ID   LIP1_YEAST              Reviewed;         150 AA.
AC   Q03579; D6W0C5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Ceramide synthase subunit LIP1;
DE   AltName: Full=LAG1/LAC1-interacting protein 1;
GN   Name=LIP1; OrderedLocusNames=YMR298W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   TOPOLOGY, AND INTERACTION WITH LAC1 AND LAG1.
RX   PubMed=15692566; DOI=10.1038/sj.emboj.7600562;
RA   Vallee B., Riezman H.;
RT   "Lip1p: a novel subunit of acyl-CoA ceramide synthase.";
RL   EMBO J. 24:730-741(2005).
CC   -!- FUNCTION: Component of the ceramide synthase complex required for
CC       synthesis of ceramides. {ECO:0000269|PubMed:15692566}.
CC   -!- SUBUNIT: Component of the ceramide synthase complex composed of at
CC       least LAC1, LAG1 and LIP1.
CC   -!- INTERACTION:
CC       Q03579; P28496: LAC1; NbExp=5; IntAct=EBI-27640, EBI-26585;
CC       Q03579; P38703: LAG1; NbExp=3; IntAct=EBI-27640, EBI-10035;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15692566}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:15692566}.
CC   -!- SIMILARITY: Belongs to the LIP1 family. {ECO:0000305}.
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DR   EMBL; X80836; CAA56807.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10199.1; -; Genomic_DNA.
DR   PIR; S47459; S47459.
DR   RefSeq; NP_014027.1; NM_001182807.1.
DR   AlphaFoldDB; Q03579; -.
DR   BioGRID; 35478; 226.
DR   ComplexPortal; CPX-1706; acyl-CoA ceramide synthase complex.
DR   DIP; DIP-4392N; -.
DR   IntAct; Q03579; 3.
DR   STRING; 4932.YMR298W; -.
DR   SwissLipids; SLP:000000917; -.
DR   iPTMnet; Q03579; -.
DR   MaxQB; Q03579; -.
DR   PaxDb; Q03579; -.
DR   PRIDE; Q03579; -.
DR   EnsemblFungi; YMR298W_mRNA; YMR298W; YMR298W.
DR   GeneID; 855344; -.
DR   KEGG; sce:YMR298W; -.
DR   SGD; S000004913; LIP1.
DR   VEuPathDB; FungiDB:YMR298W; -.
DR   eggNOG; ENOG502S1YW; Eukaryota.
DR   HOGENOM; CLU_1759093_0_0_1; -.
DR   InParanoid; Q03579; -.
DR   OMA; CDKRGEL; -.
DR   BioCyc; MetaCyc:MON3O-702; -.
DR   BioCyc; YEAST:MON3O-702; -.
DR   BRENDA; 2.3.1.297; 984.
DR   PRO; PR:Q03579; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03579; protein.
DR   GO; GO:0061576; C:acyl-CoA ceramide synthase complex; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IDA:ComplexPortal.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..150
FT                   /note="Ceramide synthase subunit LIP1"
FT                   /id="PRO_0000203352"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:15692566"
FT   TRANSMEM        21..40
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..150
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:15692566"
SQ   SEQUENCE   150 AA;  17207 MW;  75DBA35225C3065C CRC64;
     MSQPTPIITT KSAAKPKPKI FNLFRVCFIS LLLIAAVEYF KYGTRINYEW FHCTPIKEPQ
     SGSVIKLWAR GGPSCDKRGE YKTIVKRITR DYEPNDEHLS FCIIENDNVP PVHYPIHEDK
     GEPGYVAYVG YDTDSELVQE LCADSTIYHM