TXNRD1 (TRXR1)

Isoform 1 of TXNRD1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 of TXNRD1 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 of TXNRD1 also mediates cell death induced by a combination of interferon-beta and retinoic acid.

TXNRD1 (TRXR1) Related Areas

Enzyme>>Oxidoreductase>>TXNRD1/TRXR1

TXNRD1 (TRXR1) Alternative Names

TXNRD1, TRXR1, GRIM-12, MGC9145, TR, TR1, TXNR [Homo sapiens]

Txnrd1, TrxR1, TR, TR1 [Mus musculus]

Summaries for TXNRD1 (TRXR1)

Entrez Gene summary for TXNRD1 (TRXR1):

TXNRD1 gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms. [provided by RefSeq, Jul 2008]

Wikipedia summary for TXNRD1 (TRXR1):

Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene.
This gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms.

Human TXNRD1 (TRXR1) Protein General Information

 

• Protein names: Thioredoxin reductase 1, cytoplasmic
  Short name=TXNRD1
• Sequence length: 649 AA.
• Domain: The N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays.
• Sequence similarities: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
  Contains 1 glutaredoxin domain.
• Post-translational modification: The N-terminus of isoform 5 is blocked.
  ISGylated .
• Subunit structure: Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5.
• Subcellular location: Cytoplasm
  Isoform 4: Cytoplasm. Nucleus .
  Isoform 5: Cytoplasm
• Tissue specificity: Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver.
• Catalytic activity: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
• Cofactor: Binds 1 FAD per subunit.
• Induction: Isoform 5 is induced by a combination of interferon-beta and retinoic acid (at protein level). Isoform 1 is induced by estradiol or testosterone in HeLa cells.
• Miscellaneous: The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.
• Sequence caution: The sequence AAB35418.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence AAC69621.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence AAF15900.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence AAV38446.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence AAZ67916.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence BAA13674.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence CAA04503.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence CAA62629.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
  The sequence CAG38744.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

General information above from UniProt

Function for TXNRD1 (TRXR1) Protein

UniProtKB:

Isoform 1 of TXNRD1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 of TXNRD1 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 of TXNRD1 also mediates cell death induced by a combination of interferon-beta and retinoic acid.

Genatlas:

• TXNRD1 is key enzyme in the regulation of the intracellular redox environment

Homology for human TXNRD1 (TRXR1)

• homolog to chimpanzee TXNRD1 (99.60 pc)
• homolog to rattus Txnrd1 (90.78 pc)
• homolog to murine Txnrd1 (91.58 pc)
• homolog to chicken TXNRD1 (85.31 pc)

Drugs for TXNRD1 (TRXR1)

Target	Drug Name	Disease	Drug Status
TXNRD1 (TRXR1)	Auranofin	Inflammatory arthritis	Approved

Drugs for TXNRD1 (TRXR1) from TTD (Therapeutic Targets Database)