Eef2 eukaryotic translation elongation factor 2 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Eef2provided by RGD
Official Full Name: eukaryotic translation elongation factor 2provided by RGD
Primary source: RGD:61979
See related: Ensembl:ENSRNOG00000020266 AllianceGenome:RGD:61979
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Ef-2
Summary: Enables several functions, including 5S rRNA binding activity; actin filament binding activity; and p53 binding activity. Involved in several processes, including cellular response to brain-derived neurotrophic factor stimulus; positive regulation of cytoplasmic translation; and response to ischemia. Located in cytosol; membrane raft; and polysomal ribosome. Part of ribonucleoprotein complex. Human ortholog(s) of this gene implicated in glaucoma and spinocerebellar ataxia type 26. Orthologous to human EEF2 (eukaryotic translation elongation factor 2). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Spleen (RPKM 4872.9), Thymus (RPKM 4042.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 7q11

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	7	NC_086025.1 (9183836..9196255, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	7	NC_051342.1 (8533248..8538518, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	7	NC_005106.4 (11401501..11406771, complement)

Chromosome 7 - NC_086025.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A reduction in eEF2, an increase in miR-143-5p, and activation of AMPK signaling was observed in degenerative disc degeneration.
Title: MicroRNA-143-5p targeting eEF2 gene mediates intervertebral disc degeneration through the AMPK signaling pathway.
Results show that oxytocin (OXT) recruits several intracellular signaling cascades to induce protein synthesis, which mediates the anxiolytic effects of OXT within the paraventricular nucleus of the hypothalamus and suggests that eukaryotic elongation factor 2 represents a novel target for anxiety-related disorders.
Title: De Novo Protein Synthesis Mediated by the Eukaryotic Elongation Factor 2 Is Required for the Anxiolytic Effect of Oxytocin.
The results suggest that one of the possible mechanisms underlying pineal gland dysfunction during aging is the effect of lipid peroxidation on eEF-2, which is a key component of protein synthesis machinery.
Title: Aging and Oxidative Stress Decrease Pineal Elongation Factor 2: In Vivo Protective Effect of Melatonin in Young Rats Treated With Cumene Hydroperoxide.
Eukaryotic elongation factor 2 kinase activation in M. soleus under 14-day hindlimb unloading of rats
Title: Eukaryotic elongation factor 2 kinase activation in M. soleus under 14-day hindlimb unloading of rats.
Translational inhibition by CORM-2 is a result of eEF2 phosphorylation due to inhibition of PI3K-Akt-mTOR signaling.
Title: Carbon monoxide releasing molecule-2 CORM-2 represses global protein synthesis by inhibition of eukaryotic elongation factor eEF2.
melatonin prevented the molecular changes in eEF-2 and the decline in protein synthesis rate secondary to lipid peroxidation.
Title: In vitro and in vivo protection by melatonin against the decline of elongation factor-2 caused by lipid peroxidation: preservation of protein synthesis.
oxidative stress could be involved in the alterations of eEF-2, which forms adducts with malondialdehyde and 4-hydroxynonenal in the aging hypothalamo-hypophyseal system
Title: Effect of aging and oxidative stress on elongation factor-2 in hypothalamus and hypophysis.
Report interleukin-1beta as the first known activator of endogenous ADP-ribosylation of eEF-2.
Title: Endogenous ADP-ribosylation of elongation factor-2 by interleukin-1β.
results show a causal link between synaptic activity and dendritic spine morphology in rat hippocampal neurons; propose that the eEF2K/eEF2 pathway is a key biochemical sensor that couple neuronal activity to spine plasticity
Title: Synaptic activity controls dendritic spine morphology by modulating eEF2-dependent BDNF synthesis.
A Ca(2+)-calmodulin-eEF2K-eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions.
Title: A Ca(2+)-calmodulin-eEF2K-eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions.

