P70619 · GSHR_RAT

  • Protein
    Glutathione reductase
  • Gene
    Gsr
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activity

Cofactor

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD per subunit.

Features

Showing features for active site.

142450100150200250300350400
TypeIDPosition(s)Description
Active site413Proton acceptor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentexternal side of plasma membrane
Cellular Componentmitochondrion
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionglutathione binding
Molecular Functionglutathione-disulfide reductase (NADPH) activity
Molecular Functionidentical protein binding
Molecular FunctionNADP binding
Biological Processcell redox homeostasis
Biological Processcellular response to oxidative stress
Biological Processglutathione metabolic process
Biological Processresponse to activity
Biological Processresponse to cadmium ion
Biological Processresponse to ethanol
Biological Processresponse to iron(III) ion
Biological Processresponse to ischemia
Biological Processresponse to nicotine
Biological Processresponse to oxidative stress
Biological Processresponse to vitamin A
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione reductase
  • EC number
  • Short names
    GR; GRase

Gene names

    • Name
      Gsr

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P70619

Proteomes

Organism-specific databases

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000679571-424Glutathione reductase
Disulfide bond32Interchain

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer; disulfide-linked.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    424
  • Mass (Da)
    46,301
  • Last updated
    2004-07-05 v2
  • Checksum
    0714FF531F90BEBA
VNVGCVPKKVMWNTAVHSEFIHDHVDYGFQNCKSKFNWHVIKEKRDAYVSRLNNIYQNNLTKSHIEVIHGYATFRDGPQPTAEVNGKKFTAPHILIATGGVPTVPHENQIPGASLGITSDGFFQLEDLPSRSVIVGAGYIAVEIAGILSALGSKTSLMIRHDKVLRSFDSLISSNCTEELENAGGVEVLTVKKFSQVKEVKKTSSGLELHVVTALPGRKPTVTTIPDVDCLLWAIGRDPNSKGLNLNKLGIQTDDKGHILVDEFQNTNVKGVYAVGDVCGKALLTPVAIAAGRKLAHRLFEGKEDSRLDYDNIPTVVFSHPPIGTVGLTEDEAVHKYGKDNVKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGATKADFDNRVAIHPTSSEELVTLR

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0G2JU71A0A0G2JU71_RATGsr415
A0A8I6A0A3A0A8I6A0A3_RATGsr502
F1LRE1F1LRE1_RATGsr422

Sequence caution

The sequence AAB18132.1 differs from that shown. Reason: Frameshift

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U73174
EMBL· GenBank· DDBJ
AAB18132.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

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