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P36156 (GTO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-like 2

EC=2.5.1.18
Alternative name(s):
Extracellular mutant protein 4
Glutathione-dependent dehydroascorbate reductase
EC=1.8.5.1
Gene names
Name:ECM4
Synonyms:GTO2
Ordered Locus Names:YKR076W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB). May be involved in cell wall organization and biogenesis. Ref.6

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.6

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.6

Subcellular location

Cytoplasm Ref.4 Ref.7.

Induction

Under oxidative stress conditions. By agents such as diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide (t-BOOH) and cadmium in a transcriptional factors YAP1 and/or MSN2/4-dependent manner. Ref.6 Ref.7

Miscellaneous

Present with 1670 molecules/cell in log phase SD medium.

A version of this protein truncated after amino acid 200 is not active in the beta-hydroxyethyl disulfide (HED) assay.

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=1.42 mM for reduced glutathione (GSH) Ref.6

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Glutathione S-transferase omega-like 2
PRO_0000086922

Regions

Domain201 – 353153GST C-terminal

Sites

Active site461Nucleophile Ref.6

Experimental info

Mutagenesis461C → S or Y: Completely inactive as thiol transferase. No activity recovered against 1-chloro-2,4-dinitrobenzene (CDNB). Ref.6
Mutagenesis511R → A: No effect on thiol transferase activity. No effect on thiol transferase activity; when associated with D-173. Ref.6
Mutagenesis1731E → A or D: No effect on thiol transferase activity. Ref.6
Mutagenesis1741S → A: No effect on thiol transferase activity. Ref.6
Mutagenesis2461L → A: No effect on thiol transferase activity. Ref.6
Mutagenesis2801G → L: No effect on thiol transferase activity. Ref.6
Mutagenesis2871D → G: Abolishes thiol transferase activity. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P36156 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 2ED6659ADD4CA6ED

FASTA37043,274
        10         20         30         40         50         60 
MSKQWASGTN GAFKRQVSSF RETISKQHPI YKPAKGRYWL YVSLACPWAH RTLITRALKG 

        70         80         90        100        110        120 
LTSVIGCSVV HWHLDEKGWR FLDMEKQLED SEDFLEHWHD VAGGIRTAKE DSSKSFAEIK 

       130        140        150        160        170        180 
NDSQRFMVDA TNEPHYGYKR ISDLYYKSDP QYSARFTVPV LWDLETQTIV NNESSEIIRI 

       190        200        210        220        230        240 
LNSSAFDEFV DDDHKKTDLV PAQLKTQIDD FNSWVYDSIN NGVYKTGFAE KAEVYESEVN 

       250        260        270        280        290        300 
NVFEHLDKVE KILSDKYSKL KAKYGEEDRQ KILGEFFTVG DQLTEADIRL YTTVIRFDPV 

       310        320        330        340        350        360 
YVQHFKCNFT SIRAGYPFIH LWVRNLYWNY DAFRYTTDFD HIKLHYTRSH TRINPLGITP 

       370 
LGPKPDIRPL 

« Hide

References

« Hide 'large scale' references
[1]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"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].
[6]"Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases."
Garcera A., Barreto L., Piedrafita L., Tamarit J., Herrero E.
Biochem. J. 398:187-196(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MUTAGENESIS OF CYS-46; ARG-51; GLU-173; SER-174; LEU-246; GLY-280 AND ASP-287.
[7]"A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism."
Barreto L., Garcera A., Jansson K., Sunnerhagen P., Herrero E.
Eukaryot. Cell 5:1748-1759(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z28301 Genomic DNA. Translation: CAA82155.1.
BK006944 Genomic DNA. Translation: DAA09226.1.
PIRS38153.
RefSeqNP_013002.3. NM_001179866.3.

3D structure databases

ProteinModelPortalP36156.
SMRP36156. Positions 10-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34207. 8 interactions.
MINTMINT-4493799.
STRING4932.YKR076W.

Proteomic databases

PaxDbP36156.
PeptideAtlasP36156.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKR076W; YKR076W; YKR076W.
GeneID853951.
KEGGsce:YKR076W.

Organism-specific databases

CYGDYKR076w.
SGDS000001784. ECM4.

Phylogenomic databases

eggNOGCOG0435.
GeneTreeENSGT00530000065151.
HOGENOMHOG000245143.
KOK07393.
OMAVCPWATR.
OrthoDBEOG722JK6.

Enzyme and pathway databases

BioCycYEAST:G3O-32040-MONOMER.
SABIO-RKP36156.

Gene expression databases

GenevestigatorP36156.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 2 hits.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR016639. GST.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR32419. PTHR32419. 1 hit.
PfamPF13409. GST_N_2. 1 hit.
[Graphical view]
PIRSFPIRSF015753. GST. 1 hit.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 2 hits.
PROSITEPS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975356.

Entry information

Entry nameGTO2_YEAST
AccessionPrimary (citable) accession number: P36156
Secondary accession number(s): D6VXD6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 19, 2014
This is version 114 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 XI

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

Yeast

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

SIMILARITY comments

Index of protein domains and families