Submit: New GeneRIF Correction See all GeneRIFs (21)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D19S643E (e-PCR)
- UniSTS:150566

RH140185 (e-PCR)
- UniSTS:222264

RH143325 (e-PCR)
- UniSTS:232572

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables 5S rRNA binding	IDA Inferred from Direct Assay more info	PubMed
enables GTP binding	IEA Inferred from Electronic Annotation more info
enables GTPase activity	IBA Inferred from Biological aspect of Ancestor more info
enables GTPase activity	IEA Inferred from Electronic Annotation more info
enables GTPase activity	ISO Inferred from Sequence Orthology more info
enables GTPase activity	ISS Inferred from Sequence or Structural Similarity more info
enables RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables actin filament binding	IDA Inferred from Direct Assay more info	PubMed
enables p53 binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IEA Inferred from Electronic Annotation more info
enables protein kinase binding	ISO Inferred from Sequence Orthology more info
enables ribosome binding	IBA Inferred from Biological aspect of Ancestor more info
enables ribosome binding	IDA Inferred from Direct Assay more info	PubMed
enables ribosome binding	IEA Inferred from Electronic Annotation more info
enables ribosome binding	ISO Inferred from Sequence Orthology more info
enables translation elongation factor activity	IBA Inferred from Biological aspect of Ancestor more info
enables translation elongation factor activity	IEA Inferred from Electronic Annotation more info
enables translation elongation factor activity	ISO Inferred from Sequence Orthology more info
enables translation elongation factor activity	ISS Inferred from Sequence or Structural Similarity more info
enables translation elongation factor activity	TAS Traceable Author Statement more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to brain-derived neurotrophic factor stimulus	IEP Inferred from Expression Pattern more info	PubMed
involved_in glial cell proliferation	IEP Inferred from Expression Pattern more info	PubMed
involved_in hematopoietic progenitor cell differentiation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within hematopoietic progenitor cell differentiation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cytoplasmic translation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of translation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of translation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of translation	ISO Inferred from Sequence Orthology more info
involved_in response to endoplasmic reticulum stress	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to estradiol	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to ethanol	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to folic acid	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to hydrogen peroxide	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to ischemia	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to xenobiotic stimulus	IEP Inferred from Expression Pattern more info	PubMed
involved_in skeletal muscle cell differentiation	IEP Inferred from Expression Pattern more info	PubMed
involved_in skeletal muscle contraction	IEP Inferred from Expression Pattern more info	PubMed
involved_in translation	IEA Inferred from Electronic Annotation more info
involved_in translation at postsynapse	IDA Inferred from Direct Assay more info	PubMed
involved_in translation at postsynapse	IEP Inferred from Expression Pattern more info	PubMed
involved_in translational elongation	IBA Inferred from Biological aspect of Ancestor more info
involved_in translational elongation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within translational elongation	ISO Inferred from Sequence Orthology more info
involved_in translational elongation	ISO Inferred from Sequence Orthology more info
involved_in translational elongation	ISS Inferred from Sequence or Structural Similarity more info
involved_in translational elongation	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in aggresome	IEA Inferred from Electronic Annotation more info
located_in aggresome	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
NOT located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in postsynapse	IEA Inferred from Electronic Annotation more info
part_of ribonucleoprotein complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonucleoprotein complex	IDA Inferred from Direct Assay more info	PubMed
part_of ribonucleoprotein complex	IEA Inferred from Electronic Annotation more info
part_of ribonucleoprotein complex	ISO Inferred from Sequence Orthology more info
located_in ribosome	IDA Inferred from Direct Assay more info	PubMed
located_in ribosome	IEA Inferred from Electronic Annotation more info
located_in ribosome	ISO Inferred from Sequence Orthology more info
located_in synapse	IEA Inferred from Electronic Annotation more info
is_active_in synapse	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: elongation factor 2

NP_058941.1

EC 3.6.5.-

XP_063119189.1

EC 3.6.5.-

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.