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Protein

ATP-dependent RNA helicase eIF4A

Gene

TIF1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.6 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Kineticsi

  1. KM=470 µM for ATP2 Publications
  1. Vmax=2.6 pmol/sec/µg enzyme for ATP2 Publications

pH dependencei

Optimum pH is 6.0.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 73ATP8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • RNA-dependent ATPase activity Source: SGD
  • translation initiation factor activity Source: SGD

GO - Biological processi

  • regulation of gene expression Source: GO_Central
  • regulation of translational initiation Source: SGD
  • RNA secondary structure unwinding Source: GO_Central
  • translational initiation Source: SGD
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

BioCyciYEAST:G3O-31584-MONOMER.
YEAST:G3O-32027-MONOMER.
SABIO-RKP10081.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase eIF4A (EC:3.6.4.13)
Alternative name(s):
Eukaryotic initiation factor 4A
Short name:
eIF-4A
Stimulator factor I 37 kDa component
Translation initiation factor 1/2
p37
Gene namesi
Name:TIF1
Synonyms:TIF41A
Ordered Locus Names:YKR059W
AND
Name:TIF2
Synonyms:TIF41B
Ordered Locus Names:YJL138C
ORF Names:J0660
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componentsi: Chromosome X, Chromosome XI

Organism-specific databases

SGDiS000001767. TIF1.
S000003674. TIF2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic stress granule Source: SGD
  • eukaryotic translation initiation factor 4F complex Source: SGD
  • ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24F → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi42F → A: Slow growth in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi46S → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi49Q → A: Reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi49Q → E: Increases about 3-fold ATP binding but reduces about 2-fold ATPase activity in vitro. 1 Publication1
Mutagenesisi66A → D: Slow growth. 2 Publications1
Mutagenesisi66A → V: Lethal and dominant negative if overexpressed in vivo. Impairs ATP hydrolysis, RNA-helicase and translation activity in vitro. 2 Publications1
Mutagenesisi72K → A: Lethal in vivo and reduces ATP binding and ATPase activity in vitro. 1 Publication1
Mutagenesisi79A → V in TIF1-1; no growth at 36 degrees Celsius. 1 Publication1
Mutagenesisi126G → D: Lethal. 1 Publication1
Mutagenesisi127G → D: Slow growth. 1 Publication1
Mutagenesisi145G → D: Lethal. 1 Publication1
Mutagenesisi145G → S: Slow growth. 1 Publication1
Mutagenesisi170D → E: Lethal. 1 Publication1
Mutagenesisi173D → H: Lethal. 1 Publication1
Mutagenesisi311S → F: Slow growth. 1 Publication1
Mutagenesisi347R → E, G, I, S or T: Lethal and dominant negative if overexpressed. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000549682 – 395ATP-dependent RNA helicase eIF4AAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei73PhosphothreonineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei129PhosphoserineCombined sources1
Modified residuei146PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP10081.
PRIDEiP10081.

2D gel databases

SWISS-2DPAGEP10081.

PTM databases

iPTMnetiP10081.

Interactioni

Subunit structurei

Component of the eIF4F complex, which composition varies with external and internal environmental conditions. It is composed of at least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632) (By similarity). Interacts with eIF4G1/TIF4631 and eIF4G2/TIF4632.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TIF4631P399357EBI-9017,EBI-9002

Protein-protein interaction databases

BioGridi33619. 155 interactors.
34190. 127 interactors.
DIPiDIP-4571N.
IntActiP10081. 52 interactors.
MINTiMINT-8285693.

Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 17Combined sources5
Helixi24 – 27Combined sources4
Helixi31 – 40Combined sources10
Helixi47 – 57Combined sources11
Beta strandi62 – 65Combined sources4
Helixi72 – 83Combined sources12
Beta strandi93 – 96Combined sources4
Helixi100 – 113Combined sources14
Turni114 – 116Combined sources3
Beta strandi121 – 124Combined sources4
Helixi130 – 139Combined sources10
Beta strandi141 – 145Combined sources5
Helixi147 – 155Combined sources9
Beta strandi166 – 170Combined sources5
Helixi172 – 177Combined sources6
Helixi181 – 190Combined sources10
Beta strandi196 – 203Combined sources8
Helixi206 – 215Combined sources10
Beta strandi220 – 222Combined sources3
Beta strandi235 – 243Combined sources9
Helixi244 – 246Combined sources3
Helixi247 – 257Combined sources11
Beta strandi263 – 269Combined sources7
Helixi270 – 282Combined sources13
Beta strandi287 – 290Combined sources4
Helixi296 – 307Combined sources12
Beta strandi312 – 317Combined sources6
Helixi318 – 320Combined sources3
Turni321 – 323Combined sources3
Beta strandi330 – 336Combined sources7
Helixi341 – 346Combined sources6
Beta strandi359 – 365Combined sources7
Turni366 – 368Combined sources3
Helixi369 – 378Combined sources10
Beta strandi383 – 385Combined sources3
Turni391 – 394Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FUKX-ray1.75A231-395[»]
1FUUX-ray2.50A/B2-395[»]
1QDEX-ray2.00A9-232[»]
1QVAX-ray2.50A2-224[»]
2VSOX-ray2.60A/B1-395[»]
2VSXX-ray2.80A/B1-395[»]
ProteinModelPortaliP10081.
SMRiP10081.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10081.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 222Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST170
Domaini233 – 394Helicase C-terminalPROSITE-ProRule annotationAdd BLAST162

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi22 – 50Q motifAdd BLAST29
Motifi170 – 173DEAD box4

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00860000134567.
HOGENOMiHOG000268797.
InParanoidiP10081.
KOiK03257.
OMAiPGPPQQD.
OrthoDBiEOG092C2B1L.

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. 2 hits.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10081-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGITDIEE SQIQTNYDKV VYKFDDMELD ENLLRGVFGY GFEEPSAIQQ
60 70 80 90 100
RAIMPIIEGH DVLAQAQSGT GKTGTFSIAA LQRIDTSVKA PQALMLAPTR
110 120 130 140 150
ELALQIQKVV MALAFHMDIK VHACIGGTSF VEDAEGLRDA QIVVGTPGRV
160 170 180 190 200
FDNIQRRRFR TDKIKMFILD EADEMLSSGF KEQIYQIFTL LPPTTQVVLL
210 220 230 240 250
SATMPNDVLE VTTKFMRNPV RILVKKDELT LEGIKQFYVN VEEEEYKYEC
260 270 280 290 300
LTDLYDSISV TQAVIFCNTR RKVEELTTKL RNDKFTVSAI YSDLPQQERD
310 320 330 340 350
TIMKEFRSGS SRILISTDLL ARGIDVQQVS LVINYDLPAN KENYIHRIGR
360 370 380 390
GGRFGRKGVA INFVTNEDVG AMRELEKFYS TQIEELPSDI ATLLN
Length:395
Mass (Da):44,697
Last modified:January 23, 2007 - v3
Checksum:i19D8C133C815DD48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12813 Genomic DNA. Translation: CAA31301.1.
X12814 Genomic DNA. Translation: CAA31302.1.
X58099 Genomic DNA. Translation: CAA41110.1.
X87371 Genomic DNA. Translation: CAA60817.1.
Z49413 Genomic DNA. Translation: CAA89433.1.
U25436 Genomic DNA. Translation: AAA91645.1.
Z28284 Genomic DNA. Translation: CAA82138.1.
BK006943 Genomic DNA. Translation: DAA08662.1.
BK006944 Genomic DNA. Translation: DAA09210.1.
PIRiS05835. FIBY1.
RefSeqiNP_012397.1. NM_001181571.1.
NP_012985.3. NM_001179849.3.

Genome annotation databases

EnsemblFungiiYJL138C; YJL138C; YJL138C.
YKR059W; YKR059W; YKR059W.
GeneIDi853303.
853933.
KEGGisce:YJL138C.
sce:YKR059W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12813 Genomic DNA. Translation: CAA31301.1.
X12814 Genomic DNA. Translation: CAA31302.1.
X58099 Genomic DNA. Translation: CAA41110.1.
X87371 Genomic DNA. Translation: CAA60817.1.
Z49413 Genomic DNA. Translation: CAA89433.1.
U25436 Genomic DNA. Translation: AAA91645.1.
Z28284 Genomic DNA. Translation: CAA82138.1.
BK006943 Genomic DNA. Translation: DAA08662.1.
BK006944 Genomic DNA. Translation: DAA09210.1.
PIRiS05835. FIBY1.
RefSeqiNP_012397.1. NM_001181571.1.
NP_012985.3. NM_001179849.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FUKX-ray1.75A231-395[»]
1FUUX-ray2.50A/B2-395[»]
1QDEX-ray2.00A9-232[»]
1QVAX-ray2.50A2-224[»]
2VSOX-ray2.60A/B1-395[»]
2VSXX-ray2.80A/B1-395[»]
ProteinModelPortaliP10081.
SMRiP10081.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33619. 155 interactors.
34190. 127 interactors.
DIPiDIP-4571N.
IntActiP10081. 52 interactors.
MINTiMINT-8285693.

PTM databases

iPTMnetiP10081.

2D gel databases

SWISS-2DPAGEP10081.

Proteomic databases

MaxQBiP10081.
PRIDEiP10081.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL138C; YJL138C; YJL138C.
YKR059W; YKR059W; YKR059W.
GeneIDi853303.
853933.
KEGGisce:YJL138C.
sce:YKR059W.

Organism-specific databases

SGDiS000001767. TIF1.
S000003674. TIF2.

Phylogenomic databases

GeneTreeiENSGT00860000134567.
HOGENOMiHOG000268797.
InParanoidiP10081.
KOiK03257.
OMAiPGPPQQD.
OrthoDBiEOG092C2B1L.

Enzyme and pathway databases

BioCyciYEAST:G3O-31584-MONOMER.
YEAST:G3O-32027-MONOMER.
SABIO-RKP10081.

Miscellaneous databases

EvolutionaryTraceiP10081.
PROiP10081.

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. 2 hits.
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...

Entry informationi

Entry nameiIF4A_YEAST
AccessioniPrimary (citable) accession number: P10081
Secondary accession number(s): D6VW46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 199 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

TIF1 and TIF2 code for the same protein.
Present with 106000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  6. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.