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Protein

Glutaredoxin-8

Gene

GRX8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. glutathione-disulfide reductase activity Source: SGD
  3. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32435-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-8
Alternative name(s):
Glutathione-dependent oxidoreductase 8
Gene namesi
Name:GRX8
Ordered Locus Names:YLR364W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR364w.
SGDiS000004356. GRX8.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251C → S: Impairs activity. 1 Publication
Mutagenesisi28 – 281C → S: Impairs activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109109Glutaredoxin-8PRO_0000268192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi25 ↔ 28Redox-activeCurated

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ05926.
PaxDbiQ05926.
PeptideAtlasiQ05926.

Expressioni

Inductioni

Strongly induced by the exposure to arsenic which causes glutathione depletion.1 Publication

Gene expression databases

GenevestigatoriQ05926.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi31626. 2 interactions.
IntActiQ05926. 1 interaction.
MINTiMINT-4496129.
STRINGi4932.YLR364W.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1410Combined sources
Beta strandi17 – 215Combined sources
Helixi28 – 3811Combined sources
Turni41 – 433Combined sources
Beta strandi44 – 485Combined sources
Helixi54 – 6714Combined sources
Beta strandi72 – 787Combined sources
Beta strandi81 – 844Combined sources
Helixi86 – 9510Combined sources
Helixi98 – 1047Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M80NMR-A1-109[»]
ProteinModelPortaliQ05926.
SMRiQ05926. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 109105GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0695.
InParanoidiQ05926.
OMAiRKWVPTI.
OrthoDBiEOG7JMGSQ.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q05926-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAFVTKAEE MIKSHPYFQL SASWCPDCVY ANSIWNKLNV QDKVFVFDIG
60 70 80 90 100
SLPRNEQEKW RIAFQKVVGS RNLPTIVVNG KFWGTESQLH RFEAKGTLEE

ELTKIGLLP
Length:109
Mass (Da):12,519
Last modified:November 1, 1996 - v1
Checksum:i3353EFB47A61574A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19103 Genomic DNA. Translation: AAB67570.1.
AY558221 Genomic DNA. Translation: AAS56547.1.
BK006945 Genomic DNA. Translation: DAA09669.1.
PIRiS51382.
RefSeqiNP_013468.3. NM_001182253.3.

Genome annotation databases

EnsemblFungiiYLR364W; YLR364W; YLR364W.
GeneIDi851079.
KEGGisce:YLR364W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19103 Genomic DNA. Translation: AAB67570.1.
AY558221 Genomic DNA. Translation: AAS56547.1.
BK006945 Genomic DNA. Translation: DAA09669.1.
PIRiS51382.
RefSeqiNP_013468.3. NM_001182253.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M80NMR-A1-109[»]
ProteinModelPortaliQ05926.
SMRiQ05926. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31626. 2 interactions.
IntActiQ05926. 1 interaction.
MINTiMINT-4496129.
STRINGi4932.YLR364W.

Proteomic databases

MaxQBiQ05926.
PaxDbiQ05926.
PeptideAtlasiQ05926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR364W; YLR364W; YLR364W.
GeneIDi851079.
KEGGisce:YLR364W.

Organism-specific databases

CYGDiYLR364w.
SGDiS000004356. GRX8.

Phylogenomic databases

eggNOGiCOG0695.
InParanoidiQ05926.
OMAiRKWVPTI.
OrthoDBiEOG7JMGSQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-32435-MONOMER.

Miscellaneous databases

NextBioi967738.

Gene expression databases

GenevestigatoriQ05926.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. 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.

Entry informationi

Entry nameiGLRX8_YEAST
AccessioniPrimary (citable) accession number: Q05926
Secondary accession number(s): D6VZ03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 573 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.