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P23202 (URE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional regulator URE2
Alternative name(s):
Disulfide reductase
EC=1.8.4.-
Glutathione peroxidase
EC=1.11.1.9
Gene names
Name:URE2
Ordered Locus Names:YNL229C
ORF Names:N1165
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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) actvites. Ref.1 Ref.8 Ref.9 Ref.10 Ref.13 Ref.15

Catalytic activity

2 glutathione + H2O2 = glutathione disulfide + 2 H2O. Ref.15

Subunit structure

Homodimer. Interacts with NNK1. Ref.16

Subcellular location

Cytoplasm Ref.9.

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. Ref.7 Ref.22

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 (Ref.6). [URE3] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [URE3] propagation (Ref.11).

Present with 7060 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the GST superfamily.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.

KM=2.4 mM for bis-(2-hydroxyethyl) disulfide (HEDS) Ref.15

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NNK1P360034EBI-20138,EBI-9796

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 354353Transcriptional regulator URE2
PRO_0000186013

Regions

Domain112 – 19685GST N-terminal
Domain205 – 354150GST C-terminal
Region2 – 8988Prion domain (PrD)
Region164 – 1652Glutathione binding
Region180 – 1812Glutathione binding

Sites

Binding site1241Glutathione
Binding site1511Glutathione

Amino acid modifications

Modified residue21N-acetylmethionine Ref.17

Experimental info

Mutagenesis1221A → S: Reduces glutaredoxin activity. Ref.15
Mutagenesis1241N → A or V: Abolishes glutaredoxin activity. Ref.15
Mutagenesis3131F → S: Destroys protein function.

Secondary structure

.............................................. 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23202 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 2C628976034B0F1C

FASTA35440,271
        10         20         30         40         50         60 
MMNNNGNQVS NLSNALRQVN IGNRNSNTTT DQSNINFEFS TGVNNNNNNN SSSNNNNVQN 

        70         80         90        100        110        120 
NNSGRNGSQN NDNENNIKNT LEQHRQQQQA FSDMSHVEYS RITKFFQEQP LEGYTLFSHR 

       130        140        150        160        170        180 
SAPNGFKVAI VLSELGFHYN TIFLDFNLGE HRAPEFVSVN PNARVPALID HGMDNLSIWE 

       190        200        210        220        230        240 
SGAILLHLVN KYYKETGNPL LWSDDLADQS QINAWLFFQT SGHAPMIGQA LHFRYFHSQK 

       250        260        270        280        290        300 
IASAVERYTD EVRRVYGVVE MALAERREAL VMELDTENAA AYSAGTTPMS QSRFFDYPVW 

