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Protein

Eukaryotic translation initiation factor 3 subunit C

Gene

Eif3c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

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 CUniRule annotation
Short name:
eIF3cUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 8UniRule annotation
eIF3 p110UniRule annotation
Gene namesi
Name:Eif3c
Synonyms:Eif3s8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1308871. Eif3c.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Eukaryotic translation initiation factor 3 subunit CPRO_0000365376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineUniRule annotationBy similarity
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei13 – 131PhosphoserineUniRule annotationBy similarity
Modified residuei15 – 151PhosphoserineUniRule annotationBy similarity
Modified residuei16 – 161PhosphoserineUniRule annotationBy similarity
Modified residuei18 – 181PhosphoserineCombined sources
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei166 – 1661PhosphoserineCombined sources
Modified residuei178 – 1781PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineCombined sources
Modified residuei182 – 1821PhosphoserineCombined sources
Modified residuei522 – 5221PhosphothreonineUniRule annotationBy similarity
Modified residuei641 – 6411N6-acetyllysineBy similarity
Modified residuei907 – 9071PhosphoserineUniRule annotationBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiB5DFC8.
PeptideAtlasiB5DFC8.
PRIDEiB5DFC8.

PTM databases

iPTMnetiB5DFC8.
PhosphoSiteiB5DFC8.

Expressioni

Gene expression databases

GenevisibleiB5DFC8. 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, 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 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 (By similarity). Interacts with ALKBH4, IFIT1 and IFIT2 (By similarity).UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025782.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini710 – 844135PCIUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1076. Eukaryota.
ENOG410XRU3. LUCA.
GeneTreeiENSGT00390000017900.
HOGENOMiHOG000029414.
HOVERGENiHBG035174.
InParanoidiB5DFC8.
KOiK03252.
OMAiTEEICQI.
OrthoDBiEOG7DC23R.
PhylomeDBiB5DFC8.
TreeFamiTF101520.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03002. eIF3c.
InterProiIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05470. eIF-3c_N. 2 hits.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

B5DFC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRFFTTGSD SESESSLSGE ELVTKPVSGN YGKQPLLLSE DEEDTKRVVR
60 70 80 90 100
SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE
110 120 130 140 150
GVPRFYVRIL ADLEDYLNEL WEDKEGKKKM NKNNAKALST LRQKIRKYNR
160 170 180 190 200
DFESHITNYK QNPEQSADED AEKNEEDSEG SSDEDEDDDG VSGTAFLKKK
210 220 230 240 250
PDSSGESRKF HKKMEDDDED SEDSEDEEWD TSSTSSDSDS EEEEGKQTVL
260 270 280 290 300
ASKFLKKAPT TEEDKKAAEK KREDKAKKKH DRKSKRMDEE EEDNEGGEWE
310 320 330 340 350
RVRGGVPLVK EKPKMFAKGT EITHAVVIKK LNEILQVRGK KGTDRATQIE
360 370 380 390 400
LLQLLVQIAS ENNLGVGVIV KIKFNIIASL YDYNPNLATY MKPEMWQMCL
410 420 430 440 450
DCINELMDTL VAHSNIFVGE NILEESENLH NFDQPLRVRG CILTLVERMD
460 470 480 490 500
EEFTKIMQNT DPHSQEYVEH LKDEAQVCAI IERVQRYLEE KGTTEEICQI
510 520 530 540 550
YLRRILHTYY KFDYKAHQRQ LTPPEGSSKS EQDQAENEGE DSAVLMERLC
560 570 580 590 600
KYIYAKDRTD RIRTCAILCH IYHHALHSRW YQARDLMLMS HLQDNIQHAD
610 620 630 640 650
PPVQILYNRT MVQLGICAFR QGLTKDAHNA LLDIQSSGRA KELLGQGLLL
660 670 680 690 700
RSLQERNQEQ EKVERRRQVP FHLHINLELL ECVYLVSAML LEIPYMAAHE
710 720 730 740 750
SDARRRMISK QFHHQLRVGE RQPLLGPPES MREHVVAASK AMKMGDWKTC
760 770 780 790 800
HSFIINEKMN GKVWDLFPEA DKVRTMLVRK IQEESLRTYL FTYSSVYDSI
810 820 830 840 850
SMETLSDMFE LDLPTVHSII SKMIINEELM ASLDQPTQTV VMHRTEPTAQ
860 870 880 890 900
QNLALQLAEK LGSLVENNER VFDHKQGTYG GYFRDQKDGY RKNEGYMRRG
910
GYRQQQSQTA Y
Length:911
Mass (Da):105,435
Last modified:October 14, 2008 - v1
Checksum:i0935A6A8BFE1D2D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103728 mRNA. Translation: AAI03729.1.
BC169011 mRNA. Translation: AAI69011.1.
RefSeqiNP_001094132.1. NM_001100662.1.
XP_006230288.1. XM_006230226.2.
UniGeneiRn.4207.

Genome annotation databases

EnsembliENSRNOT00000025782; ENSRNOP00000025782; ENSRNOG00000018761.
GeneIDi293484.
KEGGirno:293484.
UCSCiRGD:1308871. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103728 mRNA. Translation: AAI03729.1.
BC169011 mRNA. Translation: AAI69011.1.
RefSeqiNP_001094132.1. NM_001100662.1.
XP_006230288.1. XM_006230226.2.
UniGeneiRn.4207.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025782.

PTM databases

iPTMnetiB5DFC8.
PhosphoSiteiB5DFC8.

Proteomic databases

PaxDbiB5DFC8.
PeptideAtlasiB5DFC8.
PRIDEiB5DFC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025782; ENSRNOP00000025782; ENSRNOG00000018761.
GeneIDi293484.
KEGGirno:293484.
UCSCiRGD:1308871. rat.

Organism-specific databases

CTDi8663.
RGDi1308871. Eif3c.

Phylogenomic databases

eggNOGiKOG1076. Eukaryota.
ENOG410XRU3. LUCA.
GeneTreeiENSGT00390000017900.
HOGENOMiHOG000029414.
HOVERGENiHBG035174.
InParanoidiB5DFC8.
KOiK03252.
OMAiTEEICQI.
OrthoDBiEOG7DC23R.
PhylomeDBiB5DFC8.
TreeFamiTF101520.

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

PROiB5DFC8.

Gene expression databases

GenevisibleiB5DFC8. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03002. eIF3c.
InterProiIPR027516. EIF3C.
IPR008905. EIF3C_N_dom.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05470. eIF-3c_N. 2 hits.
PF01399. PCI. 1 hit.
[Graphical view]
SMARTiSM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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].
    Tissue: Embryo and Thymus.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-18; SER-39; SER-166; SER-178; SER-181 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEIF3C_RAT
AccessioniPrimary (citable) accession number: B5DFC8
Secondary accession number(s): Q3MIB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 14, 2008
Last modified: July 6, 2016
This is version 64 of the entry and version 1 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.