GRX6 glutathione-disulfide reductase GRX6 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: GRX6
Official Full Name: glutathione-disulfide reductase GRX6
Primary source: SGD:S000002168
Locus tag: YDL010W
See related: AllianceGenome:SGD:S000002168; FungiDB:YDL010W; VEuPathDB:YDL010W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables 2 iron, 2 sulfur cluster binding activity; glutathione-disulfide reductase (NADPH) activity; and iron ion binding activity. Involved in cellular response to oxidative stress. Located in Golgi apparatus; endoplasmic reticulum membrane; and fungal-type vacuole. [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See GRX6 in Genome Data Viewer

Location:: chromosome: IV

Exon count:: 1

Sequence:: Chromosome: IV; NC_001136.10 (432330..433025)

Chromosome IV - NC_001136.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Crystal structure of Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster has been presented.
Title: Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster.
A specific function influenced by Grx6 activity is the homeostasis of intracellular calcium. Grx6-deficient mutants have reduced levels of calcium in the ER lumen, whereas accumulation occurs at the cytosol from extracellular sources.
Title: Altered intracellular calcium homeostasis and endoplasmic reticulum redox state in Saccharomyces cerevisiae cells lacking Grx6 glutaredoxin.
Compared to the classic dithiol glutaredoxin Grx1, Grx6 has a lower glutathione disulfide reductase activity but a higher glutathione S-transferase activity.
Title: Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6.
Grx6 and Grx7 do not play a general role in the oxidative folding of proteins in the early secretory pathway but rather counteract the oxidation of specific thiol groups in substrate proteins.
Title: A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance.
GRX6 could be responsible for the regulation of the sulfhydryl oxidative state at the oxidant conditions of the early secretory pathway vesicles.
Title: Saccharomyces cerevisiae Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway.
S. pombe cells harboring plasmid pFGRX6 containing the Grx6 gene had about 1.3-fold elevated Grx activity in the exponential phase, and grew better than the control cells under some stressful conditions.
Title: Expression, characterization and regulation of a Saccharomyces cerevisiae monothiol glutaredoxin (Grx6) gene in Schizosaccharomyces pombe.

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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 2 iron, 2 sulfur cluster binding	IDA Inferred from Direct Assay more info	PubMed
enables 2 iron, 2 sulfur cluster binding	IEA Inferred from Electronic Annotation more info
enables glutathione disulfide oxidoreductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables glutathione-disulfide reductase (NADPH) activity	IDA Inferred from Direct Assay more info	PubMed
enables glutathione-disulfide reductase (NADPH) activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables iron ion binding	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in cellular oxidant detoxification	IEA Inferred from Electronic Annotation more info
involved_in cellular response to oxidative stress	IBA Inferred from Biological aspect of Ancestor more info
involved_in cellular response to oxidative stress	IGI Inferred from Genetic Interaction more info	PubMed
involved_in cellular response to oxidative stress	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi apparatus	IDA Inferred from Direct Assay more info	PubMed
is_active_in Golgi lumen	IBA Inferred from Biological aspect of Ancestor more info
located_in Golgi lumen	IDA Inferred from Direct Assay more info	PubMed
is_active_in cis-Golgi network	IBA Inferred from Biological aspect of Ancestor more info
located_in cis-Golgi network	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum membrane	IDA Inferred from Direct Assay more info	PubMed
located_in fungal-type vacuole	HDA more info	PubMed
is_active_in fungal-type vacuole	IBA Inferred from Biological aspect of Ancestor more info
located_in fungal-type vacuole	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in vacuole	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: glutathione-disulfide reductase GRX6

NP_010274.1

Cis-Golgi localized monothiol glutaredoxin, binds Fe-S cluster; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; GRX6 has a paralog, GRX7, that arose from the whole genome duplication

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_001136.10 Reference assembly

Range

432330..433025

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001180069.1 → NP_010274.1 TPA: glutathione-disulfide reductase GRX6 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_010274.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VRX8, Q12438

UniProtKB/TrEMBL

G2WCE4, N1P687

Conserved Domains (1) summary

cd03419
Location:127 → 210

GRX_GRXh_1_2_like; Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, ...