Hspe1 heat shock protein family E (Hsp10) member 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Hspe1provided by RGD
Official Full Name: heat shock protein family E (Hsp10) member 1provided by RGD
Primary source: RGD:2844
See related: AllianceGenome:RGD:2844
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
Also known as: Cpn10
Summary: Predicted to enable chaperone binding activity; metal ion binding activity; and unfolded protein binding activity. Predicted to be involved in chaperone cofactor-dependent protein refolding. Located in mitochondrial matrix. Orthologous to human HSPE1 (heat shock protein family E (Hsp10) member 1). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Adrenal (RPKM 5302.4), Kidney (RPKM 1192.0) and 7 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 9q31

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	9	NC_086027.1 (64084327..64087415)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	9	NC_051344.1 (56589912..56593000)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	9	NC_005108.4 (61691246..61724948)

Chromosome 9 - NC_086027.1 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?

Data show that Rhsp10 formed fibrils from only the acidic unfolded state and Core peptide regions of these protein fibrils were determined by proteolysis followed by a combination of Edman degradation and mass spectroscopy analyses.
Title: Fibril formation of hsp10 homologue proteins and determination of fibril core regions: differences in fibril core regions dependent on subtle differences in amino acid sequence.
Hsp10 and Hsp60 suppress ubiquitination of igf-1 receptor and augment igf-1 receptor signaling in cardiac muscle
Title: Hsp10 and Hsp60 suppress ubiquitination of insulin-like growth factor-1 receptor and augment insulin-like growth factor-1 receptor signaling in cardiac muscle: implications on decreased myocardial protection in diabetic cardiomyopathy.
Cpn10 modulates Bcl-2 family and mitochondrial apoptosis signaling induced by doxorubiicin in cardiac myocytes.
Title: Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells.
Data describe the structural stabilities of chaperonin 10 from rat mitochondria and from hyperthermophilic eubacteria Thermotoga maritima, and compare the values to those of Escherichia coli GroES.
Title: Structural stability of oligomeric chaperonin 10: the role of two beta-strands at the N and C termini in structural stabilization.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	ISS Inferred from Sequence or Structural Similarity more info
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in mitochondrial inner membrane	ISO Inferred from Sequence Orthology more info
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	ISS Inferred from Sequence or Structural Similarity more info
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: 10 kDa heat shock protein, mitochondrial

Names: 10 kDa chaperonin; Heat shock 10 kD protein 1 (chaperonin 10); chaperonin 10; heat shock 10 kDa protein 1 (chaperonin 10); heat shock protein 1 (chaperonin 10); heat shock protein family E member 1; hsp10

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_012966.1 → NP_037098.1 10 kDa heat shock protein, mitochondrial

See identical proteins and their annotated locations for NP_037098.1

Status: PROVISIONAL

Source sequence(s)

U68562

UniProtKB/TrEMBL

A0A0G2JTG1, P97601

Conserved Domains (1) summary

cd00320
Location:8 → 100

cpn10; Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It ...