Dnajc10 DnaJ heat shock protein family (Hsp40) member C10 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Dnajc10provided by MGI
Official Full Name: DnaJ heat shock protein family (Hsp40) member C10provided by MGI
Primary source: MGI:MGI:1914111
See related: Ensembl:ENSMUSG00000027006 AllianceGenome:MGI:1914111
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: JPDI; ERdj5; D2Ertd706e; 1200006L06Rik
Summary: Enables several functions, including ATPase activator activity; ATPase binding activity; and oxidoreductase activity, acting on a sulfur group of donors. Involved in ERAD pathway and positive regulation of ATP-dependent activity. Located in endoplasmic reticulum. Orthologous to human DNAJC10 (DnaJ heat shock protein family (Hsp40) member C10). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in genital fat pad adult (RPKM 77.2), limb E14.5 (RPKM 18.0) and 26 other tissues See more
Orthologs: human all
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Genomic context

Location:: 2 C3; 2 48.05 cM

Exon count:: 23

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	2	NC_000068.8 (80145790..80184399)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	2	NC_000068.7 (80315446..80354055)

Chromosome 2 - NC_000068.8 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

DNAJC10 maintains survival and self-renewal of leukemia stem cells through PERK branch of the unfolded protein response.
Title: DNAJC10 maintains survival and self-renewal of leukemia stem cells through PERK branch of the unfolded protein response.
ERdj5 protects goblet cells from endoplasmic reticulum stress-mediated apoptosis under inflammatory conditions.
Title: ERdj5 protects goblet cells from endoplasmic reticulum stress-mediated apoptosis under inflammatory conditions.
Loss of ERdj5 exacerbates oxidative stress in mice with alcoholic liver disease via suppressing Nrf2.
Title: Loss of ERdj5 exacerbates oxidative stress in mice with alcoholic liver disease via suppressing Nrf2.
AAV-mediated ERdj5 overexpression protects against P23H rhodopsin toxicity.
Title: AAV-mediated ERdj5 overexpression protects against P23H rhodopsin toxicity.
ERdj5 in Innate Immune Cells Is a Crucial Factor for the Mucosal Adjuvanticity of Cholera Toxin.
Title: ERdj5 in Innate Immune Cells Is a Crucial Factor for the Mucosal Adjuvanticity of Cholera Toxin.
Ablation of the Chaperone Protein ERdj5 Results in a Sjogren's Syndrome-Like Phenotype in Mice, Consistent With an Upregulated Unfolded Protein Response in Human Patients.
Title: Ablation of the Chaperone Protein ERdj5 Results in a Sjögren's Syndrome-Like Phenotype in Mice, Consistent With an Upregulated Unfolded Protein Response in Human Patients.
These results identify ERdj5 as one of the master regulators of ER calcium homeostasis and thus shed light on the importance of cross talk among redox, Ca(2+), and protein homeostasis in the ER.
Title: Redox-assisted regulation of Ca2+ homeostasis in the endoplasmic reticulum by disulfide reductase ERdj5.
study identified the redox partners of ERdj5 from the mouse epididymis; findings show that ERdj5 interacted with two of the identified proteins via formation of intermolecular disulfide bond
Title: Identification of the redox partners of ERdj5/JPDI, a PDI family member, from an animal tissue.
Data suggest that ERdj5 contributes to ER protein quality control in the salivary gland.
Title: Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland.
study found that an endoplasmic reticulum (ER) protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins & accelerated ER-associated degradation through its physical and functional associations with EDEM & BiP
Title: ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1)
Spontaneous (1) 1 citation
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AW742525 (e-PCR)
- UniSTS:207364

NoName (e-PCR)
- UniSTS:234250

RH101846 (e-PCR)
- UniSTS:116755

D2Ertd706e (e-PCR), detects polymorphism
- UniSTS:167343

NoName (e-PCR)
- UniSTS:234437

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATPase activator activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATPase binding	IPI Inferred from Physical Interaction more info	PubMed
enables ATPase binding	ISO Inferred from Sequence Orthology more info
enables Hsp70 protein binding	IEA Inferred from Electronic Annotation more info
enables Hsp70 protein binding	ISO Inferred from Sequence Orthology more info
enables disulfide oxidoreductase activity	IDA Inferred from Direct Assay more info	PubMed
enables misfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables misfolded protein binding	ISO Inferred from Sequence Orthology more info
enables misfolded protein binding	ISS Inferred from Sequence or Structural Similarity more info
enables oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor	IBA Inferred from Biological aspect of Ancestor more info
enables oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-disulfide reductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein-disulfide reductase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein-disulfide reductase activity	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-folding chaperone binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in ERAD pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in ERAD pathway	ISO Inferred from Sequence Orthology more info
involved_in IRE1-mediated unfolded protein response	IBA Inferred from Biological aspect of Ancestor more info
involved_in intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	ISO Inferred from Sequence Orthology more info
involved_in intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of protein phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein phosphorylation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of ATP-dependent activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
involved_in protein folding in endoplasmic reticulum	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

Component	Evidence Code	Pubs
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info	PubMed
part_of endoplasmic reticulum chaperone complex	ISO Inferred from Sequence Orthology more info
part_of endoplasmic reticulum chaperone complex	ISS Inferred from Sequence or Structural Similarity more info
is_active_in endoplasmic reticulum lumen	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum lumen	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum lumen	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: dnaJ homolog subfamily C member 10

Names: DnaJ (Hsp40) homolog, subfamily C, member 10; ER-resident protein ERdj5; endoplasmic reticulum DNA J domain-containing protein 5; endoplasmic reticulum DnaJ-PDI fusion protein 1; j domain-containing PDI-like protein; j domain-containing protein disulfide isomerase-like protein

NP_077143.2

EC 1.8.4.-

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_024181.2 → NP_077143.2 dnaJ homolog subfamily C member 10 precursor

See identical proteins and their annotated locations for NP_077143.2

Status: VALIDATED

Source sequence(s)

AK004617, AK016269, AW546442, CN460590

Consensus CDS

CCDS38159.1

UniProtKB/Swiss-Prot

A2ASA2, Q71S84, Q8CH78, Q8CIB0, Q99LV4, Q9DC23

Related

ENSMUSP00000028392.8, ENSMUST00000028392.8

Conserved Domains (5) summary

COG0484
Location:34 → 132

DnaJ; DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]

cd03003
Location:129 → 229

PDI_a_ERdj5_N; PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is comprised of the first TRX domain of ERdj5 located after the ...

cd03004
Location:556 → 663

PDI_a_ERdj5_C; PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal ...

TIGR01130
Location:130 → 551

ER_PDI_fam; protein disulfide isomerase, eukaryotic

pfam00226
Location:35 → 97

DnaJ; DnaJ domain