Txnrd1 thioredoxin reductase 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Txnrd1provided by RGD
Official Full Name: thioredoxin reductase 1provided by RGD
Primary source: RGD:61959
See related: Ensembl:ENSRNOG00000009088 AllianceGenome:RGD:61959
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: Tr
Summary: The protein encoded by this gene belongs to the pyridine nucleotide-disulfide oxidoreductase family, and is a member of the thioredoxin (Trx) system. Three thioredoxin reductase (TrxR) isozymes are found in mammals. TrxRs are selenocysteine-containing flavoenzymes, which reduce thioredoxins, as well as other substrates, and play a key role in redox homoeostasis. This gene encodes an ubiquitously expressed, cytosolic form of TrxR, which functions as a homodimer containing FAD, and selenocysteine (Sec) at the active site. Sec is encoded by UGA codon that normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, the Sec insertion sequence (SECIS) element, which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing, primarily at the 5' end, results in transcript variants encoding same or different isoforms. [provided by RefSeq, Jun 2017]
Expression: Biased expression in Kidney (RPKM 368.7), Liver (RPKM 218.2) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 7q13

Exon count:: 18

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	7	NC_086025.1 (22717620..22802553, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	7	NC_051342.1 (20830042..20914990, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	7	NC_005106.4 (26946124..26984400, complement)

Chromosome 7 - NC_086025.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

miR8755p regulates IR and inflammation via targeting TXNRD1 in gestational diabetes rats.
Title: miR‑875‑5p regulates IR and inflammation via targeting TXNRD1 in gestational diabetes rats.
Compensatory Neuroprotective Response of Thioredoxin Reductase against Oxidative-Nitrosative Stress Induced by Experimental Autoimmune Encephalomyelitis in Rats: Modulation by Theta Burst Stimulation.
Title: Compensatory Neuroprotective Response of Thioredoxin Reductase against Oxidative-Nitrosative Stress Induced by Experimental Autoimmune Encephalomyelitis in Rats: Modulation by Theta Burst Stimulation.
Data suggest TrxR1 and NADPH directly protect PTP1B from inactivation by oxidation; this protection is independent of TRX1 and PRX2; this protection is blocked by auranofin (an inhibitor of TrxR1 and requires an intact selenocysteine residue in TrxR1. (TrxR1 = thioredoxin reductase 1; PTP1B = protein tyrosine phosphatase, non-receptor type 1; TRX1 = thioredoxin-1; PRX2 = paired related homeobox 2 protein)
Title: Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H(2)O(2) exposure.
Inhibition of thioredoxin reductase-1 by brevetoxin-2 is via the formation of a Michael adduct between selenocysteine and the alpha, beta-unsaturated aldehyde moiety of the toxin.
Title: Brevetoxin-2, is a unique inhibitor of the C-terminal redox center of mammalian thioredoxin reductase-1.
rat liver selenoenzyme thioredoxin reductase (Txnrd1, TR1) efficiently reduces tetrathionate
Title: Reduction of Tetrathionate by Mammalian Thioredoxin Reductase.
DSW drinking reduced ulcer area as well as apoptotic signaling in acetic acid-induced duodenal ulcers. DSW, which contains selenium, provides intestinal protection against duodenal ulcers through the upregulation of Bcl-2 and thioredoxin reductase
Title: Deep-sea water containing selenium provides intestinal protection against duodenal ulcers through the upregulation of Bcl-2 and thioredoxin reductase 1.
Trp114 of TrxR1 serves a function reminiscent of an irreversible sensor for excessive oxidation.
Title: The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death.
Active TrxR1 and TrxR2 are required for cerebellar granule cell survival.
Title: Thioredoxin/thioredoxin reductase system involvement in cerebellar granule cell apoptosis.
Sec-containing TrxR1 is absolutely required for self-sufficient growth of MEFs under high-glucose conditions, owing to an essential importance of this enzyme for elimination of glucose-derived H2O2.
Title: Sec-containing TrxR1 is essential for self-sufficiency of cells by control of glucose-derived H2O2.
The aim of the current study was to determine why TrxR activity was reduced and whether reduced TrxR activity contributed to enhanced aging myocardial ischemia/reperfusion injury.
Title: Thioredoxin reductase was nitrated in the aging heart after myocardial ischemia/reperfusion.

Submit: New GeneRIF Correction See all GeneRIFs (28)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

AW527618 (e-PCR)
- UniSTS:260887

AW527618 (e-PCR)
- UniSTS:246064

D7Wox51 (e-PCR)
- UniSTS:518733

RH138724 (e-PCR)
- UniSTS:220811

RH137037 (e-PCR)
- UniSTS:219126

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables FAD binding	IEA Inferred from Electronic Annotation more info
enables FAD binding	ISO Inferred from Sequence Orthology more info
enables FAD binding	ISS Inferred from Sequence or Structural Similarity more info
enables NAD(P)H oxidase H2O2-forming activity	IDA Inferred from Direct Assay more info	PubMed
enables NADPH peroxidase activity	IDA Inferred from Direct Assay more info	PubMed
enables NADPH peroxidase activity	IEA Inferred from Electronic Annotation more info
enables NADPH peroxidase activity	ISO Inferred from Sequence Orthology more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables mercury ion binding	IDA Inferred from Direct Assay more info	PubMed
enables selenate reductase 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	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in NADPH oxidation	IDA Inferred from Direct Assay more info	PubMed
involved_in benzene-containing compound metabolic process	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within cell population proliferation	ISO Inferred from Sequence Orthology more info
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 cellular oxidant detoxification	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within cellular oxidant detoxification	ISO Inferred from Sequence Orthology more info
involved_in cellular response to copper ion	IEP Inferred from Expression Pattern more info	PubMed
involved_in cellular response to hyperoxia	IEP Inferred from Expression Pattern more info	PubMed
acts_upstream_of_or_within gastrulation	ISO Inferred from Sequence Orthology more info
involved_in halogen metabolic process	IEP Inferred from Expression Pattern more info	PubMed
involved_in hydrogen peroxide catabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within mesoderm formation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to axon injury	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to hyperoxia	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to inorganic substance	IEA Inferred from Electronic Annotation more info
involved_in response to oxidative stress	IDA Inferred from Direct Assay more info	PubMed
involved_in response to oxidative stress	IEA Inferred from Electronic Annotation more info
involved_in response to selenium ion	IEP Inferred from Expression Pattern more info	PubMed
involved_in response to xenobiotic stimulus	IEP Inferred from Expression Pattern more info	PubMed
involved_in selenocysteine metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in fibrillar center	IEA Inferred from Electronic Annotation more info
located_in fibrillar center	ISO Inferred from Sequence Orthology more info
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in neuronal cell body	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: thioredoxin reductase 1, cytoplasmic

Names: NADPH-dependent thioredoxin reductase; peroxidase TXNRD1; selenoprotein oxidoreductase; thioredoxin reductase TR1

NP_001338910.1

EC 1.11.1.2

EC 1.8.1.9

NP_001338912.1

EC 1.11.1.2

EC 1.8.1.9

NP_001338913.1

EC 1.11.1.2

EC 1.8.1.9

NP_113802.2

EC 1.11.1.2

EC 1.8.1.9

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001351981.1 → NP_001338910.1 thioredoxin reductase 1, cytoplasmic isoform 1

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks a 5' non-coding exon; therefore, has a shorter 5' UTR compared to variant 1. Variants 1-3 encode the same isoform (1).

Source sequence(s)

AF220761, BC085726, BF415095, CB579100

UniProtKB/Swiss-Prot

O89049, Q5U344, Q9JKZ3, Q9JKZ4, Q9R1I3

UniProtKB/TrEMBL

R9PXU4

Conserved Domains (1) summary

TIGR01438
Location:11 → 499

TGR; thioredoxin and glutathione reductase selenoprotein
NM_001351983.1 → NP_001338912.1 thioredoxin reductase 1, cytoplasmic isoform 1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in the 5' UTR compared to variant 1. Variants 1-3 encode the same isoform (1).

Source sequence(s)

BC085726, BF415095, FQ090798, FQ225805

UniProtKB/Swiss-Prot

O89049, Q5U344, Q9JKZ3, Q9JKZ4, Q9R1I3

UniProtKB/TrEMBL

R9PXU4

Conserved Domains (1) summary

TIGR01438
Location:11 → 499

TGR; thioredoxin and glutathione reductase selenoprotein
NM_001351984.1 → NP_001338913.1 thioredoxin reductase 1, cytoplasmic isoform 2

Status: REVIEWED

Description

Transcript Variant: This variant (4) represents use of an alternate upstream promoter, and contains additional exons at the 5' end compared to variant 1. The encoded isoform (2) has a longer and distinct N-terminus, resulting from translation initiation at an in-frame upstream start codon, compared to isoform 1.

Source sequence(s)

BC085726, BF415095

UniProtKB/Swiss-Prot

O89049, Q5U344, Q9JKZ3, Q9JKZ4, Q9R1I3

UniProtKB/TrEMBL

R9PXU4

Conserved Domains (1) summary

TIGR01438
Location:92 → 580

TGR; thioredoxin and glutathione reductase selenoprotein
NM_031614.3 → NP_113802.2 thioredoxin reductase 1, cytoplasmic isoform 1

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the predominant transcript and encodes isoform 1. Variants 1-3 encode the same isoform.

Source sequence(s)

BC085726, BF415095, CB579100

UniProtKB/Swiss-Prot

O89049, Q5U344, Q9JKZ3, Q9JKZ4, Q9R1I3

UniProtKB/TrEMBL

R9PXU4

Related

ENSRNOP00000013612.8, ENSRNOT00000013613.8

Conserved Domains (1) summary

TIGR01438
Location:11 → 499

TGR; thioredoxin and glutathione reductase selenoprotein