AAF54221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|EMBL:AAF54221.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL90373.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL90373.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AFH89818.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE EJC COMPLEX, INTERACTION WITH BTZ; MAGO AND
RP TSU, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-150.
RX PubMed=14973490; DOI=10.1038/nature02351;
RA Palacios I.M., Gatfield D., St Johnston D., Izaurralde E.;
RT "An eIF4AIII-containing complex required for mRNA localization and
RT nonsense-mediated mRNA decay.";
RL Nature 427:753-757(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=20946982; DOI=10.1016/j.cell.2010.09.036;
RA Roignant J.Y., Treisman J.E.;
RT "Exon junction complex subunits are required to splice Drosophila MAP
RT kinase, a large heterochromatic gene.";
RL Cell 143:238-250(2010).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=20946983; DOI=10.1016/j.cell.2010.09.014;
RA Ashton-Beaucage D., Udell C.M., Lavoie H., Baril C., Lefrancois M.,
RA Chagnon P., Gendron P., Caron-Lizotte O., Bonneil E., Thibault P.,
RA Therrien M.;
RT "The exon junction complex controls the splicing of MAPK and other long
RT intron-containing transcripts in Drosophila.";
RL Cell 143:251-262(2010).
RN [8] {ECO:0000305}
RP CATALYTIC ACTIVITY, IDENTIFICATION IN THE EJC COMPLEX, AND INTERACTION WITH
RP NCM.
RX PubMed=22961380; DOI=10.1038/nsmb.2380;
RA Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
RA Blanchette M., Le Hir H.;
RT "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes
RT exon junction complex assembly.";
RL Nat. Struct. Mol. Biol. 19:983-990(2012).
CC -!- FUNCTION: ATP-dependent RNA helicase (PubMed:22961380). Core component
CC of the splicing-dependent multiprotein exon junction complex (EJC)
CC deposited at splice junctions on mRNAs (PubMed:14973490,
CC PubMed:22961380). Involved in exon definition of genes containing long
CC introns, including the rolled/MAPK gene (PubMed:20946982,
CC PubMed:20946983). Has a role in oskar mRNA localization at the
CC posterior pole of the developing oocyte (PubMed:14973490).
CC {ECO:0000269|PubMed:14973490, ECO:0000269|PubMed:20946982,
CC ECO:0000269|PubMed:20946983, ECO:0000269|PubMed:22961380,
CC ECO:0000303|PubMed:14973490, ECO:0000303|PubMed:22961380}.
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 Evidence={ECO:0000303|PubMed:22961380};
CC -!- SUBUNIT: Part of the mRNA splicing-dependent exon junction complex
CC (EJC) complex; the core complex contains btz/CASC3, eIF4AIII, mago and
CC tsu/RBM8A (PubMed:14973490, PubMed:22961380). Interacts with btz/CASC3
CC and mago (PubMed:14973490). Interacts with ncm/CWC22 (PubMed:22961380).
CC {ECO:0000269|PubMed:14973490, ECO:0000269|PubMed:22961380}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14973490}.
CC -!- DEVELOPMENTAL STAGE: Localizes to the posterior pole of the oocyte
CC during stages 1-9 of oogenesis, where it colocalizes with mago.
CC {ECO:0000269|PubMed:14973490}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000255|RuleBase:RU000492}.
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DR EMBL; AE014297; AAF54221.1; -; Genomic_DNA.
DR EMBL; AY089635; AAL90373.1; -; mRNA.
DR EMBL; BT133445; AFH89818.1; -; mRNA.
DR RefSeq; NP_649788.2; NM_141531.3.
DR AlphaFoldDB; Q9VHS8; -.
DR SMR; Q9VHS8; -.
DR BioGRID; 66168; 20.
DR IntAct; Q9VHS8; 18.
DR STRING; 7227.FBpp0081324; -.
DR PaxDb; Q9VHS8; -.
DR PRIDE; Q9VHS8; -.
DR ABCD; Q9VHS8; 2 sequenced antibodies.
DR EnsemblMetazoa; FBtr0081834; FBpp0081324; FBgn0037573.
DR GeneID; 40987; -.
DR KEGG; dme:Dmel_CG7483; -.
DR UCSC; CG7483-RA; d. melanogaster.
DR FlyBase; FBgn0037573; CG7483.
DR VEuPathDB; VectorBase:FBgn0037573; -.
DR eggNOG; KOG0328; Eukaryota.
DR GeneTree; ENSGT00940000155037; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q9VHS8; -.
DR OMA; FTHRNGR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q9VHS8; -.
DR Reactome; R-DME-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-429947; Deadenylation of mRNA.
DR Reactome; R-DME-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DME-72187; mRNA 3'-end processing.
DR Reactome; R-DME-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 40987; 1 hit in 1 CRISPR screen.
DR ChiTaRS; eIF4AIII; fly.
DR GenomeRNAi; 40987; -.
DR PRO; PR:Q9VHS8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037573; Expressed in eye disc (Drosophila) and 25 other tissues.
DR Genevisible; Q9VHS8; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0045495; C:pole plasm; IDA:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:1903040; P:exon-exon junction complex assembly; IMP:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IGI:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0008380; P:RNA splicing; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; Developmental protein; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding; Transport.
FT CHAIN 1..399
FT /note="Eukaryotic initiation factor 4A-III"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431242"
FT DOMAIN 57..227
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 238..399
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 26..54
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 175..178
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 150
FT /note="G->S: In allele eIF4AIII-19; homozygous oocytes are
FT non-viable."
FT /evidence="ECO:0000269|PubMed:14973490"
FT CONFLICT 393
FT /note="M -> V (in Ref. 3; AAL90373)"
SQ SEQUENCE 399 AA; 45645 MW; B07BD3EF9276918B CRC64;
MARKNAQAED LSNVEFETSE DVEVIPTFNA MNLKEELLRG IYAYGFEKPS AIQQRSITPI
VKGRDVIAQA QSGTGKTATF SISILQSLDT TLRETQVLCL SPTRELAVQI QKVILALGDM
MNVQCHVCIG GTNLGEDIRK LDYGQHIVSG TPGRVFDMIK RRVLRTRAIK MLVLDEADEM
LNKGFKEQIY DVYRYLPPAT QVVLISATLP HEILEMTSKF MTDPIRILVK RDELTLEGIK
QFFVAVEREE WKFDTLCDLY DTLTITQAVI FCNTKRKVDW LTEKMREANF TVSSMHGDMP
QKERDEIMKE FRAGQSRVLI TTDVWARGID VQQVSLVINY DLPNNRELYI HRIGRSGRFG
RKGVAINFVK SDDIRILRDI EQYYSTQIDE MPMNVADLI
