Eif2b5 eukaryotic translation initiation factor 2B subunit epsilon [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Eif2b5provided by RGD
Official Full Name: eukaryotic translation initiation factor 2B subunit epsilonprovided by RGD
Primary source: RGD:708380
See related: Ensembl:ENSRNOG00000038160 AllianceGenome:RGD:708380
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Enables translation initiation factor binding activity. Contributes to guanyl-nucleotide exchange factor activity. Involved in several processes, including hippocampus development; response to glucose; and response to lithium ion. Part of eukaryotic translation initiation factor 2B complex. Human ortholog(s) of this gene implicated in leukoencephalopathy with vanishing white matter. Orthologous to human EIF2B5 (eukaryotic translation initiation factor 2B subunit epsilon). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Thymus (RPKM 211.7), Muscle (RPKM 176.8) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 11q23

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	11	NC_086029.1 (93898814..93909431, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	11	NC_051346.1 (80394433..80404468, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	11	NC_005110.4 (84080273..84090259, complement)

Chromosome 11 - NC_086029.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

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?

modulation of eIF2Bepsilon expression may be sufficient to correct deficits in skeletal muscle protein synthesis associated with sepsis and other muscle-wasting conditions
Title: Ectopic expression of eIF2Bepsilon in rat skeletal muscle rescues the sepsis-induced reduction in guanine nucleotide exchange activity and protein synthesis.
oligodendroglial-derived cells expressing a mutated eIF2B5 constantly use their stress response mechanism as an adaptation mean in order to survive
Title: A point mutation in translation initiation factor 2B leads to a continuous hyper stress state in oligodendroglial-derived cells.
Data show that activation of mTORC1 is necessary and sufficient to stimulate eIF2Bepsilon mRNA translation.
Title: Activation of the mammalian target of rapamycin complex 1 is both necessary and sufficient to stimulate eukaryotic initiation factor 2Bvarepsilon mRNA translation and protein synthesis.
mTOR signaling and eIF2Bepsilon mRNA translation are linked and could have roles in the stimulation of protein synthesis following acute resistance exercise
Title: Resistance exercise increases muscle protein synthesis and translation of eukaryotic initiation factor 2Bepsilon mRNA in a mammalian target of rapamycin-dependent manner.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI716564 (e-PCR)
- UniSTS:246541

AW528025 (e-PCR)
- UniSTS:260763

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables guanyl-nucleotide exchange factor activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to guanyl-nucleotide exchange factor activity	IDA Inferred from Direct Assay more info	PubMed
enables guanyl-nucleotide exchange factor activity	IDA Inferred from Direct Assay more info	PubMed
enables guanyl-nucleotide exchange factor activity	IMP Inferred from Mutant Phenotype more info	PubMed
contributes_to guanyl-nucleotide exchange factor activity	ISO Inferred from Sequence Orthology more info
enables guanyl-nucleotide exchange factor activity	ISO Inferred from Sequence Orthology more info
contributes_to guanyl-nucleotide exchange factor activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables translation initiation factor activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to translation initiation factor activity	ISO Inferred from Sequence Orthology more info
contributes_to translation initiation factor activity	ISS Inferred from Sequence or Structural Similarity more info
enables translation initiation factor binding	IBA Inferred from Biological aspect of Ancestor more info
enables translation initiation factor binding	IDA Inferred from Direct Assay more info	PubMed
enables translation initiation factor binding	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in T cell receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in T cell receptor signaling pathway	ISS Inferred from Sequence or Structural Similarity more info
involved_in astrocyte development	ISO Inferred from Sequence Orthology more info
involved_in astrocyte development	ISS Inferred from Sequence or Structural Similarity more info
involved_in astrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in astrocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in cytoplasmic translational initiation	ISO Inferred from Sequence Orthology more info
involved_in cytoplasmic translational initiation	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in hippocampus development	IEP Inferred from Expression Pattern more info	PubMed
involved_in myelination	ISO Inferred from Sequence Orthology more info
involved_in myelination	ISS Inferred from Sequence or Structural Similarity more info
involved_in oligodendrocyte development	ISO Inferred from Sequence Orthology more info
involved_in oligodendrocyte development	ISS Inferred from Sequence or Structural Similarity more info
involved_in ovarian follicle development	ISO Inferred from Sequence Orthology more info
involved_in ovarian follicle development	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of apoptotic process	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 translational initiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to endoplasmic reticulum stress	ISO Inferred from Sequence Orthology more info
involved_in response to endoplasmic reticulum stress	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to glucose	IDA Inferred from Direct Assay more info	PubMed
involved_in response to heat	IDA Inferred from Direct Assay more info	PubMed
involved_in response to heat	ISO Inferred from Sequence Orthology more info
involved_in response to heat	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to peptide hormone	IDA Inferred from Direct Assay more info	PubMed
involved_in translational initiation	ISO Inferred from Sequence Orthology more info
involved_in translational initiation	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
part_of eukaryotic translation initiation factor 2B complex	IBA Inferred from Biological aspect of Ancestor more info
part_of eukaryotic translation initiation factor 2B complex	IDA Inferred from Direct Assay more info	PubMed
part_of eukaryotic translation initiation factor 2B complex	ISO Inferred from Sequence Orthology more info
part_of eukaryotic translation initiation factor 2B complex	ISS Inferred from Sequence or Structural Similarity more info
NOT located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: translation initiation factor eIF2B subunit epsilon

Names: eIF-2B GDP-GTP exchange factor subunit epsilon; eIF2B GDP-GTP exchange factor subunit epsilon; eukaryotic translation initiation factor 2B subunit 5 epsilon; initiation factor eIF-2Be; translation initiation factor eIF-2B subunit epsilon

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.

mRNA and Protein(s)

NM_138866.2 → NP_620221.2 translation initiation factor eIF2B subunit epsilon

See identical proteins and their annotated locations for NP_620221.2

Status: PROVISIONAL

Source sequence(s)

BC085698

UniProtKB/Swiss-Prot

Q5RKL3, Q64350

UniProtKB/TrEMBL

A6JSB3

Related

ENSRNOP00000002321.2, ENSRNOT00000002321.4

Conserved Domains (4) summary

cd05787
Location:356 → 434

LbH_eIF2B_epsilon; eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is ...

cd04197
Location:38 → 252

eIF-2B_epsilon_N; The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2

cd11558
Location:543 → 713

W2_eIF2B_epsilon; C-terminal W2 domain of eukaryotic translation initiation factor 2B epsilon

COG1208
Location:37 → 433

GCD1; NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis proteins [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis]

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086029.1 Reference GRCr8

Range

93898814..93909431 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_039087951.2 → XP_038943879.1 translation initiation factor eIF2B subunit epsilon isoform X1

Conserved Domains (3) summary

cd04197
Location:38 → 252

eIF-2B_epsilon_N; The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2

COG1044
Location:295 → 381

LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]

cl00160
Location:356 → 381

LbetaH; Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes ...
XM_039087952.2 → XP_038943880.1 translation initiation factor eIF2B subunit epsilon isoform X2

Conserved Domains (3) summary

cd04197
Location:38 → 252

eIF-2B_epsilon_N; The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2

COG1044
Location:295 → 383

LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]

cl00160
Location:356 → 386

LbetaH; Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes ...