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Q32L67 (GLRX2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutaredoxin-2, mitochondrial
Gene names
Name:GLRX2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release By similarity.

Enzyme regulation

The 2Fe-2S present in the homodimer leads to inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the presence of one-electron oxidants or reductants leading to the loss of the 2Fe-2S cluster, subsequent monomerization and activation of the enzyme By similarity.

Subunit structure

Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster By similarity.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the glutaredoxin family.

Contains 1 glutaredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1818Mitochondrion Potential
Chain19 – 157139Glutaredoxin-2, mitochondrial
PRO_0000326628

Regions

Domain51 – 151101Glutaredoxin

Sites

Metal binding621Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
Metal binding1471Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
Binding site681Glutathione By similarity
Binding site1031Glutathione By similarity
Binding site1151Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue711S-glutathionyl cysteine; alternate By similarity
Disulfide bond71 ↔ 74Redox-active; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q32L67 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 3106F9214733EFD1

FASTA15717,202
        10         20         30         40         50         60 
MYWRRAALVG TRLIPVRSSS AGRLEGPAGI SGSGMGNSTS SSLGNAATAP VNQIQETISN 

        70         80         90        100        110        120 
NCVVIFSKTS CSYCTMAKNL FHDMNVNYKV VELDMLEYGS QFQDALHKMT GERTVPRIFV 

       130        140        150 
NGTFIGGATD THRLHKEGKL LPLVHQCHLK NSKREEL 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC109742 mRNA. Translation: AAI09743.1.
RefSeqNP_001035613.1. NM_001040523.2.
XP_005216824.1. XM_005216767.1.
UniGeneBt.27603.

3D structure databases

ProteinModelPortalQ32L67.
SMRQ32L67. Positions 43-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000021249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000021249; ENSBTAP00000021249; ENSBTAG00000015972.
GeneID513762.
KEGGbta:513762.

Organism-specific databases

CTD51022.

Phylogenomic databases

eggNOGCOG0695.
GeneTreeENSGT00390000003677.
HOGENOMHOG000095204.
HOVERGENHBG096801.
InParanoidQ32L67.
KOK03676.
OMAGMESNTS.
OrthoDBEOG7QRQWZ.
TreeFamTF319627.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR015450. Grx-2.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR10168:SF17. PTHR10168:SF17. 1 hit.
PfamPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSPR00160. GLUTAREDOXIN.
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR02180. GRX_euk. 1 hit.
PROSITEPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20871016.

Entry information

Entry nameGLRX2_BOVIN
AccessionPrimary (citable) accession number: Q32L67
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families