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Trxr1 Thioredoxin reductase 1 [ Drosophila melanogaster (fruit fly) ]

Gene ID: 31760, updated on 6-Jul-2026
Official Symbol
Trxr1provided by FlyBase
Official Full Name
Thioredoxin reductase 1provided by FlyBase
Primary source
FLYBASE:FBgn0020653
Locus tag
Dmel_CG2151
See related
AllianceGenome:FB:FBgn0020653
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Drosophila melanogaster
Lineage
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
Also known as
2151; anon-WO03040301.185; anon-WO03040301.187; CG2151; Dm-TrxR; Dmel\CG2151; DmTR; DmTrx; DmTrxR; dmtrxr-1; DmTrxR-1; DTR; dTrxR; dTXNRD; dTXNRD2; gr; Gr; GR; l(1)G0154; l(1)G0379; l(1)G0477; l(1)G0481; TH; TRR; Trx; Trxr; TrxR; trxr-1; Trxr-1; TrxR-1; trxr1; TrxR1; TRXR1
Summary
Enables protein homodimerization activity and thioredoxin-disulfide reductase (NADPH) activity. Involved in cell redox homeostasis. Located in mitochondrion. Is expressed in adult brain; adult brain cell body rind; adult head; adult heart; and organism. Human ortholog(s) of this gene implicated in familial glucocorticoid deficiency. Orthologous to human TXNRD2 (thioredoxin reductase 2). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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Try the new Transcripts and proteins table
See Trxr1 in Genome Data Viewer
Location:
7D22-7E1; 1-22 cM
Exon count:
7
Annotation release Status Assembly Chr Location
Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) X NC_004354.4 (8242528..8248033)
Release 5.57 previous assembly Release 5 (GCF_000001215.2) X NC_004354.3 (8136561..8142066)

Chromosome X - NC_004354.4Genomic Context describing neighboring genes Neighboring gene stardust Neighboring gene uncharacterized protein Neighboring gene sniffer Neighboring gene NADH dehydrogenase (ubiquinone) 75 kDa subunit Neighboring gene uncharacterized protein Neighboring gene Companion of reaper

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium? Lothrop AP, et al. Biochemistry, 2014 Jan 28. PMID 24393022, Free PMC Article
  2. Molecular organization of the glutathione reductase gene in Drosophila melanogaster. Candas M, et al. Arch Biochem Biophys, 1997 Mar 15. PMID 9056265
  3. The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited. Kanzok SM, et al. J Biol Chem, 2000 Dec 22. PMID 11013257
  4. Selenium in thioredoxin reductase: a mechanistic perspective. Lacey BM, et al. Biochemistry, 2008 Dec 2. PMID 18986163, Free PMC Article
  5. Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Lothrop AP, et al. Biochemistry, 2014 Feb 4. PMID 24490974, Free PMC Article

See all (130) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Overexpression of mitochondrial TXNRD2 in Drosophila melanogaster extended median lifespan in female flies with a small lifespan extension in males; in contrast, overexpression of the cytosolic form, TXNRD1, did not produce a lifespan extension.
    Title: Mitochondrial thioredoxin reductase 2 is elevated in long-lived primate as well as rodent species and extends fly mean lifespan.
  2. Molecular orbital calculations suggested that the C-terminal hexapeptide Pro-Ala-Ser-Cys-Cys-Ser-OH functions as a redox center that alleviates the necessity for selenium in Dm-TrxR.
    Title: Identification and conformer analysis of a novel redox-active motif, Pro-Ala-Ser-Cys-Cys-Ser, in Drosophila thioredoxin reductase by semiempirical molecular orbital calculation.
  3. the role of Glu-469' in catalysis by DmTrxR
    Title: Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster.
  4. rates of steps in both the reductive and the oxidative half-reactions are markedly diminished in H464'Q thioredoxin reductase as compared to those of wild-type enzyme, indicating that His-464' is involved in both half-reactions
    Title: Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster.
  5. changing of His106 to asparagine, glutamine, and phenylalanine in various C-terminal mutants of Drosophila melanogaster thioredoxin reductase drops catalytic activity without change in pH profile
    Title: The conserved histidine 106 of large thioredoxin reductases is likely to have a structural role but not a base catalyst function.
  6. mitochondrial and cytoplasmic variants are both essential for viability
    Title: Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability.
  7. X-ray crystal structure of thioredoxin reductase at 2.4 A resolution; demonstrated that tetrapeptides equivalent to the oxidized C-terminal active sites of both mouse mitochondrial TR (mTR3) and DmTR are substrates for the truncated forms of both enzymes
    Title: Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases.
  8. redox potentials provide direct evidence for proposed catalytic mechanism of DmTrxR, & cast new light on essential role of DmTrx system in cycling GSSG/GSH & maintaining intracellular redox homeostasis in D. melanogaster without glutathione reductase.
    Title: The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila.
  9. analysis of the mechanism of high Mr thioredoxin reductase from Drosophila melanogaster
    Title: The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by FlyBase

