Hspa9 heat shock protein family A (Hsp70) member 9 [Rattus norvegicus (Norway rat)] - Gene

Summary

Symbol: Hspa9provided by RGD
Full Name: heat shock protein family A (Hsp70) member 9provided by RGD
Primary source: RGD:1311806
See related: EnsemblRapid:ENSRNOG00000019525 AllianceGenome:RGD:1311806
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: Crp40; PBP74; GRP-75; Hspa9a
Summary: Enables fibroblast growth factor binding activity; heat shock protein binding activity; and protein-folding chaperone binding activity. Involved in several processes, including calcium import into the mitochondrion; cellular response to interleukin-1; and response to thyroxine. Located in mitochondrial matrix. Biomarker of Parkinsonism and brain ischemia. Human ortholog(s) of this gene implicated in Parkinson's disease and autosomal dominant sideroblastic anemia 4. Orthologous to human HSPA9 (heat shock protein family A (Hsp70) member 9). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Heart (RPKM 1892.8), Adrenal (RPKM 1730.9) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 18p12

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	18	NC_086036.1 (26810004..26832958, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	18	NC_051353.1 (26536131..26554294, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	18	NC_005117.4 (27731072..27749235, complement)

Chromosome 18 - NC_086036.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Potential targets for the treatment of MI: GRP75-mediated Ca[2+] transfer in MAM.
Title: Potential targets for the treatment of MI: GRP75-mediated Ca(2+) transfer in MAM.
HSPA9/Mortalin mediates axo-protection and modulates mitochondrial dynamics in neurons.
Title: HSPA9/Mortalin mediates axo-protection and modulates mitochondrial dynamics in neurons.
GRP75 expression is significantly decreased in brain tissues following ICH, and that overexpression of GRP75 inhibits inflammation and neuronal apoptosis in a rat model of ICH.
Title: Overexpression of GRP75 inhibits inflammation in a rat model of intracerebral hemorrhage.
GRP75 was significantly upregulated in the retina after optic nerve crush.
Title: GRP75 Involves in Retinal Ganglion Cell Apoptosis After Rat Optic Nerve Crush.
expression of catecholamine-regulated protein 40 (CRP40) in the retina decreases in a time-dependent fashion after optic nerve transection and indicates an important function for CRP40 in physiological and pathological conditions in the retina.
Title: Expression of the 40 kDa catecholamine regulated protein in the normal and injured rat retina.
Studied polyubiquitinated proteins during inflammatory response in intestinal epithelial cells; found Grp75 and Grp78 differentially ubiquitinated between control and inflammation; results confirmed in HCT-8 cells and in TNBS induced colitis in rats.
Title: Evaluation of ubiquitinated proteins by proteomics reveals the role of the ubiquitin proteasome system in the regulation of Grp75 and Grp78 chaperone proteins during intestinal inflammation.
AKT and extracellular signal-regulated protein kinases 1 and 2 activated by Grp75 inhibited the Bax conformational change and subsequent apoptosis.
Title: Crosstalk between Raf/MEK/ERK and PI3K/AKT in suppression of Bax conformational change by Grp75 under glucose deprivation conditions.
Induction of GRP-75 phosphorylation suggests that it may play a role in the protection of cytoplasmic proteins from the damaging effect of oxidative stress known to be produced during Ang-II induced signaling.[GRP-75]
Title: Angiotensin II induces phosphorylation of glucose-regulated protein-75 in WB rat liver cells.
mortalin plays an essential role in the regulation of dopamine-dependent behavior and plays an even greater role in the pathogenesis of schizophrenia
Title: Knockdown of mortalin within the medial prefrontal cortex impairs normal sensorimotor gating.

Submit: New GeneRIF Correction

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH139216 (e-PCR)
- UniSTS:221302

d18rat101 (e-PCR)
- UniSTS:121281

BE120145 (e-PCR)
- UniSTS:247252

D18Chm4 (e-PCR)
- UniSTS:518365

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables fibroblast growth factor binding	IPI Inferred from Physical Interaction more info	PubMed
enables heat shock protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables heat shock protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein folding chaperone	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables ubiquitin protein ligase binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in calcium import into the mitochondrion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cellular response to interleukin-1	IEP Inferred from Expression Pattern more info	PubMed
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in erythrocyte differentiation	IEA Inferred from Electronic Annotation more info
involved_in erythrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in erythrocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in iron-sulfur cluster assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in iron-sulfur cluster assembly	IEA Inferred from Electronic Annotation more info
involved_in iron-sulfur cluster assembly	ISO Inferred from Sequence Orthology more info
involved_in iron-sulfur cluster assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of erythrocyte differentiation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of erythrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of erythrocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of hematopoietic stem cell differentiation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of hematopoietic stem cell differentiation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of hematopoietic stem cell differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of hemopoiesis	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of hemopoiesis	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of hemopoiesis	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in protein autophosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein export from nucleus	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within protein export from nucleus	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of erythrocyte differentiation	ISO Inferred from Sequence Orthology more info
involved_in regulation of erythrocyte differentiation	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to folic acid	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to thyroxine	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to toxic substance	IEP Inferred from Expression Pattern more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
is_active_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrial nucleoid	IEA Inferred from Electronic Annotation more info
located_in mitochondrial nucleoid	ISO Inferred from Sequence Orthology more info
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in nucleolus	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: stress-70 protein, mitochondrial

Names: 75 kDa glucose-regulated protein; GRP 75; catecholamine regulated protein 40; heat shock 70 kDa protein 9; heat shock 70kDa protein 9A; heat shock protein 9; heat shock protein family A member 9; heat shock protein, A; mortalin; mtHSP70; peptide-binding protein 74; stress-70 protein, mitochondrial-like

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_001100658.2 → NP_001094128.2 stress-70 protein, mitochondrial

See identical proteins and their annotated locations for NP_001094128.2

Status: VALIDATED

Source sequence(s)

JAXUCZ010000018

UniProtKB/Swiss-Prot

P48721

UniProtKB/TrEMBL

F1M953

Related

ENSRNOP00000026696.4, ENSRNOT00000026696.8

Conserved Domains (2) summary

cd11733
Location:52 → 428

HSPA9-like_NBD; Nucleotide-binding domain of human HSPA9, Escherichia coli DnaK, and similar proteins

PRK00290
Location:52 → 656

dnaK; molecular chaperone DnaK; Provisional