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Protein

Eukaryotic initiation factor 4A

Gene

eIF-4a

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. Involved in germ cell formation.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 818ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • mRNA binding Source: FlyBase
  • RNA cap binding Source: FlyBase
  • RNA helicase activity Source: FlyBase
  • single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: FlyBase
  • translation initiation factor activity Source: FlyBase

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • centrosome organization Source: FlyBase
  • DNA unwinding involved in DNA replication Source: FlyBase
  • dorsal/ventral axis specification Source: FlyBase
  • female germ-line stem cell asymmetric division Source: FlyBase
  • germ-line stem cell population maintenance Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • instar larval development Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • oogenesis Source: FlyBase
  • pole cell formation Source: FlyBase
  • regulation of alternative mRNA splicing, via spliceosome Source: FlyBase
  • translational initiation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-1169408. ISG15 antiviral mechanism.
R-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-429947. Deadenylation of mRNA.
R-DME-72649. Translation initiation complex formation.
R-DME-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic initiation factor 4A (EC:3.6.4.13)
Short name:
eIF-4A
Alternative name(s):
ATP-dependent RNA helicase eIF4A
Gene namesi
Name:eIF-4a
Synonyms:eIF4A, l(2L)162
ORF Names:CG9075
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001942. eIF-4a.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.

GO - Cellular componenti

  • centrosome Source: FlyBase
  • cytosol Source: FlyBase
  • eukaryotic translation initiation factor 4F complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitotic spindle Source: FlyBase
  • nucleus Source: FlyBase
  • P granule Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Eukaryotic initiation factor 4APRO_0000054947Add
BLAST

Proteomic databases

PaxDbiQ02748.
PRIDEiQ02748.

Expressioni

Gene expression databases

BgeeiQ02748.
ExpressionAtlasiQ02748. differential.
GenevisibleiQ02748. DM.

Interactioni

Subunit structurei

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G. Interacts with tud and vas.1 Publication

Protein-protein interaction databases

BioGridi60000. 35 interactions.
DIPiDIP-18113N.
IntActiQ02748. 23 interactions.
MINTiMINT-892982.
STRINGi7227.FBpp0297911.

Structurei

3D structure databases

ProteinModelPortaliQ02748.
SMRiQ02748. Positions 20-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 231171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini242 – 403162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 5829Q motifAdd
BLAST
Motifi179 – 1824DEAD box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0327. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00530000062880.
InParanoidiQ02748.
KOiK03257.
OMAiEQKETQA.
OrthoDBiEOG7XPZ5M.
PhylomeDBiQ02748.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02748-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDRNEIPQD GPASMEPEGV IESTWHEVYD NFDDMNLREE LLRGIYGYGF
60 70 80 90 100
EKPSAIQQRA IIPCVRGRDV IAQAQSGTGK TATFSIAILQ QIDTSIRECQ
110 120 130 140 150
ALILAPTREL ATQIQRVVMA LGEYMKVHSH ACIGGTNVRE DARILESGCH
160 170 180 190 200
VVVGTPGRVY DMINRKVLRT QYIKLFVLDE ADEMLSRGFK DQIQDVFKML
210 220 230 240 250
PPDVQVILLS ATMPPDVLEV SRCFMRDPVS ILVKKEELTL EGIKQFYVNV
260 270 280 290 300
KQENWKLGTL CDLYDTLSIT QSVIFCNTRR KVDQLTQEMS IHNFTVSAMH
310 320 330 340 350
GDMEQRDREV IMKQFRSGSS RVLITTDLLA RGIDVQQVSL VINYDLPSNR
360 370 380 390 400
ENYIHRIGRG GRFGRKGVAI NFITDDDRRI LKDIEQFYHT TIEEMPANIA

DLI
Length:403
Mass (Da):45,879
Last modified:December 1, 2000 - v3
Checksum:iB870FF8C420CC4F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671Missing in CAA48790 (PubMed:8455559).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69045 Genomic DNA. Translation: CAA48790.1.
AE014134 Genomic DNA. Translation: AAF52317.2.
AE014134 Genomic DNA. Translation: AAN10566.1.
AE014134 Genomic DNA. Translation: AAN10567.1.
AE014134 Genomic DNA. Translation: AAN10568.1.
AF145621 mRNA. Translation: AAD38596.1.
AY069283 mRNA. Translation: AAL39428.1.
AY121623 mRNA. Translation: AAM51950.1.
PIRiS30278.
RefSeqiNP_001245907.1. NM_001258978.3.
NP_001260117.1. NM_001273188.1.
NP_476595.1. NM_057247.5.
NP_723137.1. NM_164668.3.
NP_723138.1. NM_164669.3.
NP_723139.1. NM_164670.4.
UniGeneiDm.7226.

