AST1/YBL069W Summary Help

AST1 BASIC INFORMATION

Standard Name AST1
Systematic Name YBL069W
Feature Type ORF, Verified
Description Peripheral membrane protein that interacts with the plasma membrane ATPase Pma1p and has a role in its targeting to the plasma membrane, possibly by influencing its incorporation into lipid rafts (1, 2 and see Summary Paragraph)
Name Description ATPase-STabilizing
GO Annotations All AST1 GO evidence and references
    View Computational GO annotations for AST1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All AST1 Phenotype details and references
Large-scale survey
null
Interactions AST1 All interactions details and references
6 total interaction(s) for 4 unique genes/features.
Physical Interactions
  • Biochemical Activity: 1
  • Two-hybrid: 1
Genetic Interactions
  • Dosage Rescue: 1
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 2
Sequence Information
ChrII:90739 to 92028 | ORF Map | GBrowse
This feature contains embedded feature(s): YBL068W-A
Gbrowse
Last Update Coordinates: 2004-01-29 | Sequence: 2001-05-29
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1290 90739..92028 2004-01-29 2001-05-29
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000165

AST1 RESOURCES

Click on map for expanded view
SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for AST1

SUMMARY PARAGRAPH for AST1

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

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (3), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (4, 5). 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 (4). 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 (4).

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) (4, 5). 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 (4, 5). 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 (4) or twenty-one (5) 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. (5) but not by Nordling et al. (4).

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 (5) or MRF; mitochondrial respiratory function (4) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (4, 5), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (5)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (5) or ACR; acyl-CoA reductase (4) family - no members in S. cerevisiae

Last updated: 2008-08-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for AST1]

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) 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
4) 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
5) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
6) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7