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Q9QZD9 (EIF3I_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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 translation initiation factor 3 subunit I
Short name=eIF3i
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 2
TGF-beta receptor-interacting protein 1
Short name=TRIP-1
eIF-3-beta
eIF3 p36
Gene names
Name:Eif3i
Synonyms:Eif3s2, Trip1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. HAMAP-Rule MF_03008

Subunit structure

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Ref.7

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Phosphorylated by TGF-beta type II receptor By similarity.

Sequence similarities

Belongs to the eIF-3 subunit I family.

Contains 5 WD repeats.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DomainRepeat
WD repeat
   Molecular functionInitiation factor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componenteukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functiontranslation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Eukaryotic translation initiation factor 3 subunit I HAMAP-Rule MF_03008
PRO_0000051037

Regions

Repeat8 – 4740WD 1 HAMAP-Rule MF_03008
Repeat50 – 9142WD 2 HAMAP-Rule MF_03008
Repeat144 – 18340WD 3 HAMAP-Rule MF_03008
Repeat186 – 22540WD 4 HAMAP-Rule MF_03008
Repeat283 – 32442WD 5 HAMAP-Rule MF_03008

Amino acid modifications

Modified residue2641N6-acetyllysine By similarity
Modified residue3081Phosphotyrosine By similarity
Cross-link282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QZD9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2B29405772675CC0

FASTA32536,461
        10         20         30         40         50         60 
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA 

        70         80         90        100        110        120 
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC 

       130        140        150        160        170        180 
FVSFFDLRDP SQIDSNEPYM KIPCNDSKIT SAVWGPLGEC VIAGHESGEL NQYSAKSGEV 

       190        200        210        220        230        240 
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN 

       250        260        270        280        290        300 
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY 

       310        320 
SSGGEDGYVR IHYFDPQYFE FEFEA

« Hide

References

« Hide 'large scale' references
[1]"Mouse TRIP-1 gene isolated from murine L-929 cells."
Zhou A., Silverman R.H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Mus musculus TGF-beta receptor interacting protein 1 (TRIP1)."
Joseph P., Fan L., Whong W.-Z., Ong T.-M.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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.
Tissue: Embryo, Embryonic stem cell and Kidney.
[4]"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: C57BL/6J.
Tissue: Mammary gland.
[5]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 269-280.
Tissue: Brain.
[6]"mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B AND EIF4G1.
[7]"Reconstitution reveals the functional core of mammalian eIF3."
Masutani M., Sonenberg N., Yokoyama S., Imataka H.
EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF188297 mRNA. Translation: AAF01455.1.
AF271072 mRNA. Translation: AAF76199.1.
AK012375 mRNA. Translation: BAB28197.1.
AK002896 mRNA. Translation: BAB22440.1.
AK010781 mRNA. Translation: BAB27177.1.
BC029625 mRNA. Translation: AAH29625.1.
IPIIPI00269613.
RefSeqNP_061269.1. NM_018799.2.
UniGeneMm.250874.

3D structure databases

ProteinModelPortalQ9QZD9.
SMRQ9QZD9. Positions 1-324.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-1869798.

PTM databases

PhosphoSiteQ9QZD9.

2D gel databases

REPRODUCTION-2DPAGEQ9QZD9.

Proteomic databases

PaxDbQ9QZD9.
PRIDEQ9QZD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102593; ENSMUSP00000099653; ENSMUSG00000028798.
GeneID54709.
KEGGmmu:54709.

Organism-specific databases

CTD8668.
MGIMGI:1860763. Eif3i.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00630000089849.
HOGENOMHOG000231322.
HOVERGENHBG000900.
InParanoidQ9QZD9.
KOK03246.
OMAATVAGWS.
OrthoDBEOG4HX519.

Gene expression databases

ArrayExpressQ9QZD9.
BgeeQ9QZD9.
GenevestigatorQ9QZD9.
GermOnlineENSMUSG00000028798. Mus musculus.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
HAMAPMF_03008. eIF3i.
InterProIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 4 hits.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3I. mouse.
NextBio311544.
SOURCESearch...

Entry information

Entry nameEIF3I_MOUSE
AccessionPrimary (citable) accession number: Q9QZD9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 103 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents