Transaldolase (TALDO1)
The protein contains 337 amino acids for an estimated molecular weight of 37540 Da.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Carbohydrate metabolic process
Energy reserve metabolic process
Fructose 6-phosphate metabolic process
Glyceraldehyde-3-phosphate metabolic process
Interleukin-12-mediated signaling pathway
Pathogenesis
Pentose-phosphate shunt
Pentose-phosphate shunt, non-oxidative branch
Small molecule metabolic process
Xylulose biosynthetic process
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Intracellular anatomical structure
Nucleoplasm
Nucleus
The reference OMIM entry for this protein is 602063
Transaldolase 1; taldo1
DESCRIPTION
Transaldolase (EC 2.2.1.2) is the key enzyme of the pentose phosphate pathway, which is responsible for generation of reducing equivalents to protect cellular integrity from reactive oxygen intermediates (Banki et al., 1997).CLONING
Banki et al. (1994) cloned the TALDO1 gene. The deduced 336-amino acid protein has a predicted molecular mass of 38 kD and shows 58% overall sequence homology with the 37-kD yeast transaldolase. Kusuda et al. (1998) isolated the cDNA for the mouse homolog of TALDO1 and determined the nucleotide sequence covering the complete coding region.GENE STRUCTURE
Banki et al. (1994) determined that, unlike the intronless yeast transaldolase gene, the human TALDO1 gene contains 5 exons, the second and third of which are developed by insertion of a retrotransposable element. Detection of a retrotransposon in the coding sequence of the human transaldolase gene demonstrated the importance of these repetitive elements in the evolution of the eukaryotic genome.MAPPING
By Southern blot analysis of human/mouse somatic cell hybrid DNA, Banki et al. (1997) mapped TALDO1 to the region 11pter-p13. By fluorescence in situ hybridization (FISH), they narrowed the assignment to 11p15.5-p15.4. A truncated and mutated segment of exon 5 terminating with a poly(A) tail was identified in a pseudogene locus (TALDOP1) on chromosome 1. RT-PCR studies of mouse/human somatic cell hybrids revealed the presence of the functional gene on chromosome 11 and its absence on chromosome 1. Mapping of radiation hybrids placed TALDO1 between the markers WI-1421 and D11S922 on 11p15. By FISH, Kusuda et al. (1997) concluded that the functional TALDO1 gene is located on 1p34.1-p33. Kusuda et al. (1998) mapped a paralogous gene to 11p15, where Banki et al. (1997) had mapped the TALDO1 gene. Kusuda et al. (1998) symbolized the gene on chromosome 11 as TALDOR (TALDO related). The exon sequence of TALDOR was almost identical to that of TALDO but its exons corresponding to exons 4 and 5 of TALDO were found to be split by 4 introns. By FISH using cDNA as a probe, Kusuda et al. (1998) showed that the mouse transaldolase gene is localized to bands F3-F4 of chromosome 7 as a single-copy gene. This chromosomal region is known to be syntenic to human chromosome 11p15 rather than to 1p34.1-p33, suggesting that TALDOR is the ancestral form. The existence of TALDOR implied a duplication of the mammalian transaldolase gene after divergence of rodent and primate. Hashimoto (1998) concluded that the functional TALDO gene is on human chromosome 11 and a pseudogene on human chromosome 1.MOLECULAR GENETICS
Verhoeven et al. (2001) described a patient with transaldolase deficiency (606003) caused by a homozygous 3-bp deletion (602063.0001) in the TALDO1 gene, resulting in the absence of serine at position 171 of the transaldolase protein. This amino acid is invariable between species and is located in a conserved region, indicating its importance for enzyme activity. In 12 patients from 6 Saudi Arabian families with transaldolase deficiency, Eyaid et al. (2013) identified homozygosity for a frameshift mutation in the TALDO1 gene (602063.0002).ANIMAL MODEL
Perl et al. (2006) found that Taldo1-null mice developed normally, but males were sterile due to functional and structural defects of mitochondria. Reduced motility in Taldo1-null spermatozoa was associated with diminished mitochondrial reactive ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602063 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed