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P23116 (EIF3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. 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 translation initiation factor 3 subunit A

Short name=eIF3a
Alternative name(s):
Centrosomin
Eukaryotic translation initiation factor 3 subunit 10
eIF-3-theta
eIF3 p167
eIF3 p180
eIF3 p185
p162
Gene names
Name:Eif3a
Synonyms:Csma, Eif3, Eif3s10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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_03000

Subunit structure

Interacts with KRT7 By similarity. 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, EIF3L and EIF3K. 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. Interacts with EIF4G1 and PIWIL2. Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Note: Centrosomin-A is found in the centrosome. Centrosomin-B is found in the nucleus. Ref.3

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation By similarity. HAMAP-Rule MF_03000

Sequence similarities

Belongs to the eIF-3 subunit A family.

Contains 1 PCI domain.

RNA editing

Modified position: not applicable.
Some positions are modified by RNA editing via nucleotide deletion, up to position 787. The unedited version gives rise to centrosomin-B (shown here). The fully edited version gives rise to centrosomin-A, in which the C-terminal sequence is replaced up to position 787 by Ser-Ile-Val-Ala-STOP. A combination of alternative splicing and RNA editing resulting in this template G deletion could also explain the generation of centrosomin-A mRNA. Ref.3

Sequence caution

The sequence CAA35246.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648 and 787.

The sequence CAA59144.1 differs from that shown. Reason: Frameshift at positions 421, 468, 613, 648, 962 and 1059.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 13441343Eukaryotic translation initiation factor 3 subunit A HAMAP-Rule MF_03000
PRO_0000123538

Regions

Domain366 – 494129PCI
Repeat924 – 93181; truncated HAMAP-Rule MF_03000
Repeat932 – 941102 HAMAP-Rule MF_03000
Repeat942 – 951103; approximate HAMAP-Rule MF_03000
Repeat953 – 962104 HAMAP-Rule MF_03000
Repeat963 – 972105 HAMAP-Rule MF_03000
Repeat973 – 982106 HAMAP-Rule MF_03000
Repeat983 – 992107 HAMAP-Rule MF_03000
Repeat993 – 1002108 HAMAP-Rule MF_03000
Repeat1003 – 1012109 HAMAP-Rule MF_03000
Repeat1013 – 10221010 HAMAP-Rule MF_03000
Repeat1023 – 10321011 HAMAP-Rule MF_03000
Repeat1033 – 10421012 HAMAP-Rule MF_03000
Repeat1043 – 10521013 HAMAP-Rule MF_03000
Repeat1054 – 10631014 HAMAP-Rule MF_03000
Repeat1064 – 10731015 HAMAP-Rule MF_03000
Repeat1074 – 10831016 HAMAP-Rule MF_03000
Repeat1084 – 10931017 HAMAP-Rule MF_03000
Repeat1094 – 11031018 HAMAP-Rule MF_03000
Repeat1104 – 11131019 HAMAP-Rule MF_03000
Repeat1114 – 11231020 HAMAP-Rule MF_03000
Repeat1124 – 11331021; approximate HAMAP-Rule MF_03000
Region664 – 835172Interaction with EIF3B By similarity
Region924 – 113321021 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM] HAMAP-Rule MF_03000
Coiled coil82 – 12039 Potential
Compositional bias576 – 875300Glu-rich HAMAP-Rule MF_03000
Compositional bias924 – 1258335Asp-rich HAMAP-Rule MF_03000

Amino acid modifications

Modified residue681N6-acetyllysine By similarity
Modified residue4921Phosphoserine By similarity
Modified residue11591Phosphoserine By similarity
Modified residue13001Phosphoserine By similarity
Modified residue13261Phosphoserine By similarity

Experimental info

Sequence conflict5341L → I in AAA90910. Ref.1
Sequence conflict5341L → I in CAA35246. Ref.3
Sequence conflict5341L → I in CAA59144. Ref.3
Sequence conflict683 – 6842EL → DY in CAA35246. Ref.3
Sequence conflict683 – 6842EL → DY in CAA59144. Ref.3
Sequence conflict7171Q → H in CAA35246. Ref.3
Sequence conflict7171Q → H in CAA59144. Ref.3
Sequence conflict7661A → V in CAA35246. Ref.3
Sequence conflict7661A → V in CAA59144. Ref.3
Sequence conflict7931D → E in AAA90910. Ref.1
Sequence conflict10071G → A in CAA59144. Ref.3
Sequence conflict10561E → D in CAA59144. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P23116 [UniParc].

