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P60843 (IF4A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic initiation factor 4A-I

Short name=eIF-4A-I
Short name=eIF4A-I
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase eIF4A-1
Gene names
Name:Eif4a1
Synonyms:Ddx2a, Eif4a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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 EIF4G1/EIF4G3. Interacts with PAIP1, EIF4E and UPF2. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. May interact with NOM1. Interacts with PDCD4; this interferes with the interaction between EIF4A and EIF4G. Interacts with RBM4 By similarity.

Sequence similarities

Belongs to the DEAD box helicase family. eIF4A subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence CAA26842.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA26843.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA26845.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA26846.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 406405Eukaryotic initiation factor 4A-I
PRO_0000054935

Regions

Domain63 – 234172Helicase ATP-binding
Domain245 – 406162Helicase C-terminal
Nucleotide binding76 – 838ATP By similarity
Motif32 – 6029Q motif
Motif182 – 1854DEAD box

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue41Phosphoserine By similarity
Modified residue1181N6-acetyllysine By similarity
Modified residue1741N6-acetyllysine By similarity

Experimental info

Sequence conflict3001S → C in AAA50407. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P60843 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 6EF89939F3045420

FASTA40646,154
        10         20         30         40         50         60 
MSASQDSRSR DNGPDGMEPE GVIESNWNEI VDSFDDMNLS ESLLRGIYAY GFEKPSAIQQ 

        70         80         90        100        110        120 
RAILPCIKGY DVIAQAQSGT GKTATFAISI LQQIELDLKA TQALVLAPTR ELAQQIQKVV 

       130        140        150        160        170        180 
MALGDYMGAS CHACIGGTNV RAEVQKLQME APHIIVGTPG RVFDMLNRRY LSPKYIKMFV 

       190        200        210        220        230        240 
LDEADEMLSR GFKDQIYDIF QKLNSNTQVV LLSATMPSDV LEVTKKFMRD PIRILVKKEE 

       250        260        270        280        290        300 
LTLEGIRQFY INVEREEWKL DTLCDLYETL TITQAVIFIN TRRKVDWLTE KMHARDFTVS 

       310        320        330        340        350        360 
AMHGDMDQKE RDVIMREFRS GSSRVLITTD LLARGIDVQQ VSLVINYDLP TNRENYIHRI 

       370        380        390        400 
GRGGRFGRKG VAINMVTEED KRTLRDIETF YNTSIEEMPL NVADLI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of eukaryotic protein synthesis initiation factor genes: isolation and characterization of cDNA clones encoding factor eIF-4A."
Nielsen P.J., McMaster G.K., Trachsel H.
Nucleic Acids Res. 13:6867-6880(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and mapping of a gene for protein synthesis initiation factor 4A and its expression during differentiation of murine erythroleukemia cells."
Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.
Gene 70:231-243(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Miyashita A., Shimizu N., Nakajima T., Odani S., Kuwano R.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary gland.
[6]"Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A."
Pause A., Somenberg N.
EMBO J. 11:2643-2654(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03039 mRNA. Translation: CAA26842.1. Different initiation.
X03039 mRNA. Translation: CAA26843.1. Different initiation.
X03040 mRNA. Translation: CAA26845.1. Different initiation.
X03040 mRNA. Translation: CAA26846.1. Different initiation.
L36611 expand/collapse EMBL AC list , M22873, L36608, L36609, L36610 Genomic DNA. Translation: AAA50407.1.
AB011595 Genomic DNA. Translation: BAA25075.1.
AK077429 mRNA. Translation: BAC36796.1.
BC049915 mRNA. Translation: AAH49915.1.
IPIIPI00118676.
PIRFIMS4A. JS0039.
RefSeqNP_659207.1. NM_144958.4.
UniGeneMm.279821.
Mm.371557.
Mm.473799.

3D structure databases

ProteinModelPortalP60843.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-202155.
STRING10090.ENSMUSP00000099649.

PTM databases

PhosphoSiteP60843.

2D gel databases

REPRODUCTION-2DPAGEP60843.

Proteomic databases

PaxDbP60843.
PRIDEP60843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000163666; ENSMUSP00000127034; ENSMUSG00000059796.
GeneID13681.
KEGGmmu:13681.

Organism-specific databases

CTD1973.
MGIMGI:95303. Eif4a1.

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268797.
HOVERGENHBG107989.
InParanoidP60843.
KOK03257.
OMAIKMFILD.
OrthoDBEOG4640C1.

Gene expression databases

ArrayExpressP60843.
BgeeP60843.
CleanExMM_EIF4A1.
GenevestigatorP60843.
GermOnlineENSMUSG00000064241. Mus musculus.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284438.
SOURCESearch...

Entry information

Entry nameIF4A1_MOUSE
AccessionPrimary (citable) accession number: P60843
Secondary accession number(s): P04765, Q61516
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: April 13, 2004
Last modified: May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Translation initiation factors

List of translation initiation factor entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families