Dnajc5 DnaJ heat shock protein family (Hsp40) member C5 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Dnajc5provided by RGD
Official Full Name: DnaJ heat shock protein family (Hsp40) member C5provided by RGD
Primary source: RGD:620516
See related: EnsemblRapid:ENSRNOG00000015202 AllianceGenome:RGD:620516
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: Csp
Summary: Enables ATP-dependent protein binding activity. Predicted to be involved in chaperone-mediated protein folding and regulation of synaptic vesicle cycle. Predicted to act upstream of or within negative regulation of neuron apoptotic process. Located in terminal bouton. Is active in synaptic vesicle membrane. Human ortholog(s) of this gene implicated in neuronal ceroid lipofuscinosis 4. Orthologous to human DNAJC5 (DnaJ heat shock protein family (Hsp40) member C5). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Brain (RPKM 594.8), Thymus (RPKM 269.0) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 3q43

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	3	NC_086021.1 (188999508..189033455)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	3	NC_051338.1 (168621905..168656570)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	3	NC_005102.4 (177012714..177047787)

Chromosome 3 - NC_086021.1 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?

CSPalpha may modulate fusion pore dynamics in a phosphorylation-dependent manner.
Title: Phosphomimetic mutation of cysteine string protein-α increases the rate of regulated exocytosis by modulating fusion pore dynamics in PC12 cells.
both the J-domain and the linker domain of CSP1 are necessary to function in an important role in acinar cell exocytosis
Title: Characterization of cysteine string protein in rat parotid acinar cells.
a biochemical link between Hsp40 expression and Abeta(42) proteostasis that is cell specific
Title: Cell line specific modulation of extracellular aβ42 by Hsp40.
Establish a role for CSP-alpha in regulating digestive enzyme secretion and suggest that CSP-alpha and Hsc70 modulate specific soluble N-ethylmaleimide-sensitive attachment receptor interactions necessary for exocytosis.
Title: Functional role of J domain of cysteine string protein in Ca2+-dependent secretion from acinar cells.
palmitoylation of CSP is enhanced specifically by co-expression of the Golgi-localized palmitoyl transferases DHHC3, DHHC7, DHHC15, or DHHC17
Title: Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein.
CSPalpha activity is subject to regulation by factors that alter Hsc70 distribution and translocation within the cell
Title: The CSPalpha/G protein complex in PC12 cells.
cysteine string protein binds to a brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein
Title: A brain-specific isoform of small glutamine-rich tetratricopeptide repeat-containing protein binds to Hsc70 and the cysteine string protein.
phosphorylation-dependent interaction with synaptotagmin I
Title: Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I.
A novel alphaGDI complex from synaptic membranes contains three chaperone components: Hsp90, Hsc70 and cysteine string protein (CSP). The complex is dissociated in response to Ca(2+)-induced neurotransmitter release.
Title: Rab-alphaGDI activity is regulated by a Hsp90 chaperone complex.
Proportion of the phosphorylated protein varies between distinct brain regions and also exhibits developmental regulation.
Title: Phosphorylation of cysteine string protein in the brain: developmental, regional and synaptic specificity.

Submit: New GeneRIF Correction See all GeneRIFs (14)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ATP-dependent protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in chaperone-mediated protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone-mediated protein folding	ISO Inferred from Sequence Orthology more info
involved_in chemical synaptic transmission	TAS Traceable Author Statement more info	PubMed
acts_upstream_of_or_within negative regulation of neuron apoptotic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of neuron apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in regulation of synaptic vesicle cycle	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of synaptic vesicle cycle	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in Golgi apparatus	IEA Inferred from Electronic Annotation more info
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in chromaffin granule membrane	IEA Inferred from Electronic Annotation more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity more info
is_active_in intracellular membrane-bounded organelle	IBA Inferred from Biological aspect of Ancestor more info
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in melanosome	IEA Inferred from Electronic Annotation more info
is_active_in membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in membrane	ISS Inferred from Sequence or Structural Similarity more info
is_active_in neuromuscular junction	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity more info
is_active_in presynapse	IBA Inferred from Biological aspect of Ancestor more info
is_active_in presynapse	ISO Inferred from Sequence Orthology more info
located_in synaptic vesicle	ISO Inferred from Sequence Orthology more info
is_active_in synaptic vesicle membrane	IDA Inferred from Direct Assay more info	PubMed
located_in terminal bouton	HDA more info	PubMed

General protein information

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Preferred Names: dnaJ homolog subfamily C member 5

Names: DnaJ (Hsp40) homolog, subfamily C, member 5; cysteine string protein

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_001431433.1 → NP_001418362.1 dnaJ homolog subfamily C member 5

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P60905

UniProtKB/TrEMBL

A0A8I6A9F3, A6KLZ8
NM_001431434.1 → NP_001418363.1 dnaJ homolog subfamily C member 5

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P60905

UniProtKB/TrEMBL

A0A8I6A9F3, A6KLZ8
NM_001431435.1 → NP_001418364.1 dnaJ homolog subfamily C member 5

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P60905

UniProtKB/TrEMBL

A0A8I6A9F3, A6KLZ8
NM_024161.4 → NP_077075.1 dnaJ homolog subfamily C member 5

See identical proteins and their annotated locations for NP_077075.1

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

UniProtKB/Swiss-Prot

P60905

UniProtKB/TrEMBL

A0A8I6A9F3, A6KLZ8

Conserved Domains (1) summary

COG0484
Location:15 → 84

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

RNA

NR_197211.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003
NR_197212.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003
NR_197213.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003
NR_197214.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

JAXUCZ010000003

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_086021.1 Reference GRCr8

Range

188999508..189033455

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_008762544.4 → XP_008760766.1 dnaJ homolog subfamily C member 5 isoform X1

Conserved Domains (1) summary

COG0484
Location:15 → 84

DnaJ; DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones]
XM_008762545.4 → XP_008760767.1 dnaJ homolog subfamily C member 5 isoform X1

Related

ENSRNOP00000078729.2, ENSRNOT00000102827.2

Conserved Domains (1) summary

COG0484
Location:15 → 84

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