Gene
aldh3a2a
- ID
- ZDB-GENE-040718-74
- Name
- aldehyde dehydrogenase 3 family, member A2a
- Symbol
- aldh3a2a Nomenclature History
- Previous Names
- Type
- protein_coding_gene
- Location
- Chr: 15 Mapping Details/Browsers
- Description
- Predicted to enable 3-chloroallyl aldehyde dehydrogenase activity and aldehyde dehydrogenase (NAD+) activity. Predicted to be involved in aldehyde metabolic process. Predicted to act upstream of or within fatty acid metabolic process. Predicted to be located in endoplasmic reticulum membrane. Predicted to be active in cytoplasm. Human ortholog(s) of this gene implicated in Sjogren-Larsson syndrome and arteriosclerosis. Orthologous to human ALDH3A1 (aldehyde dehydrogenase 3 family member A1) and ALDH3A2 (aldehyde dehydrogenase 3 family member A2).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- 2 figures from 2 publications
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
-
- MGC:92064 (1 image)
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
Human Disease
| Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
|---|---|---|---|
| Sjogren-Larsson syndrome | Alliance | Sjogren-Larsson syndrome | 270200 |
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Domain, Family, and Site Summary
| Type | InterPro ID | Name |
|---|---|---|
| Conserved_site | IPR016160 | Aldehyde dehydrogenase, cysteine active site |
| Conserved_site | IPR029510 | Aldehyde dehydrogenase, glutamic acid active site |
| Domain | IPR015590 | Aldehyde dehydrogenase domain |
| Family | IPR012394 | Aldehyde dehydrogenase NAD(P)-dependent |
| Homologous_superfamily | IPR016161 | Aldehyde/histidinol dehydrogenase |
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Domain Details Per Protein
| Protein | Additional Resources | Length | Aldehyde dehydrogenase, C-terminal | Aldehyde dehydrogenase, cysteine active site | Aldehyde dehydrogenase domain | Aldehyde dehydrogenase, glutamic acid active site | Aldehyde dehydrogenase NAD(P)-dependent | Aldehyde dehydrogenase, N-terminal | Aldehyde/histidinol dehydrogenase |
|---|---|---|---|---|---|---|---|---|---|
| UniProtKB:Q90ZZ8 | InterPro | 488 |
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- Genome Browsers
| Type | Name | Annotation Method | Has Havana Data | Length (nt) | Analysis |
|---|---|---|---|---|---|
| mRNA |
aldh3a2a-201
(1)
|
Ensembl | 2,072 nt | ||
| mRNA |
aldh3a2a-202
(1)
|
Ensembl | 462 nt | ||
| mRNA |
aldh3a2a-204
(1)
|
Ensembl | 664 nt | ||
| mRNA |
aldh3a2a-205
(1)
|
Ensembl | 2,657 nt | ||
| mRNA |
aldh3a2a-206
(1)
|
Ensembl | 4,218 nt |
1 - 5 of 7 Show all
Interactions and Pathways
No data available
Plasmids
No data available
- Lu, Y., Travnickova, J., Badonyi, M., Rambow, F., Coates, A., Khan, Z., Marques, J., Murphy, L.C., Garcia-Martinez, P., Marais, R., Louphrasitthiphol, P., Chan, A.H.Y., Schofield, C.J., von Kriegsheim, A., Marsh, J.A., Pavet, V., Sansom, O.J., Illingworth, R.S., Patton, E.E. (2024) ALDH1A3-acetaldehyde metabolism potentiates transcriptional heterogeneity in melanoma. Cell Reports. 43:114406114406
- Brunsdon, H., Brombin, A., Peterson, S., Postlethwait, J.H., Patton, E.E. (2022) Aldh2 is a lineage-specific metabolic gatekeeper in melanocyte stem cells. Development (Cambridge, England). 149(10):
- Kamoshita, M., Kumar, R., Anteghini, M., Kunze, M., Islinger, M., Martins Dos Santos, V., Schrader, M. (2022) Insights Into the Peroxisomal Protein Inventory of Zebrafish. Frontiers in Physiology. 13:822509
- Lang, I., Virk, G., Zheng, D.C., Young, J., Nguyen, M.J., Amiri, R., Fong, M., Arata, A., Chadaideh, K.S., Walsh, S., Weiser, D.C. (2020) The Evolution of Duplicated Genes of the Cpi-17/Phi-1 (ppp1r14) Family of Protein Phosphatase 1 Inhibitors in Teleosts. International Journal of Molecular Sciences. 21(16):
- Lou, B., Boger, M., Bennewitz, K., Sticht, C., Kopf, S., Morgenstern, J., Fleming, T., Hell, R., Yuan, Z., Nawroth, P.P., Kroll, J. (2020) Elevated 4-hydroxynonenal induces hyperglycaemia via Aldh3a1 loss in zebrafish and associates with diabetes progression in humans. Redox Biology. 37:101723
- Lodd, E., Wiggenhauser, L.M., Morgenstern, J., Fleming, T.H., Poschet, G., Büttner, M., Tabler, C.T., Wohlfart, D.P., Nawroth, P.P., Kroll, J. (2019) The combination of loss of glyoxalase1 and obesity results in hyperglycemia. JCI insight. 4(12):
- Xiang, D., Qiao, K., Song, Z., Shen, S., Wang, M., Wang, Q. (2019) Enantioselectivity of toxicological responses induced by maternal exposure of cis-bifenthrin enantiomers in zebrafish (Danio rerio) larvae. Journal of hazardous materials. 371:655-665
- Bayés, À., Collins, M.O., Reig-Viader, R., Gou, G., Goulding, D., Izquierdo, A., Choudhary, J.S., Emes, R.D., Grant, S.G. (2017) Evolution of complexity in the zebrafish synapse proteome. Nature communications. 8:14613
- Braasch, I., Gehrke, A.R., Smith, J.J., Kawasaki, K., Manousaki, T., Pasquier, J., Amores, A., Desvignes, T., Batzel, P., Catchen, J., Berlin, A.M., Campbell, M.S., Barrell, D., Martin, K.J., Mulley, J.F., Ravi, V., Lee, A.P., Nakamura, T., Chalopin, D., Fan, S., Wcisel, D., Cañestro, C., Sydes, J., Beaudry, F.E., Sun, Y., Hertel, J., Beam, M.J., Fasold, M., Ishiyama, M., Johnson, J., Kehr, S., Lara, M., Letaw, J.H., Litman, G.W., Litman, R.T., Mikami, M., Ota, T., Saha, N.R., Williams, L., Stadler, P.F., Wang, H., Taylor, J.S., Fontenot, Q., Ferrara, A., Searle, S.M., Aken, B., Yandell, M., Schneider, I., Yoder, J.A., Volff, J.N., Meyer, A., Amemiya, C.T., Venkatesh, B., Holland, P.W., Guiguen, Y., Bobe, J., Shubin, N.H., Di Palma, F., Alföldi, J., Lindblad-Toh, K., Postlethwait, J.H. (2016) The spotted gar genome illuminates vertebrate evolution and facilitates human-teleost comparisons. Nature Genetics. 48(4):427-37
- Lončar, J., Popović, M., Krznar, P., Zaja, R., Smital, T. (2016) The first characterization of multidrug and toxin extrusion (MATE/SLC47) proteins in zebrafish (Danio rerio). Scientific Reports. 6:28937
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