Aflatoxin B1 aldehyde reductase member 2 (AKR7A2)
The protein contains 359 amino acids for an estimated molecular weight of 39589 Da.
Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. (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.
- 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.
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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The reference OMIM entry for this protein is 603418
Aldo-keto reductase family 7, member a2; akr7a2
Aldo-keto reductase 7; akr7
Aflatoxin b1-aldehyde reductase; afar
DESCRIPTION
Aldo-keto reductases, such as AKR7A2, are involved in the detoxification of aldehydes and ketones.CLONING
Ireland et al. (1998) used a rat aflatoxin B1-aldehyde reductase (AFAR) cDNA and a human EST sequence to isolate human AFAR cDNAs from cerebellum and liver libraries. The full-length cDNA encodes a 330-amino acid polypeptide with 78% identity to rat AFAR, 22% identity to a Shaker-related voltage-gated potassium channel, and 16% identity to aldose reductase (103880). Northern blot analysis revealed that AFAR is expressed in a wide range of human tissues. By EST database analysis, Kelly et al. (2002) identified an AKR7A2 splice variant that encodes a deduced 359-amino acid protein with an N-terminal extension.GENE FUNCTION
Ireland et al. (1998) showed that expressed AFAR can metabolize aflatoxin, but its specificity for some substrates differs from that of rat AFAR. They showed that AFAR is the principal human liver reductase for 2-carboxybenzaldehyde.GENE STRUCTURE
Praml et al. (2003) determined that the AKR7A2 gene contains 7 exons and spans 7.8 kb.MAPPING
By FISH and genomic sequence analysis, Praml et al. (2003) mapped the AKR7A2 gene to chromosome 1p36.1-p35, where it lies in a gene cluster with the AKR7A3 (608477) and AKR7A4 (608478) genes. The genes are oriented in a head-to-tail tandem arrangement, distal-5-prime-AKR7A2-AKR7A3-AKR7A4-3-prime-proximal. AKR7A pseudogenes are located on chromosomes Xq25 and 1p12. Praml et al. (2003) mapped the mouse Akr7a2 gene to chromosome 5, where it is proximal to the Pla2g2a gene (172411). ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 603418 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed