Dnajc3 DnaJ heat shock protein family (Hsp40) member C3 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Dnajc3provided by MGI
Official Full Name: DnaJ heat shock protein family (Hsp40) member C3provided by MGI
Primary source: MGI:MGI:107373
See related: Ensembl:ENSMUSG00000022136 AllianceGenome:MGI:107373
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: p58; mp58; Prkri; p58IPK; Dnajc3a; Dnajc3b
Summary: Enables several functions, including misfolded protein binding activity; protein kinase inhibitor activity; and protein-folding chaperone binding activity. Involved in cellular response to cold; proteolysis involved in protein catabolic process; and regulation of translational initiation. Located in cytosol and endoplasmic reticulum lumen. Is expressed in several structures, including alimentary system; brain; genitourinary system; hemolymphoid system gland; and liver and biliary system. Orthologous to human DNAJC3 (DnaJ heat shock protein family (Hsp40) member C3). [provided by Alliance of Genome Resources, Dec 2024]
Annotation information: Note: On Build36, NCBI annotated NC_000080.4:117820545..117862457 as Dnajc3 with MGI:107373. Mouse Genome Informatics (MGI) defined that location as Dnajc3b, MGI:3696572. On April 10, 2006, NCBI renamed that location to conform to the definition by MGI. With Build37, the duplicate annotation was no longer required, because the component CT025524.8 was removed from the assembly. [13 Feb 2013]
Expression: Ubiquitous expression in placenta adult (RPKM 26.5), genital fat pad adult (RPKM 18.7) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 14 E4; 14 62.6 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	14	NC_000080.7 (119175371..119219114)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	14	NC_000080.6 (118937932..118981702)

Chromosome 14 - NC_000080.7 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?

Congenital Hyperinsulinism in Humans and Insulin Secretory Dysfunction in Mice Caused by Biallelic DNAJC3 Variants.
Title: Congenital Hyperinsulinism in Humans and Insulin Secretory Dysfunction in Mice Caused by Biallelic DNAJC3 Variants.
Progranulin inhibits fibrosis by interacting with and up-regulating DNAJC3 during mouse skin wound healing.
Title: Progranulin inhibits fibrosis by interacting with and up-regulating DNAJC3 during mouse skin wound healing.
Neuronal p58[IPK] Protects Retinal Ganglion Cells Independently of Macrophage/Microglia Activation in Ocular Hypertension.
Title: Neuronal p58(IPK) Protects Retinal Ganglion Cells Independently of Macrophage/Microglia Activation in Ocular Hypertension.
Chaperone protein p58(IPK) is expressed predominantly in retinal ganglion cells (RGC), inner retinal neurons, and the photoreceptor inner segments.
Title: Identification of p58IPK as a novel neuroprotective factor for retinal neurons.
p58IPK is a general inhibitor of the eIF2alpha kinases in that it also interacts with GCN2. Thus forced overexpression of cytoplasmic p58 delays eIF2alpha phosphorylation, suppresses GCN2 phosphorylation and prolongs protein synthesis
Title: p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity.
combined deletion of ATF6alpha and the ER cochaperone p58(IPK) resulted in synthetic embryonic lethality.
Title: Synthetic embryonic lethality upon deletion of the ER cochaperone p58(IPK) and the ER stress sensor ATF6α.
Data present a working model for P58(IPK) to act together with Bip to prevent protein aggregations and promote protein foldings within ER.
Title: Structural insight into the protective role of P58(IPK) during unfolded protein response.
Coxsackievirus B3 infection induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1.
Title: Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1.
mechanism by which P58(IPK) functions to promote protein folding within the endoplasmic reticulum, determined from the crystal structure of P58(IPK)
Title: Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR.
renal injury inflicted by expression of the folding mutants was markedly enhanced by haploinsufficiency of the endoplasmic reticulum cochaperone p58(IPK).
Title: Progressive renal injury from transgenic expression of human carbonic anhydrase IV folding mutants is enhanced by deficiency of p58IPK.

Submit: New GeneRIF Correction See all GeneRIFs (17)

Variation

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Alleles

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

Chemically induced (ENU) (1)
Targeted (2) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AI413631 (e-PCR)
- UniSTS:160567

RH124804 (e-PCR)
- UniSTS:161626

Dnajc3 (e-PCR), detects polymorphism
- UniSTS:144263

AA930114 (e-PCR)
- UniSTS:209056

AU067833 (e-PCR)
- UniSTS:180719

AW047562 (e-PCR)
- UniSTS:180720

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables misfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables misfolded protein binding	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IDA Inferred from Direct Assay more info	PubMed
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase inhibitor activity	IDA Inferred from Direct Assay more info	PubMed
enables protein kinase inhibitor activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in cellular response to cold	IDA Inferred from Direct Assay more info	PubMed
involved_in endoplasmic reticulum unfolded protein response	IC Inferred by Curator more info	PubMed
involved_in negative regulation of apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within negative regulation of protein kinase activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in positive regulation of translation initiation in response to endoplasmic reticulum stress	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
involved_in proteolysis involved in protein catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in response to endoplasmic reticulum stress	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info	PubMed
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum lumen	IDA Inferred from Direct Assay more info	PubMed
located_in smooth endoplasmic reticulum	IEA Inferred from Electronic Annotation more info
located_in smooth endoplasmic reticulum	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: dnaJ homolog subfamily C member 3

Names: DnaJ (Hsp40) homolog, subfamily C, member 3; DnaJ (Hsp40) homolog, subfamily C, member 3A; DnaJ (Hsp40) homolog, subfamily C, member 3B; interferon-induced, double-stranded RNA-activated protein kinase inhibitor; protein kinase inhibitor of 58 kDa; protein kinase inhibitor p58; protein kinase, interferon inducible double stranded RNA dependent inhibitor

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_008929.4 → NP_032955.2 dnaJ homolog subfamily C member 3 precursor

See identical proteins and their annotated locations for NP_032955.2

Status: VALIDATED

Source sequence(s)

AC154377

Consensus CDS

CCDS37012.1

UniProtKB/Swiss-Prot

Q60873, Q91YW3

UniProtKB/TrEMBL

Q3UFV9, Q3UKA1

Related

ENSMUSP00000022734.8, ENSMUST00000022734.9

Conserved Domains (6) summary

COG0484
Location:392 → 498

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

sd00006
Location:37 → 65

TPR; TPR repeat [structural motif]

pfam00226
Location:394 → 459

DnaJ; DnaJ domain

pfam00515
Location:107 → 137

TPR_1; Tetratricopeptide repeat

pfam13414
Location:36 → 100

TPR_11; TPR repeat

pfam14559
Location:318 → 382

TPR_19; Tetratricopeptide repeat