TXNDC17 (TRP14, TXNL5)

Thioredoxin domain-containing protein 17, also known as TXNDC17, TRP14, and TXNL5, is a protein belonging to the thioredoxin superfamily. TXNDC17 is one of the proteins containing thioredoxin domains. Members of this superfamily share similarity of possessing a thioredoxin fold with a consensus active-site sequence (CxxC) and have functions in redox regulation, defense against oxidative stress, regulation of transcription factors, and refolding of disulfide-containing proteins. Thioredoxins are small disulfide-containing redox proteins found in all livings. It serves as a general protein disulfide oxidoreductase.

TXNDC17 (TRP14, TXNL5) Related Areas

Enzyme>>Oxidoreductase>> TXNDC17

TXNDC17 (TRP14, TXNL5) Alternative Names

MGC14353, TRP14, TXNL5[Homo sapiens]

RP23-207N15.4, 4831443O22Rik, D11Ertd672e, TRP14, Txnl5[Mus musculus]

Human TXNDC17 (TRP14, TXNL5) Protein General Information

 

• Protein names: Thioredoxin domain-containing protein 17
  Short name=TXNDC17
• Sequence length: 123 AA.
• Domain: Redox-active center
• Sequence similarities: Belongs to the thioredoxin family.
  Contains 1 thioredoxin domain.
• Post-translational modification: The oxidized protein is reduced by TRXR1.
• Subunit structure: Interacts with TRXR1 and DYNLL1/DNCL1.
• Subcellular location: Cytoplasm
• Tissue specificity: Ubiquitously expressed in cell lines.

General information above from UniProt

Function for TXNDC17 (TRP14, TXNL5) Protein

UniProtKB:

TXNDC17 is disulfide reductase. TXNDC17 may participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. TXNDC17 modulates TNF-alpha signaling and NF-kappa-B activation. TXNDC17 has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.

Genatlas:

• TXNDC17 is disulfide reductase modulating TNF-alpha signaling pathways