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Protein

Eukaryotic translation initiation factor 3 subunit A

Gene

Eif3a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

RNA-binding 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 pre-initiation 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. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.UniRule annotation

GO - Molecular functioni

  • mRNA binding Source: GO_Central
  • receptor tyrosine kinase binding Source: RGD
  • translation initiation factor activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit AUniRule annotation
Short name:
eIF3aUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 10UniRule annotation
eIF-3-thetaUniRule annotation
Gene namesi
Name:Eif3a
Synonyms:Eif3s10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1307269. Eif3a.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003663272 – 1354Eukaryotic translation initiation factor 3 subunit AAdd BLAST1353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68N6-acetyllysineBy similarity1
Modified residuei492PhosphoserineUniRule annotationBy similarity1
Modified residuei584PhosphoserineBy similarity1
Modified residuei895PhosphoserineBy similarity1
Modified residuei949PhosphoserineBy similarity1
Modified residuei1038PhosphoserineBy similarity1
Modified residuei1159PhosphoserineBy similarity1
Modified residuei1233PhosphoserineBy similarity1
Modified residuei1310PhosphoserineUniRule annotationBy similarity1
Modified residuei1336PhosphoserineUniRule annotationBy similarity1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ1JU68.
PRIDEiQ1JU68.

PTM databases

iPTMnetiQ1JU68.
PhosphoSitePlusiQ1JU68.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010117.
GenevisibleiQ1JU68. RN.

Interactioni

Subunit structurei

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 interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads 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. Also interacts with KRT7 and PIWIL2.UniRule annotation

GO - Molecular functioni

  • receptor tyrosine kinase binding Source: RGD

Protein-protein interaction databases

BioGridi253779. 1 interactor.
IntActiQ1JU68. 1 interactor.
STRINGi10116.ENSRNOP00000063484.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini366 – 494PCIUniRule annotationAdd BLAST129
Repeati924 – 9311; truncated8
Repeati932 – 941210
Repeati942 – 9513; approximate10
Repeati953 – 962410
Repeati963 – 972510
Repeati973 – 982610
Repeati983 – 992710
Repeati993 – 1002810
Repeati1003 – 1012910
Repeati1013 – 10221010
Repeati1023 – 10321110
Repeati1033 – 10421210
Repeati1043 – 10521310
Repeati1053 – 10621410
Repeati1064 – 10731510
Repeati1074 – 10831610
Repeati1084 – 10931710
Repeati1094 – 11031810
Repeati1104 – 11131910
Repeati1114 – 11232010
Repeati1124 – 11332110
Repeati1134 – 114322; approximate10

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni664 – 835Interaction with EIF3BUniRule annotationAdd BLAST172
Regioni924 – 114322 X 10 AA approximate tandem repeats of [DA]-[DE]-[ED]-R-[PLIGFSV]-[RPS]-[RW]-[RL]-[GNIHT]-[DGLPTAM]Add BLAST220

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili82 – 120UniRule annotationAdd BLAST39

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi576 – 880Glu-richAdd BLAST305
Compositional biasi924 – 1268Asp-richAdd BLAST345

Sequence similaritiesi

Belongs to the eIF-3 subunit A family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiQ1JU68.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
PhylomeDBiQ1JU68.
TreeFamiTF101522.

Family and domain databases

HAMAPiMF_03000. eIF3a. 1 hit.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PANTHERiPTHR14005:SF0. PTHR14005:SF0. 1 hit.
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q1JU68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI
60 70 80 90 100
MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKLAEEK
110 120 130 140 150
TEAAKEESQQ MVLDIEDLDN IQTPESVLLS AVSGEDTQDR TDRLLLTPWV
160 170 180 190 200
KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ AFKFCLQYTR KAEFRKLCDN
210 220 230 240 250
LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA ISMELWQEAF
260 270 280 290 300
KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
310 320 330 340 350
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE
360 370 380 390 400
KQRRLATLLG LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP
410 420 430 440 450
LKLCERVTKV LNWVREQPEK EPELQQYVPQ LQNNTILRLL QQVAQIYQSI
460 470 480 490 500
EFSRLTSLVP FVDAFQLERA IVDAARHCDL QVRIDHTSRT LSFGSDLNYA
510 520 530 540 550
TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA HILQEKEEQH
560 570 580 590 600
QLAVTAYIKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
610 620 630 640 650
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA
660 670 680 690 700
KAFKDIDIED LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER
710 720 730 740 750
AKRLEEIPLI KSAYEEQRVK DMDLWEQQEE ERITTMQLER EKALEHKNRM
760 770 780 790 800
SRMLEDRDLF VMRLKAARQS VYEEKLKQFE ERLAEERHNR LEERKRQRKE
810 820 830 840 850
ERKITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK
860 870 880 890 900
LEEVERKKRQ RELEIEERER RREEERRLGE DPLSRKDSRW GDRDSEGTWR
910 920 930 940 950
KGPEADSEWR RGPPEKEWRR ETRDDERPHR RDEDRLRRLG GDDEERESSL
960 970 980 990 1000
RPDDDRIPRR GLDDDRGPRR GPDEDRFSRR GTDDDRPSWR NADDDRPPRR
1010 1020 1030 1040 1050
IGDDDRGSWR HTDDDRPPRR GLDDDRPPRR GLDDERGSWR TAEEDRGPRR
1060 1070 1080 1090 1100
GMDDDRGPRR GGADDERSSW RNADDDRGPR RGMDDDRGPR RGLDDDRGPW
1110 1120 1130 1140 1150
RNAAEDRISR RGADDDRGPW RNMDDDRVPR RGDDARPGPW RPFVKPGGWR
1160 1170 1180 1190 1200
EKEKAREESW GPPRESRPPE EREWDRDKEK DRDNQDREEN DKDLERDRDR
1210 1220 1230 1240 1250
ERDGDREDRF RRPRDEGGWR RGPAEESSSW RDSSRRDDRD RDDRRRDRDD
1260 1270 1280 1290 1300
RRDLRDLRDR RDLRDDRDRR GPPLRSEREE ASSWRRTDDR KDDRTEERDP
1310 1320 1330 1340 1350
PRRVPPPTLS RERERERDRE GEKEKASWRA EKDRESLRRT KNETDEDGWT

TVRR
Length:1,354
Mass (Da):163,196
Last modified:March 24, 2009 - v2
Checksum:i3ED50215624CFC07
GO

Sequence cautioni

The sequence BAE94261 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CB586480 mRNA. No translation available.
AB259154 mRNA. Translation: BAE94261.1. Different initiation.
RefSeqiNP_001040552.2. NM_001047087.2.
UniGeneiRn.1644.

Genome annotation databases

EnsembliENSRNOT00000066947; ENSRNOP00000063484; ENSRNOG00000010117.
GeneIDi292148.
KEGGirno:292148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CB586480 mRNA. No translation available.
AB259154 mRNA. Translation: BAE94261.1. Different initiation.
RefSeqiNP_001040552.2. NM_001047087.2.
UniGeneiRn.1644.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253779. 1 interactor.
IntActiQ1JU68. 1 interactor.
STRINGi10116.ENSRNOP00000063484.

PTM databases

iPTMnetiQ1JU68.
PhosphoSitePlusiQ1JU68.

Proteomic databases

PaxDbiQ1JU68.
PRIDEiQ1JU68.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000066947; ENSRNOP00000063484; ENSRNOG00000010117.
GeneIDi292148.
KEGGirno:292148.

Organism-specific databases

CTDi8661.
RGDi1307269. Eif3a.

Phylogenomic databases

eggNOGiKOG2072. Eukaryota.
ENOG410XQ37. LUCA.
GeneTreeiENSGT00730000111063.
HOGENOMiHOG000246822.
HOVERGENiHBG006128.
InParanoidiQ1JU68.
KOiK03254.
OMAiAREDSWG.
OrthoDBiEOG091G01VW.
PhylomeDBiQ1JU68.
TreeFamiTF101522.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ1JU68.

Gene expression databases

BgeeiENSRNOG00000010117.
GenevisibleiQ1JU68. RN.

Family and domain databases

HAMAPiMF_03000. eIF3a. 1 hit.
InterProiIPR027512. EIF3A.
IPR000717. PCI_dom.
[Graphical view]
PANTHERiPTHR14005:SF0. PTHR14005:SF0. 1 hit.
PfamiPF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3A_RAT
AccessioniPrimary (citable) accession number: Q1JU68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. 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.