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Protein

Eukaryotic translation initiation factor 3 subunit I

Gene

Trip1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome.

GO - Molecular functioni

  • translation initiation factor activity Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
SignaLinkiO02195.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit IUniRule annotation
Short name:
eIF3iUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2UniRule annotation
TRIP-1 homolog
eIF-3-betaUniRule annotation
Gene namesi
Name:Trip1UniRule annotation
Synonyms:DmTRIP, eif3-S2UniRule annotation
ORF Names:CG8882
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0015834. Trip1.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: FlyBase
  • eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic translation initiation factor 3 complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Eukaryotic translation initiation factor 3 subunit IPRO_0000051038Add
BLAST

Proteomic databases

PaxDbiO02195.
PRIDEiO02195.

Expressioni

Gene expression databases

BgeeiO02195.
GenevisibleiO02195. DM.

Interactioni

Subunit structurei

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex. The eIF-3 complex interacts with pix.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi59895. 10 interactions.
DIPiDIP-18772N.
IntActiO02195. 3 interactions.
MINTiMINT-1576694.
STRINGi7227.FBpp0078689.

Structurei

3D structure databases

ProteinModelPortaliO02195.
SMRiO02195. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4740WD 1Add
BLAST
Repeati50 – 8940WD 2Add
BLAST
Repeati145 – 18440WD 3Add
BLAST
Repeati188 – 22740WD 4Add
BLAST
Repeati285 – 32642WD 5Add
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit I family.UniRule annotation
Contains 5 WD repeats.UniRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0643. Eukaryota.
ENOG410XQ3E. LUCA.
GeneTreeiENSGT00630000089849.
InParanoidiO02195.
KOiK03246.
OMAiKATVCAF.
OrthoDBiEOG7PVWPK.
PhylomeDBiO02195.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O02195-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPLMLQGHE RSITQIKYNR EGDLLFSCSK DQKPNVWYSL NGERLGTYDG
60 70 80 90 100
HQGAVWCLDV DWESRKLITG AGDMTAKIWD VEYGTVIASI PTKSSVRTSN
110 120 130 140 150
FSFSGNQAAY STDKAMGQSC ELFLIDVRNA DSSLSEQEPT LRIPMTESKI
160 170 180 190 200
TSMLWGPLDE TIITGHDNGN IAIWDIRKGQ KVVDSGTDHS AGINDMQLSK
210 220 230 240 250
DGTMFVTASK DTTAKLFDSE SLMCLKTYKT ERPVNSAAIS PIMDHVVLGG
260 270 280 290 300
GQDAMEVTTT STKAGKFDSR FFHLIYEEEF ARLKGHFGPI NSLAFHPDGK
310 320
SYASGGEDGF VRVQTFDSTY FENIFE
Length:326
Mass (Da):36,160
Last modified:July 1, 1997 - v1
Checksum:iB07D35F9E47F3F31
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90930 mRNA. Translation: AAB53431.1.
AE014134 Genomic DNA. Translation: AAF52183.1.
AY118527 mRNA. Translation: AAM49896.1.
RefSeqiNP_523478.1. NM_078754.4.
UniGeneiDm.2654.

Genome annotation databases

EnsemblMetazoaiFBtr0079053; FBpp0078689; FBgn0015834.
GeneIDi33710.
KEGGidme:Dmel_CG8882.
UCSCiCG8882-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U90930 mRNA. Translation: AAB53431.1.
AE014134 Genomic DNA. Translation: AAF52183.1.
AY118527 mRNA. Translation: AAM49896.1.
RefSeqiNP_523478.1. NM_078754.4.
UniGeneiDm.2654.

3D structure databases

ProteinModelPortaliO02195.
SMRiO02195. Positions 1-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59895. 10 interactions.
DIPiDIP-18772N.
IntActiO02195. 3 interactions.
MINTiMINT-1576694.
STRINGi7227.FBpp0078689.

Proteomic databases

PaxDbiO02195.
PRIDEiO02195.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079053; FBpp0078689; FBgn0015834.
GeneIDi33710.
KEGGidme:Dmel_CG8882.
UCSCiCG8882-RA. d. melanogaster.

Organism-specific databases

CTDi33710.
FlyBaseiFBgn0015834. Trip1.

Phylogenomic databases

eggNOGiKOG0643. Eukaryota.
ENOG410XQ3E. LUCA.
GeneTreeiENSGT00630000089849.
InParanoidiO02195.
KOiK03246.
OMAiKATVCAF.
OrthoDBiEOG7PVWPK.
PhylomeDBiO02195.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
SignaLinkiO02195.

Miscellaneous databases

GenomeRNAii33710.
NextBioi784905.
PROiO02195.

Gene expression databases

BgeeiO02195.
GenevisibleiO02195. DM.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
HAMAPiMF_03008. eIF3i.
InterProiIPR027525. eIF3i.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the TRIP-1 homologs from Saccharomyces cerevisiae and Drosophila melanogaster."
    Cho S.H., Evangelista C., Padgett R.W.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Embryo.
  5. "The essential Drosophila ATP-binding cassette domain protein, pixie, binds the 40 S ribosome in an ATP-dependent manner and is required for translation initiation."
    Andersen D.S., Leevers S.J.
    J. Biol. Chem. 282:14752-14760(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIX, ASSOCIATION WITH THE 40S RIBOSOME.

Entry informationi

Entry nameiEIF3I_DROME
AccessioniPrimary (citable) accession number: O02195
Secondary accession number(s): Q540Y6, Q9VMX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 11, 2016
This is version 119 of the entry and version 1 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.