Eukaryotic translation initiation factor 3 subunit A

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P23116 (EIF3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › centrosome. 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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	RNA editing
Domain	Coiled coil Repeat
Molecular function	Initiation factor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	formation of translation initiation complex Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.7. Source: UniProtKB microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara
Molecular_function	translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 1344

1343

Eukaryotic translation initiation factor 3 subunit A HAMAP-Rule MF_03000

PRO_0000123538

Regions

Domain

366 – 494

129

PCI

Repeat

924 – 931

1; truncated HAMAP-Rule MF_03000

Repeat

932 – 941

2 HAMAP-Rule MF_03000

Repeat

942 – 951

3; approximate HAMAP-Rule MF_03000

Repeat

953 – 962

4 HAMAP-Rule MF_03000

Repeat

963 – 972

5 HAMAP-Rule MF_03000

Repeat

973 – 982

6 HAMAP-Rule MF_03000

Repeat

983 – 992

7 HAMAP-Rule MF_03000

Repeat

993 – 1002

8 HAMAP-Rule MF_03000

Repeat

1003 – 1012

9 HAMAP-Rule MF_03000

Repeat

1013 – 1022

10 HAMAP-Rule MF_03000

Repeat

1023 – 1032

11 HAMAP-Rule MF_03000

Repeat

1033 – 1042

12 HAMAP-Rule MF_03000

Repeat

1043 – 1052

13 HAMAP-Rule MF_03000

Repeat

1054 – 1063

14 HAMAP-Rule MF_03000

Repeat

1064 – 1073

15 HAMAP-Rule MF_03000

Repeat

1074 – 1083

16 HAMAP-Rule MF_03000

Repeat

1084 – 1093

17 HAMAP-Rule MF_03000

Repeat

1094 – 1103

18 HAMAP-Rule MF_03000

Repeat

1104 – 1113

19 HAMAP-Rule MF_03000

Repeat

1114 – 1123

20 HAMAP-Rule MF_03000

Repeat

1124 – 1133

21; approximate HAMAP-Rule MF_03000

Region

664 – 835

172

Interaction with EIF3B By similarity

Region

924 – 1133

210

21 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM] HAMAP-Rule MF_03000

Coiled coil

82 – 120

Potential

Compositional bias

576 – 875

300

Glu-rich HAMAP-Rule MF_03000

Compositional bias

924 – 1258

335

Asp-rich HAMAP-Rule MF_03000

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

492

Phosphoserine By similarity

Modified residue

1159

Phosphoserine By similarity

Modified residue

1300

Phosphoserine By similarity

Modified residue

1326

Phosphoserine By similarity

Experimental info

Sequence conflict

534

L → I in AAA90910. Ref.1

Sequence conflict

534

L → I in CAA35246. Ref.3

Sequence conflict

534

L → I in CAA59144. Ref.3

Sequence conflict

683 – 684

EL → DY in CAA35246. Ref.3

Sequence conflict

683 – 684

EL → DY in CAA59144. Ref.3

Sequence conflict

717

Q → H in CAA35246. Ref.3

Sequence conflict

717

Q → H in CAA59144. Ref.3

Sequence conflict

766

A → V in CAA35246. Ref.3

Sequence conflict

766

A → V in CAA59144. Ref.3

Sequence conflict

793

D → E in AAA90910. Ref.1

Sequence conflict

1007

G → A in CAA59144. Ref.3

Sequence conflict

1056

E → D in CAA59144. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P23116 [UniParc].

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

FASTA

1,344

161,936

        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' referencesShow '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. 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.
IPI	IPI00129276.
PIR	S13800. T42637.
RefSeq	NP_034253.3. NM_010123.3.
UniGene	Mm.2238. Mm.482533.
3D structure databases
ProteinModelPortal	P23116.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23116. 18 interactions.
MINT	MINT-1860578.
PTM databases
PhosphoSite	P23116.
Proteomic databases
PaxDb	P23116.
PRIDE	P23116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025955; ENSMUSP00000025955; ENSMUSG00000024991.
GeneID	13669.
KEGG	mmu:13669.
UCSC	uc008ibx.1. mouse.
Organism-specific databases
CTD	8661.
MGI	MGI:95301. Eif3a.
Phylogenomic databases
eggNOG	NOG236708.
GeneTree	ENSGT00690000102108.
HOGENOM	HOG000246822.
HOVERGEN	HBG006128.
InParanoid	P23116.
KO	K03254.
OMA	QDRDEND.
OrthoDB	EOG4B2SWM.
Gene expression databases
ArrayExpress	P23116.
Bgee	P23116.
Genevestigator	P23116.
GermOnline	ENSMUSG00000024991. Mus musculus.
Family and domain databases
HAMAP	MF_03000. eIF3a.
InterPro	IPR000717. PCI_dom. [Graphical view]
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF3A. mouse.
NextBio	284428.
SOURCE	Search...

Entry information

Entry name

EIF3A_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents