YPC1_YEAST
ID YPC1_YEAST Reviewed; 316 AA.
AC P38298; D6VQH8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Alkaline ceramidase YPC1;
DE EC=3.5.1.-;
DE AltName: Full=Acyl-CoA-independent ceramide synthase;
GN Name=YPC1; OrderedLocusNames=YBR183W; ORFNames=YBR1305;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX PubMed=10702247; DOI=10.1074/jbc.275.10.6876;
RA Mao C., Xu R., Bielawska A., Obeid L.M.;
RT "Cloning of an alkaline ceramidase from Saccharomyces cerevisiae. An enzyme
RT with reverse (CoA-independent) ceramide synthase activity.";
RL J. Biol. Chem. 275:6876-6884(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871891; DOI=10.1002/yea.320101116;
RA Demolis N., Jacquet M., Mallet L.;
RT "A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes
RT encoding ribosomal proteins and six putative new genes, one of which
RT encodes a putative transcriptional factor.";
RL Yeast 10:1511-1525(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10900202; DOI=10.1074/jbc.m003683200;
RA Mao C., Xu R., Bielawska A., Szulc Z.M., Obeid L.M.;
RT "Cloning and characterization of a Saccharomyces cerevisiae alkaline
RT ceramidase with specificity for dihydroceramide.";
RL J. Biol. Chem. 275:31369-31378(2000).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11694577; DOI=10.1091/mbc.12.11.3417;
RA Schorling S., Vallee B., Barz W.P., Riezman H., Oesterhelt D.;
RT "Lag1p and Lac1p are essential for the acyl-CoA-dependent ceramide synthase
RT reaction in Saccharomyces cerevisae.";
RL Mol. Biol. Cell 12:3417-3427(2001).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [8]
RP TOPOLOGY.
RX PubMed=23445175; DOI=10.1042/bj20130085;
RA Ramachandra N., Conzelmann A.;
RT "Membrane topology of yeast alkaline ceramidase YPC1.";
RL Biochem. J. 452:585-594(2013).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24866405; DOI=10.1111/1567-1364.12169;
RA Voynova N.S., Mallela S.K., Vazquez H.M., Cerantola V., Sonderegger M.,
RA Knudsen J., Ejsing C.S., Conzelmann A.;
RT "Characterization of yeast mutants lacking alkaline ceramidases YPC1 and
RT YDC1.";
RL FEMS Yeast Res. 14:776-788(2014).
CC -!- FUNCTION: Alkaline ceramidase that hydrolyzes phytoceramide and also
CC dihydroceramide into phytosphingosine or dihydrosphingosine. Prefers
CC phytoceramide. Has also reverse activity as acyl-CoA-independent
CC ceramide synthase, catalyzing synthesis of phytoceramide and
CC dihydroceramide from palmitic acid and phytosphingosine or
CC dihydrosphingosine. Is not responsible for the breakdown of unsaturated
CC ceramide (PubMed:10702247, PubMed:10900202, PubMed:11694577,
CC PubMed:24866405). Preferentially uses very long chain fatty acids (C-24
CC and C-26) in vivo compared to C-16 in vitro (PubMed:24866405).
CC {ECO:0000269|PubMed:10702247, ECO:0000269|PubMed:10900202,
CC ECO:0000269|PubMed:11694577, ECO:0000269|PubMed:24866405}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexanoyl-sphinganine = hexanoate + sphinganine;
CC Xref=Rhea:RHEA:38887, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:76226;
CC Evidence={ECO:0000269|PubMed:10702247, ECO:0000269|PubMed:10900202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38888;
CC Evidence={ECO:0000305|PubMed:10702247, ECO:0000305|PubMed:10900202};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + sphinganine = H2O + N-hexadecanoylsphinganine;
CC Xref=Rhea:RHEA:43440, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57817, ChEBI:CHEBI:67042;
CC Evidence={ECO:0000269|PubMed:10900202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43441;
CC Evidence={ECO:0000305|PubMed:10900202};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-(4R)-hydroxysphinganine = (4R)-
CC hydroxysphinganine + hexadecanoate; Xref=Rhea:RHEA:33755,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:64124,
CC ChEBI:CHEBI:65107; Evidence={ECO:0000269|PubMed:10702247,
CC ECO:0000269|PubMed:10900202};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33756;
CC Evidence={ECO:0000305|PubMed:10702247, ECO:0000305|PubMed:10900202};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33757;
CC Evidence={ECO:0000305|PubMed:10702247, ECO:0000305|PubMed:10900202};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-
CC enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:72959;
CC Evidence={ECO:0000269|PubMed:10702247};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892;
CC Evidence={ECO:0000305|PubMed:10702247};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-(4R)-4-hydroxysphinganine + H2O = (4R)-
CC hydroxysphinganine + a fatty acid; Xref=Rhea:RHEA:33555,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:31998,
CC ChEBI:CHEBI:64124; Evidence={ECO:0000269|PubMed:11694577};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33557;
CC Evidence={ECO:0000305|PubMed:11694577};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10900202, ECO:0000269|PubMed:24866405}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the cortical ER.
