Aldehyde dehydrogenase family 3 member B1 (ALDH3B1)
The protein contains 468 amino acids for an estimated molecular weight of 51840 Da.
Oxidizes medium and long chain saturated and unsaturated aldehydes (PubMed:17382292, PubMed:23721920). Metabolizes also benzaldehyde (PubMed:17382292). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (PubMed:17382292, PubMed:23721920). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (PubMed:17382292). May have a protective role against the cytotoxicity induced by lipid peroxidation (PubMed:17382292). (updated: July 3, 2019)
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.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Alcohol metabolic process
Aldehyde catabolic process
Cellular response to oxidative stress
Ethanol catabolic process
Lipid metabolic process
Neutrophil degranulation
Oxidation-reduction process
Response to oxidative stress
Sphingolipid biosynthetic process
The reference OMIM entry for this protein is 600466
Aldehyde dehydrogenase 3 family, member b1; aldh3b1
Aldehyde dehydrogenase 7; aldh7
Acetaldehyde dehydrogenase 7
CLONING
The aldehyde dehydrogenases are a family of isozymes that may play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. Hsu et al. (1994) reported the cloning and sequencing of a cDNA encoding a new human ALDH, designated ALDH7. Degenerate oligodeoxyribonucleotides derived from conserved regions of known ALDH cDNAs amplified a 408-bp product from human kidney total RNA by the reverse transcription-PCR procedure. This PCR product was subcloned, selected, and used as a probe to screen a human kidney cDNA library. The full-length human kidney cDNA of ALDH7 is 2,791 bp long and contains an open reading frame encoding 468 amino acids. The deduced sequence of ALDH7 was longer than that of human stomach ALDH3 (100660) by 15 amino acids at the C terminus. The degree of identity between the 2 isozymes was 52% with a positional alignment of 453 amino acids. Northern blot analysis demonstrated that lung is another major tissue expressing ALDH7.GENE STRUCTURE
Hsu et al. (1997) determined the structure of the ALDH7 and ALDH8 (601917) genes. The ALDH7 gene spans about 20 kb of genomic DNA and is composed of 9 coding exons. The ALDH8 gene is over 10 kb in length and consists of at least 10 exons. The ALDH8 gene contains an in-frame stop codon at the seventeenth codon position from the first initiator Met. The coding region of the ALDH7 gene shows about 86% nucleotide identity with the corresponding region of the ALDH8 gene. The numbers and positions of the introns of the 2 genes are conserved, suggesting that gene duplication is involved in the expansion of the ALDH gene family. The human ALDH7 and ALDH8 genes have a close evolutionary relationship with human ALDH3.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ALDH7 gene to chromosome 11 (TMAP RH69713). ... More on the omim web site
July 4, 2019: 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
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for ALDH3B1
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600466 was added.