Q9CQM5 · TXD17_MOUSE

  • Protein
    Thioredoxin domain-containing protein 17
  • Gene
    Txndc17
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide (By similarity).

Features

Showing features for active site, site.

1123102030405060708090100110120
TypeIDPosition(s)Description
Active site43Nucleophile
Site44Contributes to redox potential value
Site45Contributes to redox potential value
Active site46Nucleophile

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
Molecular Functionperoxidase activity
Molecular Functionprotein-disulfide reductase (NAD(P)H) activity
Biological Processtumor necrosis factor-mediated signaling pathway

Names & Taxonomy

Protein names

  • Recommended name
    Thioredoxin domain-containing protein 17
  • Alternative names
    • 14 kDa thioredoxin-related protein (TRP14)
    • Protein 42-9-9
    • Thioredoxin-like protein 5

Gene names

    • Name
      Txndc17
    • Synonyms
      Txnl5

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9CQM5
  • Secondary accessions
    • Q3TE14
    • Q921A9
    • Q9D0Y4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001200232-123Thioredoxin domain-containing protein 17
Disulfide bond43↔46Redox-active

Post-translational modification

The oxidized protein is reduced by TRXR1.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with TRXR1 and DYNLL1/DNCL1.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-123Thioredoxin

Sequence similarities

Belongs to the thioredoxin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    123
  • Mass (Da)
    14,015
  • Last updated
    2001-06-01 v1
  • Checksum
    763689BCCAABD8ED
MATFEEVSVLGFEEFDKAVKEHEGKTIFAYFSGSKDTEGKSWCPDCVEAEPVIREGLKHVTEDCVFIYCQVGDKPYWKDPNNDFRQKLKITAVPTLLKYGTPQKLVESECCQSSLVEMIFSED

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict22in Ref. 2; BAE41434
Sequence conflict24in Ref. 2; BAB23225
Sequence conflict40in Ref. 1; CAC51438
Sequence conflict76in Ref. 2; BAE41434

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ344103
EMBL· GenBank· DDBJ
CAC51438.1
EMBL· GenBank· DDBJ
mRNA
AK004219
EMBL· GenBank· DDBJ
BAB23225.1
EMBL· GenBank· DDBJ
mRNA
AK007595
EMBL· GenBank· DDBJ
BAB25126.1
EMBL· GenBank· DDBJ
mRNA
AK013103
EMBL· GenBank· DDBJ
BAB28648.1
EMBL· GenBank· DDBJ
mRNA
AK076425
EMBL· GenBank· DDBJ
BAC36336.1
EMBL· GenBank· DDBJ
mRNA
AK169882
EMBL· GenBank· DDBJ
BAE41434.1
EMBL· GenBank· DDBJ
mRNA
BX119911
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC030344
EMBL· GenBank· DDBJ
AAH30344.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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