       310        320        330        340        350 
LVGDKLTIAD LAFVPWNNVV DRIGINIKIE FPEVYKWTKH MMRRPAVIKA LRGE 

« Hide

References

« Hide 'large scale' references
[1]"The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases."
Coschigano P.W., Magasanik B.
Mol. Cell. Biol. 11:822-832(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein."
Edskes H.K., Wickner R.B.
Proc. Natl. Acad. Sci. U.S.A. 99:16384-16391(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 14085 / CBS 3093 / IFO 1997 / NRRL Y-12657, ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Boots, CBS 2087, CBS 4734, CBS 5112, CBS 5287, CBS 7957, Chevalieri / ATCC 10604 / CBS 405 / IFO 0258 / NRRL Y-1546, Fleischmann, McPhie Sourdough, SAF, Sigma 1278B, Wyeast#1007, YJM 143, YJM 280, YJM 320, YJM 326 and YJM 415.
[3]"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae."
Wickner R.B.
Science 264:566-569(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
[7]"Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells."
Masison D.C., Wickner R.B.
Science 270:93-95(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN PRION.
[8]"Interaction of the GATA factor Gln3p with the nitrogen regulator Ure2p in Saccharomyces cerevisiae."
Blinder D., Coschigano P.W., Magasanik B.
J. Bacteriol. 178:4734-4736(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors."
Beck T., Hall M.N.
Nature 402:689-692(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Nitrogen catabolite repression of DAL80 expression depends on the relative levels of Gat1p and Ure2p production in Saccharomyces cerevisiae."
Cunningham T.S., Andhare R., Cooper T.G.
J. Biol. Chem. 275:14408-14414(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p."
Moriyama H., Edskes H.K., Wickner R.B.
Mol. Cell. Biol. 20:8916-8922(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION, PRION CURING.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms."
Bai M., Zhou J.M., Perrett S.
J. Biol. Chem. 279:50025-50030(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Novel glutaredoxin activity of the yeast prion protein Ure2 reveals a native-like dimer within fibrils."
Zhang Z.R., Perrett S.
J. Biol. Chem. 284:14058-14067(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ALA-122 AND ASN-124.
[16]"A global protein kinase and phosphatase interaction network in yeast."
Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B., Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D., Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C., Nesvizhskii A.I., Tyers M.
Science 328:1043-1046(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NNK1.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds."
Bousset L., Belrhali H., Melki R., Morera S.
Biochemistry 40:13564-13573(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 95-354 IN COMPLEX WITH GLUTATHIONE AND INHIBITORS.
[19]"The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p."
Umland T.C., Taylor K.L., Rhee S., Wickner R.B., Davies D.R.
Proc. Natl. Acad. Sci. U.S.A. 98:1459-1464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 97-354.
[20]"Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae."
Bousset L., Belrhali H., Janin J., Melki R., Morera S.
Structure 9:39-46(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-353.
[21]"Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p."
Chan J.C., Oyler N.A., Yau W.M., Tycko R.
Biochemistry 44:10669-10680(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 10-39.
[22]"Characterization of beta-sheet structure in Ure2p(1-89) yeast prion fibrils by solid-state nuclear magnetic resonance."
Baxa U., Wickner R.B., Steven A.C., Anderson D.E., Marekov L.N., Yau W.M., Tycko R.
Biochemistry 46:13149-13162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-89, DOMAIN PRION.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Mad yeast disease - Issue 47 of June 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35268 Genomic DNA. Translation: AAA35201.1.
AF525174 Genomic DNA. Translation: AAM93167.1.
AF525175 Genomic DNA. Translation: AAM93168.1.
AF525176 Genomic DNA. Translation: AAM93169.1.
AF525177 Genomic DNA. Translation: AAM93170.1.
AF525178 Genomic DNA. Translation: AAM93171.1.
AF525179 Genomic DNA. Translation: AAM93172.1.
AF525180 Genomic DNA. Translation: AAM93173.1.
AF525181 Genomic DNA. Translation: AAM93174.1.
AF525182 Genomic DNA. Translation: AAM93175.1.
AF525183 Genomic DNA. Translation: AAM93176.1.
AF525184 Genomic DNA. Translation: AAM93177.1.
AF525185 Genomic DNA. Translation: AAM93178.1.
AF525186 Genomic DNA. Translation: AAM93179.1.
AF525187 Genomic DNA. Translation: AAM93180.1.
AF525188 Genomic DNA. Translation: AAM93181.1.
AF525189 Genomic DNA. Translation: AAM93182.1.
AF525190 Genomic DNA. Translation: AAM93183.1.
AF525191 Genomic DNA. Translation: AAM93184.1.
AF525192 Genomic DNA. Translation: AAM93185.1.
Z69381 Genomic DNA. Translation: CAA93369.1.
Z71505 Genomic DNA. Translation: CAA96134.1.
BK006947 Genomic DNA. Translation: DAA10329.1.
PIRA39609.
RefSeqNP_014170.1. NM_001183067.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6WX-ray2.50A/B/C/D94-354[»]
1G6YX-ray2.80A/B94-354[»]
1HQOX-ray2.30A/B97-354[»]
1JZRX-ray2.90A/B/C/D95-354[»]
1K0AX-ray2.50A/B95-354[»]
1K0BX-ray2.50A/B/C/D95-354[»]
1K0CX-ray2.50A/B/C/D95-354[»]
1K0DX-ray2.20A/B/C/D95-354[»]
DisProtDP00353.
ProteinModelPortalP23202.
SMRP23202. Positions 96-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35609. 287 interactions.
DIPDIP-1308N.
IntActP23202. 29 interactions.
MINTMINT-393865.
STRING4932.YNL229C.

Proteomic databases

MaxQBP23202.
PaxDbP23202.
PeptideAtlasP23202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL229C; YNL229C; YNL229C.
GeneID855492.
KEGGsce:YNL229C.

Organism-specific databases

CYGDYNL229c.
SGDS000005173. URE2.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125742.
KOK00799.
OMAVYKWTKH.
OrthoDBEOG7KWSWX.

Enzyme and pathway databases

BioCycYEAST:YNL229C-MONOMER.

Gene expression databases

GenevestigatorP23202.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR017298. Prion_URE2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PIRSFPIRSF037861. Prion_URE2. 1 hit.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23202.
NextBio979478.

Entry information

Entry nameURE2_YEAST
AccessionPrimary (citable) accession number: P23202
Secondary accession number(s): D6W0W3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references