Last modified July 27, 2011. Version 5.
Checksum: 215F5CCB8A2C7296

FASTA1,344161,936
        10         20         30         40         50         60 
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD 

        70         80         90        100        110        120 
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK TEAAKEESQQ MVLDIEDLDN 

       130        140        150        160        170        180 
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ 

       190        200        210        220        230        240 
AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA 

       250        260        270        280        290        300 
ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY 

       310        320        330        340        350        360 
HLSREMRKNL TQEEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG 

       370        380        390        400        410        420 
LQAPPTRIGL INDMVRFSVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK 

       430        440        450        460        470        480 
EPELQQYVPQ LQNNTILRLL QQVAQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL 

       490        500        510        520        530        540 
QVRIDHTSRT LSFGSDLNYA TREDAPVGPH LQSMPSEQIR NQLTAMSSVL AKALEVIRPA 

       550        560        570        580        590        600 
HILQEKEEQH QLAVNAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE 

       610        620        630        640        650        660 
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED 

       670        680        690        700        710        720 
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRVK 

       730        740        750        760        770        780 
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE 

       790        800        810        820        830        840 
ERLAEERHSR LEDRKRQRKE ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE 

       850        860        870        880        890        900 
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD DPLSRKDSRW GDRDSEGTWR 

       910        920        930        940        950        960 
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL RPDDDRIPRR 

       970        980        990       1000       1010       1020 
GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR IGDDDRGSWR HTDDDRPPRR 

      1030       1040       1050       1060       1070       1080 
GLDDERGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGMDDDRGPR 

      1090       1100       1110       1120       1130       1140 
RGLDDDRGPW RNAAEDRISR RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR 

      1150       1160       1170       1180       1190       1200 
EKEKAREESW GPPRESRPSE EREWDRDKEK DRDNQDREEN DKDLERDRDR ERDGDREDRF 

      1210       1220       1230       1240       1250       1260 
RRPRDEGGWR RGPAEESSSW RDSSRRDDRD REDRRRDRDD RRDLRDLRDR RDLRDDRDRR 

      1270       1280       1290       1300       1310       1320 
GPPLRSEREE ASSWRRTDDR KDDRTEERDP PRRVPPPALS RDRERERERE GEKEKASWRA 

      1330       1340 
EKDRESLRRT KNETDEDGWT TVRR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the 162 kDa component of a multi-protein complex phosphorylated by Src."
Fisher R., Fillmore H., Reynolds A.B.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The centrosomal protein centrosomin A and the nuclear protein centrosomin B derive from one gene by post-transcriptional processes involving RNA editing."
Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.
J. Cell Sci. 110:2573-2578(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 401-1142 (CENTROSOMIN B), SUBCELLULAR LOCATION, RNA EDITING.
Tissue: Ehrlich ascites tumor cell.
[4]"Murine cDNAs coding for the centrosomal antigen centrosomin A."
Joswig G., Petzelt C., Werner D.
J. Cell Sci. 98:37-43(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 514-790 (CENTROSOMIN A).
Tissue: Ehrlich ascites tumor cell.
[5]Joswig G., Petzelt C., Werner D.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[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.
[8]"MILI, a PIWI-interacting RNA-binding protein, is required for germ Line stem cell self-renewal and appears to positively regulate translation."
Unhavaithaya Y., Hao Y., Beyret E., Yin H., Kuramochi-Miyagawa S., Nakano T., Lin H.
J. Biol. Chem. 284:6507-6519(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIWIL2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14172 mRNA. Translation: AAA90910.1.
AC163019 Genomic DNA. No translation available.
X84651 mRNA. Translation: CAA59144.1. Frameshift.
X17373 mRNA. Translation: CAA35246.1. Frameshift.
PIRS13800.
T42637.
RefSeqNP_034253.3. NM_010123.3.
UniGeneMm.2238.
Mm.482533.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199415. 20 interactions.
IntActP23116. 33 interactions.
MINTMINT-1860578.

PTM databases

PhosphoSiteP23116.

Proteomic databases

PaxDbP23116.
PRIDEP23116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
GeneID13669.
KEGGmmu:13669.
UCSCuc008ibx.1. mouse.

Organism-specific databases

CTD8661.
MGIMGI:95301. Eif3a.

Phylogenomic databases

eggNOGNOG236708.
GeneTreeENSGT00730000111063.
HOGENOMHOG000246822.
HOVERGENHBG006128.
InParanoidP23116.
KOK03254.
OMARGPWRNT.
OrthoDBEOG7BGHKJ.
TreeFamTF101522.

Gene expression databases

ArrayExpressP23116.
BgeeP23116.
GenevestigatorP23116.

Family and domain databases

HAMAPMF_03000. eIF3a.
InterProIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PANTHERPTHR14005:SF0. PTHR14005:SF0. 1 hit.
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3A. mouse.
NextBio284428.
PROP23116.
SOURCESearch...

Entry information

Entry nameEIF3A_MOUSE
AccessionPrimary (citable) accession number: P23116
Secondary accession number(s): E9QQ50, Q60697, Q62162
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 122 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

Translation initiation factors

List of translation initiation factor entries