YPC1/YBR183W Summary Help

Standard Name YPC1 1
Systematic Name YBR183W
Feature Type ORF, Verified
Description Alkaline ceramidase; also has reverse (CoA-independent) ceramide synthase activity; catalyzes both breakdown and synthesis of phytoceramide; overexpression confers fumonisin B1 resistance; YPC1 has a paralog, YDC1, that arose from the whole genome duplication (1, 2, 3 and see Summary Paragraph)
Name Description Yeast Phyto-Ceramidase 1
Gene Product Alias alkaline ceramidase 1
Chromosomal Location
ChrII:596115 to 597065 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All YPC1 GO evidence and references
  View Computational GO annotations for YPC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 8 genes
Resources
Pathways
Classical genetics
null
overexpression
Large-scale survey
null
Resources
79 total interaction(s) for 67 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 2
  • PCA: 34

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 1
  • Dosage Rescue: 7
  • Negative Genetic: 18
  • Phenotypic Enhancement: 2
  • Positive Genetic: 9
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 3
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 316
Molecular Weight (Da) 36,419
Isoelectric Point (pI) 8.35
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:596115 to 597065 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..951 596115..597065 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000387
SUMMARY PARAGRAPH for YPC1

About sphingolipid metabolism

Sphingolipids are essential components of the plasma membrane in all eukaryotic cells. S. cerevisiae cells make three complex sphingolipids: inositol-phosphoceramide (IPC), mannose-inositol-phosphoceramide (MIPC), and mannose-(inositol phosphate)2-ceramide (M(IP)2C)(4). In the yeast plasma membrane sphingolipids concentrate with ergosterol to form lipid rafts, specialized membrane microdomains implicated in a variety of cellular processes, including sorting of membrane proteins and lipids, as well as organizing and regulating signaling cascades (5). Intermediates in sphingolipid biosynthesis have been shown to play important roles as signaling molecules and growth regulators. Sphingolipid long chain bases (LCBs), dihydrosphingosine (DHS) and phytosphingosine (PHS), have been implicated as secondary messengers in signaling pathways that regulate the heat stress response (6, 7). Other intermediates, phytoceramide and long-chain base phosphates (LCBPs), have been shown to be components of the tightly-controlled ceramide/LCBP rheostat, which regulates cell growth (8). Since phosphoinositol-containing sphingolipids are unique to fungi, the sphingolipid biosynthesis pathway is considered a target for antifungal drugs (9, 10).

YPC1 and YDC1 are homologous genes that encode alkaline ceramidase. Ceramide is an intermediate in the sphingolipid biosynthesis pathway and has been shown in mammals to have a role in apoptosis and the stress response. Ceramidase activity is conserved in eukaryotic and prokaryotic systems. Ypc1p has specificity for phytoceramide while Ydc1p has specificity for dihydroceramide. In the presence of fumonisin B1, a mycotoxin and ceramide synthase inhibitor, Ypc1p has a acyl-CoA-independent reverse activity that results in ceramide production, and thus can function as a ceramide synthase. Dual activity of Ypc1p suggests the possibility that a salvage pathway to synthesize ceramides exists in yeast (11, 1, 2).

Last updated: 2007-10-05 Contact SGD

References cited on this page View Complete Literature Guide for YPC1
1) Mao C, et al.  (2000) Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity. J Biol Chem 275(10):6876-84
2) Mao C, et al.  (2000) Cloning and characterization of a Saccharomyces cerevisiae alkaline ceramidase with specificity for dihydroceramide. J Biol Chem 275(40):31369-78
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) Dickson RC and Lester RL  (2002) Sphingolipid functions in Saccharomyces cerevisiae. Biochim Biophys Acta 1583(1):13-25
5) Bagnat M and Simons K  (2002) Lipid rafts in protein sorting and cell polarity in budding yeast Saccharomyces cerevisiae. Biol Chem 383(10):1475-80
6) Jenkins GM, et al.  (1997) Involvement of yeast sphingolipids in the heat stress response of Saccharomyces cerevisiae. J Biol Chem 272(51):32566-72
7) Ferguson-Yankey SR, et al.  (2002) Mutant analysis reveals complex regulation of sphingolipid long chain base phosphates and long chain bases during heat stress in yeast. Yeast 19(7):573-86
8) Kobayashi SD and Nagiec MM  (2003) Ceramide/long-chain base phosphate rheostat in Saccharomyces cerevisiae: regulation of ceramide synthesis by Elo3p and Cka2p. Eukaryot Cell 2(2):284-94
9) Nagiec MM, et al.  (1997) Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J Biol Chem 272(15):9809-17
10) Sugimoto Y, et al.  (2004) IPC synthase as a useful target for antifungal drugs. Curr Drug Targets Infect Disord 4(4):311-22
11) Schorling S, et al.  (2001) Lag1p and Lac1p are essential for the Acyl-CoA-dependent ceramide synthase reaction in Saccharomyces cerevisae. Mol Biol Cell 12(11):3417-27