CC {ECO:0000269|PubMed:24866405}.
CC -!- SIMILARITY: Belongs to the alkaline ceramidase family. {ECO:0000305}.
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DR EMBL; AF191745; AAF43604.1; -; Genomic_DNA.
DR EMBL; U02073; AAB60277.1; -; Genomic_DNA.
DR EMBL; Z36052; CAA85144.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07298.1; -; Genomic_DNA.
DR PIR; S46055; S46055.
DR RefSeq; NP_009742.1; NM_001178531.1.
DR AlphaFoldDB; P38298; -.
DR SMR; P38298; -.
DR BioGRID; 32881; 272.
DR DIP; DIP-7405N; -.
DR IntAct; P38298; 30.
DR MINT; P38298; -.
DR STRING; 4932.YBR183W; -.
DR SwissLipids; SLP:000000372; -.
DR PaxDb; P38298; -.
DR PRIDE; P38298; -.
DR EnsemblFungi; YBR183W_mRNA; YBR183W; YBR183W.
DR GeneID; 852481; -.
DR KEGG; sce:YBR183W; -.
DR SGD; S000000387; YPC1.
DR VEuPathDB; FungiDB:YBR183W; -.
DR eggNOG; KOG2329; Eukaryota.
DR GeneTree; ENSGT00730000110920; -.
DR HOGENOM; CLU_063293_3_0_1; -.
DR InParanoid; P38298; -.
DR OMA; IMFEPLR; -.
DR BioCyc; MetaCyc:YBR183W-MON; -.
DR BioCyc; YEAST:YBR183W-MON; -.
DR BRENDA; 3.5.1.23; 984.
DR PRO; PR:P38298; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38298; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0070774; F:phytoceramidase activity; IMP:SGD.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IMP:SGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; IGI:SGD.
DR GO; GO:0046514; P:ceramide catabolic process; IMP:SGD.
DR InterPro; IPR008901; ACER.
DR PANTHER; PTHR46187; PTHR46187; 1.
DR Pfam; PF05875; Ceramidase; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..316
FT /note="Alkaline ceramidase YPC1"
FT /id="PRO_0000212466"
FT TOPO_DOM 1..36
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:23445175,
FT ECO:0000305|PubMed:16847258"
FT INTRAMEM 37..57
FT /evidence="ECO:0000305|PubMed:23445175"
FT TOPO_DOM 58..68
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT INTRAMEM 69..89
FT /evidence="ECO:0000305|PubMed:23445175"
FT TOPO_DOM 90..93
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..160
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT INTRAMEM 161..181
FT /evidence="ECO:0000305|PubMed:23445175"
FT TOPO_DOM 182..195
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT INTRAMEM 196..216
FT /evidence="ECO:0000305|PubMed:23445175"
FT TOPO_DOM 217..228
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:23445175"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000269|PubMed:23445175"
FT DISULFID 27..219
FT /evidence="ECO:0000269|PubMed:23445175"
SQ SEQUENCE 316 AA; 36420 MW; 90DD942A4522508F CRC64;
MGIFRWNYPE SSVPGVWGET TSTIDWCEEN YVVSPYIAEW SNTLTNSVFI LSAIYTTYSA
YKNKLEKRFL LIGFGYGLVG VGSWLFHMTL KYRFQLLDEL PMIYAMCIPT WSLVCEAKEA
LLNGDNHKKV PLFEQIFIGV IIGLAVTTAS ILYVIYKNVD IHQILFGVQI VVVAATAGSL
TYRYVHDPLA KRNLKASMAL GAILFLSGYI SWLLDIHYCS FWVHVRRSIL ALPLGVLLEP
HGWWHILTGM GIYFYIVSLE HLRVITLNVS CNYQFIWRWK VFPELIWKGR KPSTRYSLEL
FGPYVEDQSI EVKKEK
