P17695 (GLRX2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-2, mitochondrial

Alternative name(s):
Glutathione-dependent oxidoreductase 2
Thioltransferase

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [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.6 Ref.9 Ref.10
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.8
Induction	In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase. Ref.6 Ref.7
Miscellaneous	Present with 31400 molecules/cell in log phase SD medium. Ref.11 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 Ref.9 Ref.10 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
Sequence caution	The sequence AAB23389.1 differs from that shown. Reason: Erroneous initiation.

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 Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from mutant phenotype. Source: SGD cellular response to oxidative stress Inferred from mutant phenotype Ref.6. Source: SGD electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay Ref.8. Source: SGD mitochondrion Inferred from direct assay Ref.8. Source: SGD
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione peroxidase activity Inferred from direct assay Ref.10. Source: SGD glutathione transferase activity Inferred from direct assay Ref.10. Source: SGD protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

35

Mitochondrion Ref.5

Chain

36 – 143

108

Glutaredoxin-2, mitochondrial

PRO_0000141612

Regions

Domain

41 – 143

103

Glutaredoxin

Amino acid modifications

Modified residue

37

1

Phosphoserine Ref.12

Modified residue

91

1

Phosphoserine Ref.12

Modified residue

94

1

Phosphoserine Ref.12

Modified residue

123

1

Phosphoserine Ref.12

Disulfide bond

61 ↔ 64

Redox-active

Secondary structure

1

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143

Helix Strand Turn

Details...

Helix

38 – 47

10

Beta strand

52 – 57

6

Helix

62 – 72

11

Helix

79 – 81

3

Beta strand

82 – 86

5

Helix

87 – 89

3

Helix

95 – 103

9

Beta strand

111 – 114

4

Helix

123 – 130

8

Helix

134 – 137

4

Turn

138 – 141

4

Sequences

	Sequence		Length	Mass (Da)
	P17695 [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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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].
[12]	"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

EMBL
GenBank
DDBJ

S45268 Genomic DNA. Translation: AAB23389.1. Different initiation.
U33057 Genomic DNA. Translation: AAB64953.1.
AY692896 Genomic DNA. Translation: AAT92915.1.
BK006938 Genomic DNA. Translation: DAA12344.1.

PIR

GDBY. S69570.

RefSeq

NP_010801.1. NM_001180821.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P17695.

SMR

P17695. Positions 36-143.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5271N.

IntAct

P17695. 7 interactions.

MINT

MINT-568234.

STRING

P17695.

Proteomic databases

PeptideAtlas

P17695.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR513W; YDR513W; YDR513W.

GeneID

852124.

KEGG

sce:YDR513W.

NMPDR

fig|4932.3.peg.1575.

Organism-specific databases

CYGD

YDR513w.

SGD

S000002921. GRX2.

Phylogenomic databases

eggNOG

fuNOG12136.

GeneTree

EFGT00050000002871.

HOGENOM

HBG728471.

OMA

CRRAKAV.

OrthoDB

EOG4V1B9J.

Gene expression databases

ArrayExpress

P17695.

Genevestigator

P17695.

GermOnline

YDR513W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00462. Glutaredoxin. 1 hit.
[Graphical view]

PRINTS

PR00160. GLUTAREDOXIN.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

TIGRFAMs

TIGR02180. GRX_euk. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

NextBio

970510.

Entry information

Entry name

GLRX2_YEAST

Accession

Primary (citable) accession number: P17695
Secondary accession number(s): D6VTD4, Q6B234

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	February 21, 2006
Last modified:	December 14, 2011
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program