P23202 · URE2_YEAST

Function

function

Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of genes expressed upon nitrogen limitation. Is also an atypical glutaredoxin without a catalytical cysteine residue. Has glutathione peroxidase and thiol:disulfide oxidoreductase activities in both native and fibrillar form. Also shows insulin disulfide reductase and dehydroascorbic acid reductase (DHAR) activities.

Miscellaneous

[URE3] is the prion form of URE2. [URE3] is the result of a conformational change of the cellular URE2 protein that becomes self-propagating and infectious. This conformational change generates a form of URE2 that assembles into amyloid fibrils. [URE3]-aggregates sequester soluble URE2, which then fails to retain GLN3 in the cytoplasm, resulting in GLN3 activation and consequently derepression of genes that are required for utilization of poor nirogen sources (PubMed:7909170).
[URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (PubMed:11073991).
Present with 7060 molecules/cell in log phase SD medium.

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.4 mMbis-(2-hydroxyethyl) disulfide (HEDS)
kcat is 1.2 sec-1 with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site124glutathione (UniProtKB | ChEBI)
Binding site151glutathione (UniProtKB | ChEBI)
Binding site164-165glutathione (UniProtKB | ChEBI)
Binding site180-181glutathione (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglutathione peroxidase activity
Molecular Functionphosphoprotein binding
Molecular Functiontranscription corepressor activity
Biological Processnegative regulation of transcription by transcription factor localization
Biological Processnitrate assimilation
Biological Processprotein urmylation
Biological Processregulation of nitrogen utilization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcriptional regulator URE2
  • Alternative names

Gene names

    • Name
      URE2
    • ORF names
      N1165
    • Ordered locus names
      YNL229C

Organism names

  • Taxonomic identifier
  • Strains
    • ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657
    • ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220
    • Boots
    • CBS 2087
    • CBS 4734
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces

Accessions

  • Primary accession
    P23202
  • Secondary accessions
    • D6W0W3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis122Reduces glutaredoxin activity.
Mutagenesis124Abolishes glutaredoxin activity.
Mutagenesis313Destroys protein function.

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylmethionine
ChainPRO_00001860132-354Transcriptional regulator URE2

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer. Interacts with NNK1.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P23202GLN3 P184942EBI-20138, EBI-7657
BINARY P23202NNK1 P360034EBI-20138, EBI-9796

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region2-89Prion domain (PrD)
Region22-76Disordered
Domain112-196GST N-terminal
Domain205-354GST C-terminal

Domain

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form.

Sequence similarities

Belongs to the GST superfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    354
  • Mass (Da)
    40,271
  • Last updated
    1991-11-01 v1
  • Checksum
    2C628976034B0F1C
MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M35268
EMBL· GenBank· DDBJ
AAA35201.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525174
EMBL· GenBank· DDBJ
AAM93167.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525175
EMBL· GenBank· DDBJ
AAM93168.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525176
EMBL· GenBank· DDBJ
AAM93169.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525177
EMBL· GenBank· DDBJ
AAM93170.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525178
EMBL· GenBank· DDBJ
AAM93171.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525179
EMBL· GenBank· DDBJ
AAM93172.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525180
EMBL· GenBank· DDBJ
AAM93173.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525181
EMBL· GenBank· DDBJ
AAM93174.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525182
EMBL· GenBank· DDBJ
AAM93175.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525183
EMBL· GenBank· DDBJ
AAM93176.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525184
EMBL· GenBank· DDBJ
AAM93177.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525185
EMBL· GenBank· DDBJ
AAM93178.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525186
EMBL· GenBank· DDBJ
AAM93179.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525187
EMBL· GenBank· DDBJ
AAM93180.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525188
EMBL· GenBank· DDBJ
AAM93181.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525189
EMBL· GenBank· DDBJ
AAM93182.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525190
EMBL· GenBank· DDBJ
AAM93183.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525191
EMBL· GenBank· DDBJ
AAM93184.1
EMBL· GenBank· DDBJ
Genomic DNA
AF525192
EMBL· GenBank· DDBJ
AAM93185.1
EMBL· GenBank· DDBJ
Genomic DNA
Z69381
EMBL· GenBank· DDBJ
CAA93369.1
EMBL· GenBank· DDBJ
Genomic DNA
Z71505
EMBL· GenBank· DDBJ
CAA96134.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006947
EMBL· GenBank· DDBJ
DAA10329.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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