Function Evidence Code Pubs
enables antioxidant activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables antioxidant activity NAS
Non-traceable Author Statement
more info
 PubMed 
enables catalytic activity, acting on a protein IEA
Inferred from Electronic Annotation
more info
  
enables flavin adenine dinucleotide binding IEA
Inferred from Electronic Annotation
more info
  
NOT enables glutathione-disulfide reductase (NADPH) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
enables oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables thioredoxin-disulfide reductase (NADPH) activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables thioredoxin-disulfide reductase (NADPH) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables thioredoxin-disulfide reductase (NADPH) activity IEA
Inferred from Electronic Annotation
more info
  
enables thioredoxin-disulfide reductase (NADPH) activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Process Evidence Code Pubs
involved_in cell redox homeostasis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in cell redox homeostasis IEA
Inferred from Electronic Annotation
more info
  
involved_in cell redox homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cellular oxidant detoxification IEA
Inferred from Electronic Annotation
more info
  
involved_in determination of adult lifespan TAS
Traceable Author Statement
more info
 PubMed 
involved_in response to toxic substance IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in mitochondrion IDA
Inferred from Direct Assay
more info
 PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
thioredoxin reductase 1
Names
CG2151-PA
CG2151-PB
CG2151-PC
CG2151-PD
Trxr1-PA
Trxr1-PB
Trxr1-PC
Trxr1-PD
disulfide reductase
glutathione reductase
thioredoxin reductase
thioredoxin reductase-1
NP_001368975.1
NP_511082.2
NP_727251.1
NP_727252.1

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_004354.4 Reference assembly

    Range
    8242528..8248033
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_078527.3 → NP_511082.2  thioredoxin reductase 1, isoform A

    See identical proteins and their annotated locations for NP_511082.2

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P91938
    Related
    FBpp0071115
    Conserved Domains (4) summary
    TIGR01438
    Location:8 → 490
    TGR; thioredoxin and glutathione reductase selenoprotein
    pfam00070
    Location:189 → 263
    Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase
    pfam02852
    Location:363 → 472
    Pyr_redox_dim; Pyridine nucleotide-disulphide oxidoreductase, dimerization domain
    cl21454
    Location:10 → 45
    NADB_Rossmann; Rossmann-fold NAD(P)(+)-binding proteins

  2. NM_167149.2 → NP_727251.1  thioredoxin reductase 1, isoform B

    See identical proteins and their annotated locations for NP_727251.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P91938, Q1RKZ0, Q53YG2, Q961E3, Q9W3H2, Q9W3H3
    Related
    FBpp0071116
    Conserved Domains (4) summary
    TIGR01438
    Location:113 → 595
    TGR; thioredoxin and glutathione reductase selenoprotein
    pfam00070
    Location:294 → 368
    Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase
    pfam02852
    Location:468 → 577
    Pyr_redox_dim; Pyridine nucleotide-disulphide oxidoreductase, dimerization domain
    cl21454
    Location:115 → 150
    NADB_Rossmann; Rossmann-fold NAD(P)(+)-binding proteins

  3. NM_167150.2 → NP_727252.1  thioredoxin reductase 1, isoform C

    See identical proteins and their annotated locations for NP_727252.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P91938
    Related
    FBpp0071117
    Conserved Domains (4) summary
    TIGR01438
    Location:25 → 507
    TGR; thioredoxin and glutathione reductase selenoprotein
    pfam00070
    Location:206 → 280
    Pyr_redox; Pyridine nucleotide-disulphide oxidoreductase
    pfam02852
    Location:380 → 489
    Pyr_redox_dim; Pyridine nucleotide-disulphide oxidoreductase, dimerization domain
    cl21454
    Location:27 → 62
    NADB_Rossmann; Rossmann-fold NAD(P)(+)-binding proteins

  4. NM_001382047.1 → NP_001368975.1  thioredoxin reductase 1, isoform D

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A6H2EFX8
    Conserved Domains (1) summary
    TIGR01438
    Location:42 → 524
    TGR; thioredoxin and glutathione reductase selenoprotein
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
A0A6H2EFX8 A0A6H2EFX8
P91938.2 P91938

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