Genome annotation databases

EnsemblMetazoaiFBtr0079175; FBpp0078806; FBgn0001942.
FBtr0079176; FBpp0078807; FBgn0001942.
FBtr0079177; FBpp0078808; FBgn0001942.
FBtr0079178; FBpp0078809; FBgn0001942.
FBtr0307068; FBpp0297911; FBgn0001942.
FBtr0331201; FBpp0303628; FBgn0001942.
GeneIDi33835.
KEGGidme:Dmel_CG9075.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69045 Genomic DNA. Translation: CAA48790.1.
AE014134 Genomic DNA. Translation: AAF52317.2.
AE014134 Genomic DNA. Translation: AAN10566.1.
AE014134 Genomic DNA. Translation: AAN10567.1.
AE014134 Genomic DNA. Translation: AAN10568.1.
AF145621 mRNA. Translation: AAD38596.1.
AY069283 mRNA. Translation: AAL39428.1.
AY121623 mRNA. Translation: AAM51950.1.
PIRiS30278.
RefSeqiNP_001245907.1. NM_001258978.3.
NP_001260117.1. NM_001273188.1.
NP_476595.1. NM_057247.5.
NP_723137.1. NM_164668.3.
NP_723138.1. NM_164669.3.
NP_723139.1. NM_164670.4.
UniGeneiDm.7226.

3D structure databases

ProteinModelPortaliQ02748.
SMRiQ02748. Positions 20-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60000. 35 interactions.
DIPiDIP-18113N.
IntActiQ02748. 23 interactions.
MINTiMINT-892982.
STRINGi7227.FBpp0297911.

Proteomic databases

PaxDbiQ02748.
PRIDEiQ02748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079175; FBpp0078806; FBgn0001942.
FBtr0079176; FBpp0078807; FBgn0001942.
FBtr0079177; FBpp0078808; FBgn0001942.
FBtr0079178; FBpp0078809; FBgn0001942.
FBtr0307068; FBpp0297911; FBgn0001942.
FBtr0331201; FBpp0303628; FBgn0001942.
GeneIDi33835.
KEGGidme:Dmel_CG9075.

Organism-specific databases

CTDi33835.
FlyBaseiFBgn0001942. eIF-4a.

Phylogenomic databases

eggNOGiKOG0327. Eukaryota.
COG0513. LUCA.
GeneTreeiENSGT00530000062880.
InParanoidiQ02748.
KOiK03257.
OMAiEQKETQA.
OrthoDBiEOG7XPZ5M.
PhylomeDBiQ02748.

Enzyme and pathway databases

ReactomeiR-DME-1169408. ISG15 antiviral mechanism.
R-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-429947. Deadenylation of mRNA.
R-DME-72649. Translation initiation complex formation.
R-DME-72662. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSieIF-4a. fly.
GenomeRNAii33835.
PROiQ02748.

Gene expression databases

BgeeiQ02748.
ExpressionAtlasiQ02748. differential.
GenevisibleiQ02748. DM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of an essential Drosophila gene that is homologous to the translation initiation factor eIF-4A of yeast and mouse."
    Dorn R., Morawietz H., Reuter G., Saumweber H.
    Mol. Gen. Genet. 237:233-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head and Ovary.
  6. "Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins."
    Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.
    Mech. Dev. 125:865-873(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TUD AND VAS, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiIF4A_DROME
AccessioniPrimary (citable) accession number: Q02748
Secondary accession number(s): A4UZV9, Q9U9Y6, Q9VMJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Translation initiation factors
    List of translation initiation factor entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.