Triokinase/FMN cyclase (DAK)
The protein contains 575 amino acids for an estimated molecular weight of 58947 Da.
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response (PubMed:17600090). (updated: Nov. 22, 2017)
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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs2260655 | |
| dbSNP:rs35723406 | |
| TKFCD | |
| TKFCD |
Biological Process
Carbohydrate phosphorylation
Cellular carbohydrate metabolic process
Fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate
Glycerol catabolic process
Glycerol metabolic process
Innate immune response
Negative regulation of MDA-5 signaling pathway
Regulation of innate immune response
The reference OMIM entry for this protein is 615844
Dihydroxyacetone kinase 2, s. cerevisiae, homolog of; dak
Dha kinase/fmn cyclase
DESCRIPTION
DAK has bifunctional activity: it catalyzes the reaction flavin adenine dinucleotide (FAD) to riboflavin 4-prime,5-prime-phosphate (cyclic flavin mononucleotide, or cFMN), in addition to ATP-dependent phosphorylation of dihydroxyacetone (DHA) (Cabezas et al., 2005).CLONING
By searching a database for sequences similar to purified rat liver FMN cyclase, followed by PCR of a brain cDNA library, Cabezas et al. (2005) cloned human DAK, which they called DHA kinase/FMN cyclase. The deduced protein contains 575 amino acids and shares 84 to 99% identity with its mammalian orthologs. It also has orthologs in several lower organisms. SDS-PAGE detected recombinant human DAK at an apparent molecular mass of 59.4 kD.GENE FUNCTION
Cabezas et al. (2005) found that both recombinant human DAK and purified rat liver FMN cyclase catalyzed phosphorylation of DHA and formation of cFMN. In addition, each activity of human DAK was inhibited by the substrates of the other: ATP and dihydroxyacetone were strong and weak inhibitors of FMN cyclase activity, respectively, whereas FAD was a weak, but likely full, inhibitor of DHA kinase activity. Cabezas et al. (2005) observed that the 2 activities of DAK were related, but they reasoned that the active sites may not fully coincide, since DHA was only a partial inhibitor of FMN cyclase activity.GENE STRUCTURE
Cabezas et al. (2005) determined that the DAK gene contains 17 exons.MAPPING
By genomic sequence analysis, Cabezas et al. (2005) mapped the DAK gene to chromosome 11q12.2. ... More on the omim web site
Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 615844 was added.