Q05926 (GLRX8_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-8

Alternative name(s):
Glutathione-dependent oxidoreductase 8

Gene names

Name:	GRX8
Ordered Locus Names:	YLR364W

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	109 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Ref.7 Ref.8
Subunit structure	Monomer. Ref.8
Subcellular location	Cytoplasm Ref.4.
Induction	Strongly induced by the exposure to arsenic which causes glutathione depletion. Ref.6
Miscellaneous	Present with 573 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.4. Source: SGD
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from direct assay Ref.8. 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
	Chain	1 – 109	109	Glutaredoxin-8		PRO_0000268192
Regions
	Domain	5 – 109	105	Glutaredoxin
Amino acid modifications
	Disulfide bond	25 ↔ 28		Redox-active Probable
Experimental info
	Mutagenesis	25	1	C → S: Impairs activity. Ref.8
	Mutagenesis	28	1	C → S: Impairs activity. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q05926 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3353EFB47A61574A	FASTA	109	12,519
	10 20 30 40 50 60 MSAFVTKAEE MIKSHPYFQL SASWCPDCVY ANSIWNKLNV QDKVFVFDIG SLPRNEQEKW 70 80 90 100 RIAFQKVVGS RNLPTIVVNG KFWGTESQLH RFEAKGTLEE ELTKIGLLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[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]	"Integrating phenotypic and expression profiles to map arsenic-response networks." Haugen A.C., Kelley R., Collins J.B., Tucker C.J., Deng C., Afshari C.A., Brown J.M., Ideker T., Van Houten B. Genome Biol. 5:R95.1-R95.18(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance." Mesecke N., Spang A., Deponte M., Herrmann J.M. Mol. Biol. Cell 19:2673-2680(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux." Eckers E., Bien M., Stroobant V., Herrmann J.M., Deponte M. Biochemistry 48:1410-1423(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-25 AND CYS-28.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U19103 Genomic DNA. Translation: AAB67570.1. AY558221 Genomic DNA. Translation: AAS56547.1. BK006945 Genomic DNA. Translation: DAA09669.1.
PIR	S51382.
RefSeq	NP_013468.3. NM_001182253.3.
3D structure databases
ProteinModelPortal	Q05926.
SMR	Q05926. Positions 2-98.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05926. 1 interaction.
STRING	4932.YLR364W.
Proteomic databases
PaxDb	Q05926.
PeptideAtlas	Q05926.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR364W; YLR364W; YLR364W.
GeneID	851079.
KEGG	sce:YLR364W. sce:YLR368W.
Organism-specific databases
CYGD	YLR364w.
SGD	S000004356. GRX8.
Phylogenomic databases
eggNOG	COG0695.
KO	K15070.
OMA	WCPDCVY.
OrthoDB	EOG43V358.
Gene expression databases
Genevestigator	Q05926.
GermOnline	YLR364W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.30.10. 1 hit.
InterPro	IPR002109. Glutaredoxin. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. False negative. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967738.

Entry information

Entry name

GLRX8_YEAST

Accession

Primary (citable) accession number: Q05926
Secondary accession number(s): D6VZ03

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program