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Protein

Alkaline ceramidase YPC1

Gene

YPC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes phytoceramide and also dihydroceramide into phytosphingosine or dihydrosphingosine. Prefers phytoceramide. Has also reverse hydrolysis activity, catalyzing synthesis of phytoceramide and dihydroceramide from palmitic acid and phytosphingosine or dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide.

GO - Molecular functioni

  1. phytoceramidase activity Source: SGD
  2. sphingosine N-acyltransferase activity Source: SGD

GO - Biological processi

  1. ceramide biosynthetic process Source: SGD
  2. ceramide catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:YBR183W-MONOMER.
YEAST:YBR183W-MONOMER.
ReactomeiREACT_189220. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline ceramidase YPC1 (EC:3.5.1.-)
Gene namesi
Name:YPC1
Ordered Locus Names:YBR183W
ORF Names:YBR1305
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR183w.
SGDiS000000387. YPC1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei69 – 8921HelicalSequence AnalysisAdd
BLAST
Topological domaini90 – 934LumenalSequence Analysis
Transmembranei94 – 11421HelicalSequence AnalysisAdd
BLAST
Topological domaini115 – 13521CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei136 – 15621HelicalSequence AnalysisAdd
BLAST
Topological domaini157 – 1604LumenalSequence Analysis
Transmembranei161 – 18121HelicalSequence AnalysisAdd
BLAST
Topological domaini182 – 19514CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei196 – 21621HelicalSequence AnalysisAdd
BLAST
Topological domaini217 – 22812LumenalSequence AnalysisAdd
BLAST
Transmembranei229 – 24921HelicalSequence AnalysisAdd
BLAST
Topological domaini250 – 31667CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cortical endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum Source: SGD
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. Golgi membrane Source: UniProtKB-SubCell
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Alkaline ceramidase YPC1PRO_0000212466Add
BLAST

Proteomic databases

PaxDbiP38298.

Expressioni

Gene expression databases

GenevestigatoriP38298.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGP1P253761EBI-2103141,EBI-2357
CHO1P084561EBI-2103141,EBI-14055
ERV29P533371EBI-2103141,EBI-23662
OST1P415431EBI-2103141,EBI-12651
PMP2P409751EBI-2103141,EBI-2043041
RTN1Q049471EBI-2103141,EBI-38020
SAC1P323681EBI-2103141,EBI-16210
SPF1P399861EBI-2103141,EBI-3128
TAF2P232551EBI-2103141,EBI-18862
YHR080CP388001EBI-2103141,EBI-24597

Protein-protein interaction databases

BioGridi32881. 67 interactions.
DIPiDIP-7405N.
IntActiP38298. 30 interactions.
MINTiMINT-1354145.
STRINGi4932.YBR183W.

Structurei

3D structure databases

ProteinModelPortaliP38298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline ceramidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG250726.
GeneTreeiENSGT00730000111189.
HOGENOMiHOG000192011.
InParanoidiP38298.
KOiK05848.
OMAiGSWCFHG.
OrthoDBiEOG76DV3Q.

Family and domain databases

InterProiIPR008901. Ceramidase.
[Graphical view]
PfamiPF05875. Ceramidase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38298-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGIFRWNYPE SSVPGVWGET TSTIDWCEEN YVVSPYIAEW SNTLTNSVFI
60 70 80 90 100
LSAIYTTYSA YKNKLEKRFL LIGFGYGLVG VGSWLFHMTL KYRFQLLDEL
110 120 130 140 150
PMIYAMCIPT WSLVCEAKEA LLNGDNHKKV PLFEQIFIGV IIGLAVTTAS
160 170 180 190 200
ILYVIYKNVD IHQILFGVQI VVVAATAGSL TYRYVHDPLA KRNLKASMAL
210 220 230 240 250
GAILFLSGYI SWLLDIHYCS FWVHVRRSIL ALPLGVLLEP HGWWHILTGM
260 270 280 290 300
GIYFYIVSLE HLRVITLNVS CNYQFIWRWK VFPELIWKGR KPSTRYSLEL
310
FGPYVEDQSI EVKKEK
Length:316
Mass (Da):36,420
Last modified:October 1, 1994 - v1
Checksum:i90DD942A4522508F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191745 Genomic DNA. Translation: AAF43604.1.
U02073 Genomic DNA. Translation: AAB60277.1.
Z36052 Genomic DNA. Translation: CAA85144.1.
BK006936 Genomic DNA. Translation: DAA07298.1.
PIRiS46055.
RefSeqiNP_009742.1. NM_001178531.1.

Genome annotation databases

EnsemblFungiiYBR183W; YBR183W; YBR183W.
GeneIDi852481.
KEGGisce:YBR183W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191745 Genomic DNA. Translation: AAF43604.1.
U02073 Genomic DNA. Translation: AAB60277.1.
Z36052 Genomic DNA. Translation: CAA85144.1.
BK006936 Genomic DNA. Translation: DAA07298.1.
PIRiS46055.
RefSeqiNP_009742.1. NM_001178531.1.

3D structure databases

ProteinModelPortaliP38298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32881. 67 interactions.
DIPiDIP-7405N.
IntActiP38298. 30 interactions.
MINTiMINT-1354145.
STRINGi4932.YBR183W.

Proteomic databases

PaxDbiP38298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR183W; YBR183W; YBR183W.
GeneIDi852481.
KEGGisce:YBR183W.

Organism-specific databases

CYGDiYBR183w.
SGDiS000000387. YPC1.

Phylogenomic databases

eggNOGiNOG250726.
GeneTreeiENSGT00730000111189.
HOGENOMiHOG000192011.
InParanoidiP38298.
KOiK05848.
OMAiGSWCFHG.
OrthoDBiEOG76DV3Q.

Enzyme and pathway databases

BioCyciMetaCyc:YBR183W-MONOMER.
YEAST:YBR183W-MONOMER.
ReactomeiREACT_189220. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi971453.
PROiP38298.

Gene expression databases

GenevestigatoriP38298.

Family and domain databases

InterProiIPR008901. Ceramidase.
[Graphical view]
PfamiPF05875. Ceramidase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme with reverse (CoA-independent) ceramide synthase activity."
    Mao C., Xu R., Bielawska A., Obeid L.M.
    J. Biol. Chem. 275:6876-6884(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes encoding ribosomal proteins and six putative new genes, one of which encodes a putative transcriptional factor."
    Demolis N., Jacquet M., Mallet L.
    Yeast 10:1511-1525(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiYPC1_YEAST
AccessioniPrimary (citable) accession number: P38298
Secondary accession number(s): D6VQH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.