Ccs copper chaperone for superoxide dismutase [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ccsprovided by MGI
Official Full Name: copper chaperone for superoxide dismutaseprovided by MGI
Primary source: MGI:MGI:1333783
See related: Ensembl:ENSMUSG00000034108 AllianceGenome:MGI:1333783
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: Ccsd
Summary: Predicted to enable copper ion binding activity; enzyme binding activity; and superoxide dismutase copper chaperone activity. Acts upstream of or within positive regulation of oxidoreductase activity. Predicted to be located in cytoplasm and nucleus. Is expressed in heart. Human ortholog(s) of this gene implicated in amyotrophic lateral sclerosis. Orthologous to human CCS (copper chaperone for superoxide dismutase). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in liver adult (RPKM 83.8), liver E18 (RPKM 73.3) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 19 A; 19 4.11 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	19	NC_000085.7 (4875394..4889326, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	19	NC_000085.6 (4825366..4839356, complement)

Chromosome 19 - NC_000085.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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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?

results suggest that a SOD1 supplement to healthy mice may not be necessary to modulate cell proliferation and neuroblast differentiation in the dentate gyrus
Title: Effects of Cu,Zn-superoxide dismutase on cell proliferation and neuroblast differentiation in the mouse dentate gyrus.
Small interfering RNA (siRNA) targeting CCS was introduced into metallothionein-knockout mouse fibroblasts (MT-KO cells) and their wild type cells (MT-WT cells) to reveal the interactive role of CCS with other Cu-regulating proteins.
Title: Roles of copper chaperone for superoxide dismutase 1 and metallothionein in copper homeostasis.
effects of copper chaperone for SOD1 on mitochondrial dysfunction are SOD1 mutation dependent and correlate with SOD1 redox susceptibility
Title: Redox susceptibility of SOD1 mutants is associated with the differential response to CCS over-expression in vivo.
Study finds that as expected, CCS over-expression promotes oxidation of a wild-type SOD1 disulfide; however, in the diseased G93A/CCS mouse, there was no increased oxidation of the mutant SOD1 disulfide.
Title: Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.
These results establish that CCS/G93A SOD1 mice manifest an isolated complex IV deficiency which may underlie a substantial part of mutant SOD1-induced mitochondrial cytopathy.
Title: Isolated cytochrome c oxidase deficiency in G93A SOD1 mice overexpressing CCS protein.
A mechanism determining the abundance of CCS that is competitive with the process of copper delivery to SOD1 is described, revealing a unique post-translational component of intracellular copper homeostasis.
Title: Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase.
CCS-independent activation of mammalian SOD1 involves glutathione
Title: Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone.
Associated with copper deficiency were higher levels of Ccs in erythrocytes.
Title: Cu,Zn-superoxide dismutase is lower and copper chaperone CCS is higher in erythrocytes of copper-deficient rats and mice.
CCS is necessary for the efficient incorporation of copper into SOD1 in motor neurons, but it does not modify the onset and progression of motor neuron disease in SOD1-mutant mice.
Title: Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading.

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Variation

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Alleles

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

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

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Ccsd (e-PCR), detects polymorphism
- UniSTS:164680

PMC16025P1 (e-PCR)
- UniSTS:271450

NoName (e-PCR)
- UniSTS:225122

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables copper ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables copper ion binding	IEA Inferred from Electronic Annotation more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables superoxide dismutase copper chaperone activity	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
acts_upstream_of_or_within positive regulation of oxidoreductase activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in removal of superoxide radicals	IBA Inferred from Biological aspect of Ancestor more info
involved_in superoxide metabolic process	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in mitochondrial intermembrane space	TAS Traceable Author Statement more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
located_in nucleus	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: copper chaperone for superoxide dismutase

Names: superoxide dismutase copper chaperone

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_016892.4 → NP_058588.1 copper chaperone for superoxide dismutase

See identical proteins and their annotated locations for NP_058588.1

Status: VALIDATED

Source sequence(s)

AC141437

Consensus CDS

CCDS29438.1

UniProtKB/Swiss-Prot

Q9CRJ9, Q9WU84

UniProtKB/TrEMBL

A0A494BBF1, Q543K2

Related

ENSMUSP00000035486.6, ENSMUST00000037246.7

Conserved Domains (3) summary

PLN02957
Location:13 → 253

PLN02957; copper, zinc superoxide dismutase

cd00305
Location:89 → 227

Cu-Zn_Superoxide_Dismutase; Copper/zinc superoxide dismutase (SOD). superoxide dismutases catalyse the conversion of superoxide radicals to molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the ...

cd00371
Location:15 → 73

HMA; Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain ...