Q93379 · GSHR_CAEEL
- ProteinGlutathione reductase, mitochondrial
- Genegsr-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids473 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Maintains high levels of reduced glutathione in the cytosol (PubMed:23593298).
Involved in resistance to oxidative stress and starvation (PubMed:23593298).
Together with thioredoxin reductase txtr-1, required for the reduction of disulfide groups in the cuticle during molting (PubMed:21199936).
Involved in resistance to oxidative stress and starvation (PubMed:23593298).
Together with thioredoxin reductase txtr-1, required for the reduction of disulfide groups in the cuticle during molting (PubMed:21199936).
Catalytic activity
- 2 glutathione + NADP+ = glutathione disulfide + H+ + NADPH
Cofactor
Note: Binds 1 FAD per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
34.1 μM | glutathione disulfide | 25 | ||||
12.9 μM | NADPH | 25 |
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | glutathione-disulfide reductase (NADPH) activity | |
Molecular Function | NADP binding | |
Biological Process | cell redox homeostasis | |
Biological Process | cellular response to oxidative stress | |
Biological Process | ecdysis, collagen and cuticulin-based cuticle | |
Biological Process | glutathione metabolic process | |
Biological Process | response to superoxide |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione reductase, mitochondrial
- EC number
- Short namesGR
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionQ93379
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown causes a severe decrease in survival upon treatment with oxidants including juglone, paraquat and to a lesser extent, cumen and tert-butylhydroperoxide (tBOOH). Enhances further the production of gamma-glutamylycysteine and glutathione disulfide upon juglone treatment. Increases gst-4 and gcs-1 expression. Reduces lifespan (PubMed:23593298).
RNAi-mediated knockdown in a trxr-1 mutant background causes an arrest during larval molting characterized by a partial detachment of the old cuticle and an impaired ability to reduce cuticle components (PubMed:21199936).
RNAi-mediated knockdown in a trxr-1 mutant background causes an arrest during larval molting characterized by a partial detachment of the old cuticle and an impaired ability to reduce cuticle components (PubMed:21199936).
PTM/Processing
Features
Showing features for chain, transit peptide, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000436306 | ?-473 | Glutathione reductase, mitochondrial | |||
Sequence: MLRFRCILSTSRSIMSGVKEFDYLVIGGGSGGIASARRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIPNIKGAEHGIDSDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETNPLHLHKNTQVTEVIKGDDGLLTIKTTTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGETDNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMRGGVKPE | ||||||
Transit peptide | 1-? | Mitochondrion | ||||
Disulfide bond | 58↔63 | Redox-active | ||||
Sequence: CVNVGC |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Expressed at all larval stages and in adults in intestine, vulva muscle, pharynx and some cells in the tail.
Induction
Induced by the oxidant juglone and starvation.
Gene expression databases
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q93379-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Namea
- Length473
- Mass (Da)51,467
- Last updated1998-08-01 v2
- ChecksumE1DAA50758109D80
Q93379-2
- Nameb
- Differences from canonical
- 1-14: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058343 | 1-14 | in isoform b | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284603 EMBL· GenBank· DDBJ | CAB03763.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284603 EMBL· GenBank· DDBJ | CAD88214.1 EMBL· GenBank· DDBJ | Genomic DNA |