CCS1 copper chaperone CCS1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: CCS1
Official Full Name: copper chaperone CCS1
Primary source: SGD:S000004641
Locus tag: YMR038C
See related: AllianceGenome:SGD:S000004641; FungiDB:YMR038C; VEuPathDB:YMR038C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: LYS7
Summary: Enables superoxide dismutase copper chaperone activity. Involved in protein maturation by copper ion transfer. Located in cytosol; mitochondrial inner membrane; and nucleus. Used to study amyotrophic lateral sclerosis; cataract; neurodegenerative disease; and sensorineural hearing loss. 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, Apr 2022]
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Genomic context

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See CCS1 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (347511..348260, complement)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Lack of SOD1 in a RAD51 mutant depending on CCS1 exacerbates genomic instability and oxidative stress-mediated cytotoxicity in Saccharomyces cerevisiae.
Title: Lack of superoxide dismutase in a rad51 mutant exacerbates genomic instability and oxidative stress-mediated cytotoxicity in Saccharomyces cerevisiae.
propose a complete molecular mechanism for CCS1 activity and reclassification as a first-of-its-kind "dual chaperone."
Title: The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturation.
Data suggest that Ccs1 activates immature Sod1 by delivering copper and facilitating oxidation of intramolecular disulfide bond in Sod1; Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on the apoenzyme. (Ccs1 = copper chaperone for superoxide dismutase; Sod1 = copper-zinc superoxide dismutase)
Title: Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.
Data show that the aging process increased the DNA damage rates 3-fold in the wild type and more than 5-fold in superoxide dismutases sod1Delta, sod2Delta, and molecular chaperone ccs1Delta mutant cells.
Title: Absence of superoxide dismutase activity causes nuclear DNA fragmentation during the aging process.
CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition.
Title: Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes.
Localization of the reduced, Ccs1-independent forms of Sod1 relied on Mia40, an essential component of the mitochondrial intermembrane space import and assembly pathway
Title: Mia40 and MINOS act in parallel with Ccs1 in the biogenesis of mitochondrial Sod1.
The Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in the copper chaperone Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.
Title: Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system.
The oxidoreductase of the mitochondrial disulfide relay, Mia40, controls oxidative folding of domain I of the copper chaperone Ccs1 whereby controlling the cellular distribution of Ccs1 and, consequently, active Superoxide dismutase 1 (Sod1).
Title: Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol.
Results describe the identification of the copper chaperone for superoxide dismutase as a mediator of copper delivery to XIAP in cells.
Title: Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination.
Cu,Zn-superoxide dismutase is activated in the absence of oxygen and the copper chaperone CCS
Title: Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS.

Submit: New GeneRIF Correction See all GeneRIFs (13)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

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 metal ion binding	IEA Inferred from Electronic Annotation more info
enables superoxide dismutase copper chaperone activity	IBA Inferred from Biological aspect of Ancestor more info
enables superoxide dismutase copper chaperone activity	IGI Inferred from Genetic Interaction more info	PubMed
enables superoxide dismutase copper chaperone activity	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in protein maturation by copper ion transfer	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
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial inner membrane	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial intermembrane space	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: copper chaperone CCS1

NP_013752.1

Copper chaperone for superoxide dismutase Sod1p; involved in oxidative stress protection; Met-X-Cys-X2-Cys motif within N-terminus is involved in insertion of copper into Sod1p under conditions of copper deprivation; required for regulation of yeast copper genes in response to DNA-damaging agents; protein abundance increases in response to DNA replication stress; human homolog CCS can complement yeast ccs1 null mutant

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001145.3 Reference assembly

Range

347511..348260 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182535.1 → NP_013752.1 TPA: copper chaperone CCS1 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013752.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VZL3, P40202

UniProtKB/TrEMBL

A6ZMA0, B3LLT7, G2WK91, N1P5D6

Conserved Domains (1) summary

PLN02957
Location:15 → 238

PLN02957; copper, zinc superoxide dismutase