AST2/YER101C Summary Help

Standard Name AST2 1
Systematic Name YER101C
Feature Type ORF, Verified
Description Lipid raft associated protein; overexpression restores Pma1p localization to lipid rafts which is required for targeting of Pma1p to the plasma membrane; sometimes classified in the medium-chain dehydrogenase/reductases (MDRs) superfamily; AST2 has a paralog, AST1, that arose from the whole genome duplication (1, 2, 3 and see Summary Paragraph)
Name Description ATPase STabilizing 1
Chromosomal Location
ChrV:361794 to 360502 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All AST2 GO evidence and references
  View Computational GO annotations for AST2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 2 genes
Large-scale survey
12 total interaction(s) for 10 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Biochemical Activity: 1
  • Reconstituted Complex: 2
  • Two-hybrid: 3

Genetic Interactions
  • Negative Genetic: 3
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 430
Molecular Weight (Da) 48,370
Isoelectric Point (pI) 9.59
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:361794 to 360502 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1293 361794..360502 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000903

About the medium-chain dehydrogenase/reductase (MDR) family

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (4), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (5, 3). 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, 3). They contain 0, 1, or 2 zinc atoms (6). 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, 3). 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 (3) 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. (3) 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 (3) or MRF; mitochondrial respiratory function (5) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (5, 3), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (3)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (3) or ACR; acyl-CoA reductase (5) family - no members in S. cerevisiae

Last updated: 2008-08-19 Contact SGD

References cited on this page View Complete Literature Guide for AST2
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) 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
3) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
4) 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
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) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463():373-7