| Standard Name | AST1 1 |
|---|---|
| Systematic Name | YBL069W |
| Feature Type | ORF, Verified |
| Description | Lipid raft associated protein; interacts with the plasma membrane ATPase Pma1p and has a role in its targeting to the plasma membrane by influencing its incorporation into lipid rafts; sometimes classified in the medium-chain dehydrogenase/reductases (MDRs) superfamily; AST1 has a paralog, AST2, that arose from the whole genome duplication (1, 2, 3, 4 and see Summary Paragraph) |
| Name Description | ATPase STabilizing 1 |
| Chromosomal Location | |
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| View Computational GO annotations for AST1 | |
| Molecular Function | |
| Manually curated |
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| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Classical genetics | |
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| null | |
| Large-scale survey | |
| null |
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| Resources |
| 11 total interaction(s) for 9 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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| Resources |
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
| This feature contains embedded feature(s): YBL068W-A | |||||||||||||
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| Last Update | Coordinates: 2011-02-03 | Sequence: 2001-05-29 | ||||||||||||
| Subfeature details |
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| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000165 |
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About the medium-chain dehydrogenase/reductase (MDR) family
Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (5), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (6, 4). Many MDR members are basic metabolic enzymes acting on alcohols or aldehydes, and thus these enzymes may have roles in detoxifying alcohols and related compounds, protecting against environmental stresses such as osmotic shock, reduced or elevated temperatures, or oxidative stress (6). The family also includes the mammalian zeta-crystallin lens protein, which may protect the lens against oxidative damage and enzymes which produce lignocellulose in plants (6).
MDR enzymes typically have subunits of about 350 aa residues and are two-domain proteins, with a catalytic domain and a second domain for binding to the nicotinamide cofactor, either NAD(H) or NADP(H) (6, 4). They contain 0, 1, or 2 zinc atoms (7). When zinc is present, it is involved in catalysis at the active site.
Based on phylogenetic and sequence analysis, the members of the MDR superfamily can be further divided into more closely related subgroups (6, 4). In families which are widespread from prokaryotes to eukaryotes, some members appear conserved across all species, while others appear to be due to lineage specific duplications. Some subgroups are only found in certain taxa. S. cerevisiae contains fifteen (6) or twenty-one (4) members of the MDR superfamily, listed below. The difference in number is due to six sequences that were included as members of the quinone oxidoreductase family by Riveros-Rosas et al. (4) but not by Nordling et al. (6).
Zinc-containing enzyme groups:
- PDH; "polyol" dehydrogenase family - BDH1, BDH2, SOR1, SOR2, XYL2
- ADH; class III alcohol dehydrogenase family - SFA1
- Y-ADH; "yeast" alcohol dehydrogenase family - ADH1, ADH2, ADH3, ADH5
- CADH; cinnamyl alcohol dehydrogenase family - ADH6, ADH7
Non-zinc-containing enzyme groups:
- NRBP; nuclear receptor binding protein (4) or MRF; mitochondrial respiratory function (6) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (6, 4), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (4)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (4) or ACR; acyl-CoA reductase (6) family - no members in S. cerevisiae
| 1) | Chang A and Fink GR (1995) Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J Cell Biol 128(1-2):39-49 |
| 2) | Bagnat M, et al. (2001) Plasma membrane proton ATPase Pma1p requires raft association for surface delivery in yeast. Mol Biol Cell 12(12):4129-38 |
| 3) | Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 |
| 4) | Riveros-Rosas H, et al. (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34 |
| 5) | Jornvall H, et al. (1981) Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci U S A 78(7):4226-30 |
| 6) | Nordling E, et al. (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76 |
| 7) | Persson B, et al. (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7 |





