URE2 glutathione peroxidase [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: URE2
Official Full Name: glutathione peroxidase
Primary source: SGD:S000005173
Locus tag: YNL229C
See related: AllianceGenome:SGD:S000005173; FungiDB:YNL229C; VEuPathDB:YNL229C
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 glutathione peroxidase activity and phosphoprotein binding activity. Involved in several processes, including cytoplasmic sequestering of transcription factor; protein urmylation; and response to aluminum ion. Located in cytoplasm. [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (219137..220201, complement)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The yeast protein Ure2p triggers Tau pathology in a mouse model of tauopathy.
Title: The yeast protein Ure2p triggers Tau pathology in a mouse model of tauopathy.
Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.
Title: Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.
Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity.
Title: Innate immunity to yeast prions: Btn2p and Cur1p curing of the [URE3] prion is prevented by 60S ribosomal protein deficiency or ubiquitin/proteasome system overactivity.
Investigating the role of the transcriptional regulator Ure2 on the metabolism of Saccharomyces cerevisiae: a multi-omics approach.
Title: Investigating the role of the transcriptional regulator Ure2 on the metabolism of Saccharomyces cerevisiae: a multi-omics approach.
Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.
Title: Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.
This study reports on the finding of two genes, ITT1, an inhibitor of translation termination, and RPS1A, a small ribosomal protein, that when deleted yeast cells exhibit similar metal sensitivity phenotypes to gene deletion strain for URE2.
Title: Heavy metal sensitivities of gene deletion strains for ITT1 and RPS1A connect their activities to the expression of URE2, a key gene involved in metal detoxification in yeast.
DnaJB6-protected yeast cells from polyglutamine toxicity and cured yeast of both [URE3] prions and weak variants of [PSI(+)] prions but not strong [PSI(+)] prions
Title: Human J-protein DnaJB6b Cures a Subset of Saccharomyces cerevisiae Prions and Selectively Blocks Assembly of Structurally Related Amyloids.
study found that, in addition to Sis1,[URE3-1] is specifically dependent upon Swa2; data suggest that prion-chaperone specificity arises from the Swa2 TPR domain and supports a model where Swa2 acts through Hsp70, most likely to provide additional access points for Hsp104 to promote prion template generation
Title: Swa2, the yeast homolog of mammalian auxilin, is specifically required for the propagation of the prion variant [URE3-1].
Proteasomal degradation of Ure2p yields amyloidogenic N-terminal peptides and a C-terminal resistant fragment. In contrast to Sup35p, fibrillar Ure2p resists proteasomal degradation.
Title: The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.
We show that Cpr7 interacts with Ure2 and enhances its fibrillation. The requirement of Cpr7 is specific for [URE3] as its deletion does not antagonize both strong and weak variant of another yeast prion
Title: Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.

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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 glutathione peroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables glutathione peroxidase activity	IEA Inferred from Electronic Annotation more info
enables glutathione transferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables phosphoprotein binding	IDA Inferred from Direct Assay more info	PubMed
enables transcription corepressor 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 negative regulation of transcription by transcription factor localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in nitrate assimilation	IEA Inferred from Electronic Annotation more info
involved_in protein urmylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of nitrogen utilization	IEA Inferred from Electronic Annotation more info
involved_in regulation of nitrogen utilization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of nitrogen utilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of nitrogen utilization	IPI Inferred from Physical Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: glutathione peroxidase

NP_014170.1

EC 1.11.1.9

Nitrogen catabolite repression transcriptional regulator; inhibits GLN3 transcription in good nitrogen source; role in sequestering Gln3p and Gat1p to the cytoplasm; has glutathione peroxidase activity and can mutate to acquire GST activity; self-assembly under limited nitrogen conditions creates [URE3] prion and releases catabolite repression

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_001146.8 Reference assembly

Range

219137..220201 complement

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001183067.1 → NP_014170.1 TPA: glutathione peroxidase [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014170.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W0W3, P23202

UniProtKB/TrEMBL

A6ZRL3, B3LP70, B5VQI2, C7GPD0, C8ZG05, G2WLN6, N1NX06, Q7LLZ5

Conserved Domains (2) summary

cd10293
Location:208 → 350

GST_C_Ure2p; C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases

cd03048
Location:114 → 194

GST_N_Ure2p_like; GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources ...