ATH1/YPR026W Summary Help

Standard Name ATH1 1
Systematic Name YPR026W
Feature Type ORF, Verified
Description Acid trehalase required for utilization of extracellular trehalose; involved in intracellular trehalose degradation during growth recovery after saline stress (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description Acid TreHalase 1
Chromosomal Location
ChrXVI:615379 to 619014 | ORF Map | GBrowse
Gene Ontology Annotations All ATH1 GO evidence and references
  View Computational GO annotations for ATH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
25 total interaction(s) for 20 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Biochemical Activity: 1

Genetic Interactions
  • Dosage Rescue: 3
  • Negative Genetic: 4
  • Phenotypic Enhancement: 5
  • Positive Genetic: 5
  • Synthetic Growth Defect: 1
  • Synthetic Rescue: 3

Expression Summary
Length (a.a.) 1,211
Molecular Weight (Da) 136,919
Isoelectric Point (pI) 5.15
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXVI:615379 to 619014 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3636 615379..619014 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 | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000006230

Trehalose is a storage carbohydrate that can either be synthesized by the cell or obtained from the external environment, and is converted by trehalase with water into two glucose molecules (6). S. cerevisiae has two trehalase enzymes, an acid trehalase encoded by ATH1 (2) and a neutral trehalase encoded by NTH1 (7). A third locus, NTH2, is 77% identical to NTH1, but does not appear to encode a trehalase activity, or be involved in trehalose catabolism, since an nth2 null mutant exhibits normal levels of neutral trehalase activity and trehalose (8).

Extracellular trehalose is degraded by Ath1p (4), which was originally predicted to be a vacuolar protein, but has since been experimentally shown to localize mainly in the periplasmic space, with a small fraction also occurring in the cell wall (4). ATH1 does not appear to be stress-induced (9). Deletion of ATH1 results in complete loss of acid trehalase activity and an inability to use trehalose as a carbon source (3).

Last updated: 2005-08-12 Contact SGD

References cited on this page View Complete Literature Guide for ATH1
1) Destruelle M, et al.  (1995) Isolation and characterization of a novel yeast gene, ATH1, that is required for vacuolar acid trehalase activity. Yeast 11(11):1015-25
2) Alizadeh P and Klionsky DJ  (1996) Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae. FEBS Lett 391(3):273-8
3) Nwaka S, et al.  (1996) Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. FEBS Lett 386(2-3):235-8
4) Jules M, et al.  (2004) Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae. Appl Environ Microbiol 70(5):2771-8
5) Garre E and Matallana E  (2009) The three trehalases Nth1p, Nth2p and Ath1p participate in the mobilization of intracellular trehalose required for recovery from saline stress in Saccharomyces cerevisiae. Microbiology 155(Pt 9):3092-9
6) Francois J and Parrou JL  (2001) Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 25(1):125-45
7) Kopp M, et al.  (1993) Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae. J Biol Chem 268(7):4766-74
8) Nwaka S, et al.  (1995) Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae. J Biol Chem 270(17):10193-8
9) Zahringer H, et al.  (1997) Neutral trehalase Nth1p of Saccharomyces cerevisiae encoded by the NTH1 gene is a multiple stress responsive protein. FEBS Lett 412(3):615-20