Tdo2 tryptophan 2,3-dioxygenase [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tdo2provided by MGI
Official Full Name: tryptophan 2,3-dioxygenaseprovided by MGI
Primary source: MGI:MGI:1928486
See related: Ensembl:ENSMUSG00000028011 AllianceGenome:MGI:1928486
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: TO; TDO; chky
Summary: Predicted to enable several functions, including heme binding activity; oxygen binding activity; and tryptophan 2,3-dioxygenase activity. Predicted to be involved in aromatic amino acid metabolic process and protein homotetramerization. Is expressed in cerebellum; liver; male reproductive gland or organ; and small intestine. Human ortholog(s) of this gene implicated in Gilles de la Tourette syndrome and familial hypertryptophanemia. Orthologous to human TDO2 (tryptophan 2,3-dioxygenase). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Restricted expression toward liver adult (RPKM 173.8) See more
Orthologs: human all
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Genomic context

Location:: 3 E3; 3 35.97 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	3	NC_000069.7 (81865719..81883035, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	3	NC_000069.6 (81958412..81975728, complement)

Chromosome 3 - NC_000069.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

A comprehensive analysis of TDO2 expression in immune cells and characterization of immune cell phenotype in TDO2 knockout mice.
Title: A comprehensive analysis of TDO2 expression in immune cells and characterization of immune cell phenotype in TDO2 knockout mice.
Tryptophan 2,3-Dioxygenase Expression Identified in Murine Decidual Stromal Cells Is Not Essential for Feto-Maternal Tolerance.
Title: Tryptophan 2,3-Dioxygenase Expression Identified in Murine Decidual Stromal Cells Is Not Essential for Feto-Maternal Tolerance.
The autoimmune response elicited by mouse hepatitis virus (MHV-A59) infection is modulated by liver tryptophan-2,3-dioxygenase (TDO).
Title: The autoimmune response elicited by mouse hepatitis virus (MHV-A59) infection is modulated by liver tryptophan-2,3-dioxygenase (TDO).
Tdo2 deficiency had no significant effects on such as prepulse inhibition, depression-like and social behaviors.
Title: Comprehensive behavioral analysis of tryptophan 2,3-dioxygenase (Tdo2) knockout mice.
TDO-deficiency protected from neuronal loss in the spinal cord but not in the optic nerves.
Title: Tryptophan-2,3-Dioxygenase (TDO) deficiency is associated with subclinical neuroprotection in a mouse model of multiple sclerosis.
Study demonstrated that n-butylidenephthalide (n-BP)functions by regulating the early part of the kynurenine pathway through the downregulation of tryptophan 2, 3-dioxygenase (TDO2), which decreases the downstream neurotoxic product, quinolinic acid (QA). Findings indicate a correlation between n-BP, TDO2, QA, calpain, and toxic fragment formation.
Title: n-Butylidenephthalide exhibits protection against neurotoxicity through regulation of tryptophan 2, 3 dioxygenase in spinocerebellar ataxia type 3.
Data suggest that Indoleamine 2,3-dioxygenase 1 (IDO1) appears to be a potential hallmark of liver lesions, and its deficiency protects mice from CCl4-induced fibrosis mediated by Th17 cells down-regulation and tryptophan 2,3-dioxygenase (TDO) compensatory increase.
Title: Indoleamine 2,3-dioxygenase 1 deficiency attenuates CCl4-induced fibrosis through Th17 cells down-regulation and tryptophan 2,3-dioxygenase compensation.
Findings suggest non-redundant neurophysiological roles for indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2 and tryptophan 2,3-dioxygenase in modulating brain activities and metabolism.
Title: Deletion of TDO2, IDO-1 and IDO-2 differentially affects mouse behavior and cognitive function.
Data suggest that high-fat diet (HFD) alters regulation of expression of sirtuins (Sirt4 and Sirt7) and enzymes in NAD biosynthetic pathway (Tdo2 and Nnmt); these alterations are more prominent in liver as compared to white adipose tissue or skeletal muscle; Tdo2 and Nnmt may serve as markers of HFD consumption. (Tdo2 = tryptophan 2,3-dioxygenase; Nnmt = nicotinamide N-methyltransferase)
Title: Tissue-specific regulation of sirtuin and nicotinamide adenine dinucleotide biosynthetic pathways identified in C57Bl/6 mice in response to high-fat feeding.
both TDO and IDO biosynthesize nicotinamide from D-tryptophan and L-tryptophan in mice
Title: Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of D-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice.

Submit: New GeneRIF Correction See all GeneRIFs (16)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (4) 1 citation
Spontaneous (1)
Targeted (4) 1 citation

General gene information

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Markers

RH124606 (e-PCR)
- UniSTS:161428

AI194855 (e-PCR)
- UniSTS:207514

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables amino acid binding	IEA Inferred from Electronic Annotation more info
enables amino acid binding	ISO Inferred from Sequence Orthology more info
enables heme binding	IBA Inferred from Biological aspect of Ancestor more info
enables heme binding	ISO Inferred from Sequence Orthology more info
enables heme binding	ISS Inferred from Sequence or Structural Similarity more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables oxygen binding	IEA Inferred from Electronic Annotation more info
enables oxygen binding	ISO Inferred from Sequence Orthology more info
enables tryptophan 2,3-dioxygenase activity	IBA Inferred from Biological aspect of Ancestor more info
enables tryptophan 2,3-dioxygenase activity	ISO Inferred from Sequence Orthology more info
enables tryptophan 2,3-dioxygenase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in protein homotetramerization	ISO Inferred from Sequence Orthology more info
involved_in protein homotetramerization	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to nitroglycerin	IEA Inferred from Electronic Annotation more info
involved_in tryptophan catabolic process to acetyl-CoA	IBA Inferred from Biological aspect of Ancestor more info
involved_in tryptophan catabolic process to acetyl-CoA	IEA Inferred from Electronic Annotation more info
involved_in tryptophan catabolic process to acetyl-CoA	ISO Inferred from Sequence Orthology more info
involved_in tryptophan catabolic process to kynurenine	IEA Inferred from Electronic Annotation more info
involved_in tryptophan catabolic process to kynurenine	ISO Inferred from Sequence Orthology more info
involved_in tryptophan catabolic process to kynurenine	ISS Inferred from Sequence or Structural Similarity more info
involved_in tryptophan metabolic process	IEA Inferred from Electronic Annotation more info
involved_in tryptophan metabolic process	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: tryptophan 2,3-dioxygenase

Names: TRPO; tdo variant1; tdo variant2; tryptamin 2,3-dioxygenase; tryptophan oxygenase; tryptophan pyrrolase; tryptophanase

NP_064295.2

EC 1.13.11.11

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.