YML131W Summary 
| Systematic Name | YML131W |
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| Feature Type | ORF, Verified |
| Description | Protein of unknown function; similar to medium chain dehydrogenase/reductases; expression induced by stresses including osmotic shock, DNA damaging agents, and other chemicals; GFP-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress (1, 2, 3, 4, 5, 6, 7, 8, 9, 10 and see Summary Paragraph) |
| Chromosomal Location | |
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| View Computational GO annotations for YML131W | |
| Molecular Function | |
| Manually curated |
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| Biological Process | |
| Manually curated |
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| Cellular Component | |
| High-throughput |
| 14 total interaction(s) for 14 unique genes/features. | |
| Physical Interactions |
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| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
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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 | S000004600 |
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About the medium-chain dehydrogenase/reductase (MDR) family
Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (11), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (5, 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 (5). 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 (5).
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) (5, 4). They contain 0, 1, or 2 zinc atoms (12). 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 (5, 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 (5) 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. (5).
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 (5) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (5, 4), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (4)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (4) or ACR; acyl-CoA reductase (5) family - no members in S. cerevisiae
Last updated: 2008-08-19 
| 1) | Rep M, et al. (2001) The Saccharomyces cerevisiae Sko1p transcription factor mediates HOG pathway-dependent osmotic regulation of a set of genes encoding enzymes implicated in protection from oxidative damage. Mol Microbiol 40(5):1067-83 |
| 2) | Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 |
| 3) | Jelinsky SA and Samson LD (1999) Global response of Saccharomyces cerevisiae to an alkylating agent. Proc Natl Acad Sci U S A 96(4):1486-91 |
| 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) | 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 |
| 6) | Lee MW, et al. (2007) Global protein expression profiling of budding yeast in response to DNA damage. Yeast 24(3):145-54 |
| 7) | Iwahashi H, et al. (2007) Evaluation of toxicity of the mycotoxin citrinin using yeast ORF DNA microarray and Oligo DNA microarray. BMC Genomics 8:95 |
| 8) | Del Vescovo V, et al. (2008) Role of Hog1 and Yaf9 in the transcriptional response of Saccharomyces cerevisiae to cesium chloride. Physiol Genomics 33(1):110-20 |
| 9) | Trott A, et al. (2008) Activation of Heat Shock and Antioxidant Responses by the Natural Product Celastrol: Transcriptional Signatures of a Thiol-targeted Molecule. Mol Biol Cell 19(3):1104-12 |
| 10) | Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 |
| 11) | 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 |
| 12) | Persson B, et al. (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7 |
