Reviewed, UniProtKB/Swiss-Prot P17695 (GLRX2_YEAST)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-2, mitochondrial
Alternative name(s):
    Thioltransferase
    Glutathione-dependent oxidoreductase 2

Gene names

Name:	GRX2
Synonyms:	TTR, TTR1
Ordered Locus Names:	YDR513W
ORF Names:	D9719.17

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Ref.5 Ref.8 Ref.9
Subcellular location	Cytoplasm. Mitochondrion. Note: Two forms, a long and a short one are found in the mitochondrion, but only the short one is detected in the cytoplasm. Ref.7
Induction	In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase. Ref.5 Ref.6
Miscellaneous	Present with 31400 molecules/cell in log phase SD medium. Ref.10 It is unclear whether the long polypeptide observed in mitochondria represents the immature form of the protein before cleavage of the transit peptide and release of the short form into the cytoplasm or whether two mature isoforms exists.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.
Biophysicochemical properties	Kinetic parameters: KM=2.0 mM for H2O2 KM=2.2 mM for tert-butyl hydroperoxide KM=0.87 mM for cumene hydroperoxide KM=0.17 mM for 1-chloro-2,4-dinitrobenzene KM=0.27 mM for 1,2-dichloro-4-nitrobenzene

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm Mitochondrion
Domain	Redox-active center Transit peptide
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Ref.5 Inferred from direct assay. Source: SGD electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Ref.5 Inferred from mutant phenotype. Source: SGD transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.7 Inferred from direct assay. Source: SGD mitochondrion Ref.7 Inferred from direct assay. Source: SGD
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione peroxidase activity Ref.9 Inferred from direct assay. Source: SGD glutathione transferase activity Ref.9 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERP1	Q05359	1	EBI-7699,EBI-6581
ERV25	P54837	1	EBI-7699,EBI-6642
SPC1	P46965	1	EBI-7699,EBI-17823
SPF1	P39986	1	EBI-7699,EBI-3128
SWP1	Q02795	1	EBI-7699,EBI-12666
YOP1	Q12402	1	EBI-7699,EBI-37092

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion Ref.4
	Chain	36 – 143	108	Glutaredoxin-2, mitochondrial		PRO_0000141612
Regions
	Domain	41 – 143	103	Glutaredoxin
Amino acid modifications
	Modified residue	37	1	Phosphoserine Ref.11
	Modified residue	91	1	Phosphoserine Ref.11
	Modified residue	94	1	Phosphoserine Ref.11
	Modified residue	123	1	Phosphoserine Ref.11
	Disulfide bond	61 ↔ 64		Redox-active

Sequences

	Sequence		Length	Mass (Da)
	P17695-1 [UniParc]. Last modified February 21, 2006. Version 3. Checksum: 99A79B87695B2266	FASTA	143	15,861
	10 20 30 40 50 60 METNFSFDSN LIVIIIITLF ATRIIAKRFL STPKMVSQET VAHVKDLIGQ KEVFVAAKTY 70 80 90 100 110 120 CPYCKATLST LFQELNVPKS KALVLELDEM SNGSEIQDAL EEISGQKTVP NVYINGKHIG 130 140 GNSDLETLKK NGKLAEILKP VFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a gene encoding yeast thioltransferase." Gan Z.-R. Biochem. Biophys. Res. Commun. 187:949-955(1992) [PubMed: 1530649] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DMY6.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete amino acid sequence of yeast thioltransferase (glutaredoxin)." Gan Z.-R., Polokoff M.A., Jacobs J.W., Sardana M.K. Biochem. Biophys. Res. Commun. 168:944-951(1990) [PubMed: 2189409] [Abstract] Cited for: PROTEIN SEQUENCE OF 36-141.
[5]	"The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species." Luikenhuis S., Perrone G., Dawes I.W., Grant C.M. Mol. Biol. Cell 9:1081-1091(1998) [PubMed: 9571241] [Abstract] Cited for: FUNCTION, INDUCTION.
[6]	"Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae." Grant C.M., Luikenhuis S., Beckhouse A., Soderbergh M., Dawes I.W. Biochim. Biophys. Acta 1490:33-42(2000) [PubMed: 10786615] [Abstract] Cited for: INDUCTION.
[7]	"Two isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartments." Pedrajas J.R., Porras P., Martinez-Galisteo E., Padilla C.A., Miranda-Vizuete A., Barcena J.A. Biochem. J. 364:617-623(2002) [PubMed: 11958675] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"The yeast glutaredoxins are active as glutathione peroxidases." Collinson E.J., Wheeler G.L., Garrido E.O., Avery A.M., Avery S.V., Grant C.M. J. Biol. Chem. 277:16712-16717(2002) [PubMed: 11875065] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Role of yeast glutaredoxins as glutathione S-transferases." Collinson E.J., Grant C.M. J. Biol. Chem. 278:22492-22497(2003) [PubMed: 12684511] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-91; SER-94 AND SER-123, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

S45268 Genomic DNA. Translation: AAB23389.1. Different initiation.
U33057 Genomic DNA. Translation: AAB64953.1.
AY692896 Genomic DNA. Translation: AAT92915.1.

PIR

GDBY. S69570.

RefSeq

NP_010801.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CTF	X-ray	2.10	A	35-143	[»]
3CTG	X-ray	1.50	A	35-143	[»]
3D4M	X-ray	2.05	A	35-143	[»]
3D5J	X-ray	1.91	A/B	35-143	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5271N.

IntAct

P17695. 9 interactions.

Proteomic databases

PeptideAtlas

P17695.

Genome annotation databases

Ensembl

YDR513W. Saccharomyces cerevisiae. [Contig view]

GeneID

852124.

GenomeReviews

Gene locus YDR513W in contig Z71256_GR.

KEGG

sce:YDR513W.

NMPDR

fig|4932.3.peg.1575.

Organism-specific databases

CYGD

YDR513w.

SGD

S000002921. GRX2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P17695.

OMA

P17695. LELDEMS.

Gene expression databases

GermOnline

YDR513W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_sub.
IPR011899. GRX_euk.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00462. Glutaredoxin. 1 hit.
[Graphical view]

PRINTS

PR00160. GLUTAREDOXIN.

TIGRFAMs

TIGR02180. GRX_euk. 1 hit.

PROSITE

PS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

970510.

Entry information

Entry name

GLRX2_YEAST

Accession

Primary (citable) accession number: P17695
Secondary accession number(s): Q6B234

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 21, 2006
Last modified:	June 16, 2009
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)