P36156 (GTO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cytoplasm
Molecular function	Oxidoreductase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from sequence or structural similarity Ref.6. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.4Ref.7. Source: SGD
Molecular_function	glutathione dehydrogenase (ascorbate) activity Inferred from electronic annotation. Source: EC glutathione transferase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Glutathione S-transferase omega-like 2		PRO_0000086922
Regions
	Domain	201 – 353	153	GST C-terminal
Sites
	Active site	46	1	Nucleophile Ref.6
Experimental info
	Mutagenesis	46	1	C → S or Y: Completely inactive as thiol transferase. No activity recovered against 1-chloro-2,4-dinitrobenzene (CDNB). Ref.6
	Mutagenesis	51	1	R → A: No effect on thiol transferase activity. No effect on thiol transferase activity; when associated with D-173. Ref.6
	Mutagenesis	173	1	E → A or D: No effect on thiol transferase activity. Ref.6
	Mutagenesis	174	1	S → A: No effect on thiol transferase activity. Ref.6
	Mutagenesis	246	1	L → A: No effect on thiol transferase activity. Ref.6
	Mutagenesis	280	1	G → L: No effect on thiol transferase activity. Ref.6
	Mutagenesis	287	1	D → G: Abolishes thiol transferase activity. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P36156 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 2ED6659ADD4CA6ED	FASTA	370	43,274
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[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.
PIR	S38153.
RefSeq	NP_013002.3. NM_001179866.3.
3D structure databases
ProteinModelPortal	P36156.
SMR	P36156. Positions 10-370.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4493799.
STRING	4932.YKR076W.
Proteomic databases
PaxDb	P36156.
PeptideAtlas	P36156.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YKR076W; YKR076W; YKR076W.
GeneID	853951.
KEGG	sce:YKR076W.
Organism-specific databases
CYGD	YKR076w.
SGD	S000001784. ECM4.
Phylogenomic databases
eggNOG	COG0435.
GeneTree	ENSGT00530000065151.
HOGENOM	HOG000245143.
KO	K07393.
OMA	EDANDAH.
OrthoDB	EOG4617CM.
Enzyme and pathway databases
BioCyc	YEAST:G3O-32040-MONOMER.
SABIO-RK	P36156.
Gene expression databases
Genevestigator	P36156.
GermOnline	YKR076W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 2 hits.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR016639. GST. IPR012336. Thioredoxin-like_fold. [Graphical view]
PANTHER	PTHR32419. PTHR32419. 1 hit.
PIRSF	PIRSF015753. GST. 1 hit.
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975356.

Entry information

Entry name

GTO2_YEAST

Accession

Primary (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:	May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program