Fructose-bisphosphate aldolase A (ALDOA)
The protein contains 364 amino acids for an estimated molecular weight of 39420 Da.
Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity). (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.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| dbSNP:rs11553107 | |
| GSD12 | |
| dbSNP:rs11553108 | |
| GSD12 | |
| GSD12 | |
| GSD12 |
Biological Process
Actin filament organization
ATP biosynthetic process
Binding of sperm to zona pellucida
Blood coagulation
Canonical glycolysis
Carbohydrate metabolic process
Fructose 1,6-bisphosphate metabolic process
Fructose metabolic process
Gluconeogenesis
Glucose metabolic process
Glycolytic process
Muscle cell cellular homeostasis
Neutrophil degranulation
Pathogenesis
Platelet activation
Platelet degranulation
Protein homotetramerization
Regulation of cell shape
Small molecule metabolic process
Striated muscle contraction
The reference OMIM entry for this protein is 103850
Aldolase a, fructose-bisphosphate; aldoa
Fructose-1,6-bisphosphate aldolase a
Aldolase a; alda
Aldolase 1
Fructoaldolase a
DESCRIPTION
Fructose-1,6-bisphosphate aldolase (EC 4.1.2.13) is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The enzyme is a tetramer of identical 40-kD subunits. Vertebrates have 3 aldolase isozymes, aldolases A, B (ALDOB; 612724), and C (ALDOC; 103870), which are distinguished by their electrophoretic and catalytic properties. The sequence of the aldolases around the active-site lysine is highly conserved in evolution. Mammalian tissues express aldolase isozymes in a well-characterized pattern. Developing embryo produces aldolase A, which continues to be expressed in many adult tissues, sometimes at much higher levels than in embryo. In adult muscle, aldolase A can be as much as 5% of total cellular protein. In adult liver, kidney, and intestine, aldolase A expression is repressed and aldolase B is produced. In brain and other nervous tissue, aldolase A and C are expressed about equally. In transformed liver cells, aldolase A replaces aldolase B (Rottmann et al., 1984).CLONING
Electrophoretic variants of fructoaldolase were reported by Charlesworth (1972). Sakakibara et al. (1985) cloned aldolase A from a human liver cDNA library. The deduced protein contains 363 amino acids. RNA blot analysis revealed a 1.6-kb ALDOA mRNA in skeletal muscle and a 1.7-kb ALDOA mRNA in liver and placenta. Freemont et al. (1988) presented the complete amino acid sequence of human skeletal muscle fructose-bisphosphate aldolase, comprising 363 residues.GENE STRUCTURE
Izzo et al. (1988) found that the ALDOA gene spans 7.5 kb and contains 12 exons. It occurs as a single copy per haploid human genome. Eight exons containing the coding sequence were common to all mRNAs extracted from several mammalian sources. Four additional exons were identified in the 5-prime UTR: the first was contained in the ubiquitous mRNA, the second in the muscle-specific mRNA, and the third and fourth in a minor mRNA in human liver. S(1)-nuclease-protection analysis of the 5-prime end of mRNA from cultured fibroblasts, muscle, and hepatoma cell lines revealed 4 different transcription initiation sites. The presence of conventional sequences for 4 eukaryotic promoters was also demonstrated. The nucleotide similarities in the coding region and the intron-exon organization of aldolases A, B, and C confirmed that they arose from a common ancestral gene, with aldolase B diverging first.MAPPING
Harris (1974) concluded that 3 loci determine aldolase. Cohen-Haguenauer et al. (1985) assigned aldolase A to chromosome 16, whereas Kukita et al. (1985) assigned it to chromosome 22. However, Kukita et al. (1987) mapped the ALDOA gene to chromosome 16 by 3 different methods: molecular hybridization to hybrid cell DNA, molecular hybridization to DNA of sorted metaphase chromosomes, and in situ hybridization. In situ hybridization indicated that the gene is located on the chromosome 16q22-q24 band. Serero et al. (1988) also assigned the aldolase A gene to chromosome 16 by Southern blot analysis of human genomic DNA with a cDNA probe. Aldolase A pseudogenes were found on chromosomes 3 and 10. The map location of the 3 aldolase genes and the aldolase pseudogene (see 612724) is of considerable interest from the point of view of chromosome evolution. The 4 genes are found on 2 pairs of morphologically similar chromosomes, 9 and 10, and 16 and 17. These ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
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 103850 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed