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Protein

Glutaredoxin-2, mitochondrial

Gene

GLRX2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Enzyme regulationi

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive formBy similarity
Binding sitei68 – 681GlutathioneBy similarity
Binding sitei103 – 1031GlutathioneBy similarity
Binding sitei115 – 1151Glutathione; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi147 – 1471Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive formBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. response to hydrogen peroxide Source: Ensembl
  3. response to organic substance Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-2, mitochondrial
Gene namesi
Name:GLRX2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 16

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1818MitochondrionSequence AnalysisAdd
BLAST
Chaini19 – 157139Glutaredoxin-2, mitochondrialPRO_0000326628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi71 ↔ 74Redox-active; alternateBy similarity
Modified residuei71 – 711S-glutathionyl cysteine; alternateBy similarity

Keywords - PTMi

Disulfide bond, Glutathionylation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021249.

Structurei

3D structure databases

ProteinModelPortaliQ32L67.
SMRiQ32L67. Positions 43-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 151101GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0695.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ32L67.
KOiK03676.
OMAiNYTAVEL.
OrthoDBiEOG7QRQWZ.
TreeFamiTF319627.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q32L67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYWRRAALVG TRLIPVRSSS AGRLEGPAGI SGSGMGNSTS SSLGNAATAP
60 70 80 90 100
VNQIQETISN NCVVIFSKTS CSYCTMAKNL FHDMNVNYKV VELDMLEYGS
110 120 130 140 150
QFQDALHKMT GERTVPRIFV NGTFIGGATD THRLHKEGKL LPLVHQCHLK

NSKREEL
Length:157
Mass (Da):17,202
Last modified:December 5, 2005 - v1
Checksum:i3106F9214733EFD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109742 mRNA. Translation: AAI09743.1.
RefSeqiNP_001035613.1. NM_001040523.2.
XP_005216824.1. XM_005216767.2.
XP_010811391.1. XM_010813089.1.
UniGeneiBt.27603.

Genome annotation databases

EnsembliENSBTAT00000021249; ENSBTAP00000021249; ENSBTAG00000015972.
GeneIDi513762.
KEGGibta:513762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109742 mRNA. Translation: AAI09743.1.
RefSeqiNP_001035613.1. NM_001040523.2.
XP_005216824.1. XM_005216767.2.
XP_010811391.1. XM_010813089.1.
UniGeneiBt.27603.

3D structure databases

ProteinModelPortaliQ32L67.
SMRiQ32L67. Positions 43-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021249; ENSBTAP00000021249; ENSBTAG00000015972.
GeneIDi513762.
KEGGibta:513762.

Organism-specific databases

CTDi51022.

Phylogenomic databases

eggNOGiCOG0695.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG096801.
InParanoidiQ32L67.
KOiK03676.
OMAiNYTAVEL.
OrthoDBiEOG7QRQWZ.
TreeFamiTF319627.

Miscellaneous databases

NextBioi20871016.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiGLRX2_BOVIN
AccessioniPrimary (citable) accession number: Q32L67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 7, 2008
Last sequence update: December 5, 2005
Last modified: March 3, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.