ALDH1A3

ALDH1A3
Identifiers
AliasesALDH1A3, ALDH1A6, ALDH6, MCOP8, RALDH3, aldehyde dehydrogenase 1 family member A3
External IDsMGI: 1861722 HomoloGene: 68080 GeneCards: ALDH1A3
Gene location (Human)
Chr.Chromosome 15 (human)[1]
Band15q26.3Start100,877,714 bp[1]
End100,916,626 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

220

56847

Ensembl

ENSG00000184254

ENSMUSG00000015134

UniProt

P47895

Q9JHW9

RefSeq (mRNA)

NM_001293815
NM_000693
NM_001037224

NM_053080

RefSeq (protein)

NP_000684
NP_001280744

NP_444310

Location (UCSC)Chr 15: 100.88 – 100.92 MbChr 7: 66.39 – 66.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aldehyde dehydrogenase 1 family, member A3, also known as ALDH1A3 or retinaldehyde dehydrogenase 3 (RALDH3), is an enzyme that in humans is encoded by the ALDH1A3 gene,[5]

Function

Aldehyde dehydrogenase isozymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. The enzyme encoded by this gene uses retinal as a substrate, either in a free or a cellular retinol-binding protein form.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000184254 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015134 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Hsu LC, Chang WC, Hiraoka L, Hsieh CL (November 1994). "Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6". Genomics. 24 (2): 333–41. doi:10.1006/geno.1994.1624. PMID 7698756.
  6. ↑ "Entrez Gene: ALDH1A3".

Further reading

  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Wan C, Shi Y, Zhao X, et al. (2009). "Positive association between ALDH1A2 and schizophrenia in the Chinese population". Prog. Neuropsychopharmacol. Biol. Psychiatry. 33 (8): 1491–5. doi:10.1016/j.pnpbp.2009.08.008. PMID 19703508.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Nishimura M, Yoshitsugu H, Naito S, Hiraoka I (2002). "Evaluation of gene induction of drug-metabolizing enzymes and transporters in primary culture of human hepatocytes using high-sensitivity real-time reverse transcription PCR". Yakugaku Zasshi. 122 (5): 339–61. doi:10.1248/yakushi.122.339. PMID 12040753.
  • Cañestro C, Catchen JM, Rodríguez-Marí A, et al. (2009). Gojobori T, ed. "Consequences of lineage-specific gene loss on functional evolution of surviving paralogs: ALDH1A and retinoic acid signaling in vertebrate genomes". PLoS Genet. 5 (5): e1000496. doi:10.1371/journal.pgen.1000496. PMC 2682703. PMID 19478994.
  • Saito A, Kawamoto M, Kamatani N (2009). "Association study between single-nucleotide polymorphisms in 199 drug-related genes and commonly measured quantitative traits of 752 healthy Japanese subjects". J. Hum. Genet. 54 (6): 317–23. doi:10.1038/jhg.2009.31. PMID 19343046.
  • Rexer BN, Zheng WL, Ong DE (2001). "Retinoic acid biosynthesis by normal human breast epithelium is via aldehyde dehydrogenase 6, absent in MCF-7 cells". Cancer Res. 61 (19): 7065–70. PMID 11585737.
  • Yoshida A, Rzhetsky A, Hsu LC, Chang C (1998). "Human aldehyde dehydrogenase gene family". Eur. J. Biochem. 251 (3): 549–57. doi:10.1046/j.1432-1327.1998.2510549.x. PMID 9490025.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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