Taldo1 transaldolase 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Taldo1provided by MGI
Official Full Name: transaldolase 1provided by MGI
Primary source: MGI:MGI:1274789
See related: Ensembl:ENSMUSG00000025503 AllianceGenome:MGI:1274789
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Summary: This gene encodes a key enzyme of the nonoxidative pentose phosphate pathway that provides ribose-5-phosphate for nucleic acid synthesis and nicotinamide adenine dinucleotide phosphate (NADPH) for lipid biosynthesis. The encoded protein is important for maintaining structure and function of mitochondria. Studies in knockout mice identify that deficiency of this gene product is a cause of sperm dysmotility and male infertility. Deficiency of this protein has also been identified as a cause of hepatocarcinogenesis in mice. Two related pseudogenes have been identified on chromosome 10. [provided by RefSeq, Mar 2010]
Expression: Ubiquitous expression in large intestine adult (RPKM 211.6), subcutaneous fat pad adult (RPKM 187.0) and 27 other tissues See more
Orthologs: human all
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Genomic context

Location:: 7 F5; 7 86.73 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	7	NC_000073.7 (140972073..140982889)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	7	NC_000073.6 (141392160..141402976)

Chromosome 7 - NC_000073.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Transaldolase inhibits CD36 expression by modulating glutathione-p38 signaling, exerting protective effects against macrophage foam cell formation.
Title: Transaldolase inhibits CD36 expression by modulating glutathione-p38 signaling, exerting protective effects against macrophage foam cell formation.
These results demonstrate that the nucleocytoplasmic distribution of TALDO1, modulated via alternative translational initiation and dimer formation, plays an important role in a wide range of metabolic networks
Title: Two isoforms of TALDO1 generated by alternative translational initiation show differential nucleocytoplasmic distribution to regulate the global metabolic network.
Data show that erythronic acid was identified as a major abnormal metabolite in all patients and in knock-out TALDO mice implicating an as yet unknown biochemical pathway in this disease.
Title: Mitochondrial involvement and erythronic acid as a novel biomarker in transaldolase deficiency.
Reduced beta-catenin phosphorylation and enhanced c-Jun expression in Taldo1-/- livers reflected adaptation to oxidative stress
Title: Prevention of hepatocarcinogenesis and increased susceptibility to acetaminophen-induced liver failure in transaldolase-deficient mice by N-acetylcysteine.
These data reveal an essential role of transaldolase in sperm-cell mitochondrial function and, thus, male fertility.
Title: Transaldolase is essential for maintenance of the mitochondrial transmembrane potential and fertility of spermatozoa.

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Variation

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Alleles

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

Endonuclease-mediated (2)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables carbohydrate binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	IDA Inferred from Direct Assay more info	PubMed
enables monosaccharide binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables transaldolase activity	IBA Inferred from Biological aspect of Ancestor more info
enables transaldolase activity	IDA Inferred from Direct Assay more info	PubMed
enables transaldolase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables transaldolase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in carbohydrate metabolic process	IEA Inferred from Electronic Annotation more info
involved_in fructose 6-phosphate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in glyceraldehyde-3-phosphate metabolic process	ISO Inferred from Sequence Orthology more info
involved_in pentose-phosphate shunt	IDA Inferred from Direct Assay more info	PubMed
involved_in pentose-phosphate shunt	IEA Inferred from Electronic Annotation more info
involved_in pentose-phosphate shunt	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in pentose-phosphate shunt	ISO Inferred from Sequence Orthology more info
involved_in pentose-phosphate shunt, non-oxidative branch	IBA Inferred from Biological aspect of Ancestor more info
involved_in pentose-phosphate shunt, non-oxidative branch	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: transaldolase

NP_035658.1

EC 2.2.1.2

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.