ID   LIP1_KLULA              Reviewed;         147 AA.
AC   Q6CXA2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Ceramide synthase subunit LIP1;
GN   Name=LIP1; OrderedLocusNames=KLLA0A09999g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the ceramide synthase complex required for
CC       synthesis of ceramides. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ceramide synthase complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LIP1 family. {ECO:0000305}.
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DR   EMBL; CR382121; CAH03025.1; -; Genomic_DNA.
DR   RefSeq; XP_451437.1; XM_451437.1.
DR   AlphaFoldDB; Q6CXA2; -.
DR   STRING; 28985.XP_451437.1; -.
DR   EnsemblFungi; CAH03025; CAH03025; KLLA0_A09999g.
DR   GeneID; 2896365; -.
DR   KEGG; kla:KLLA0_A09999g; -.
DR   eggNOG; ENOG502S1YW; Eukaryota.
DR   HOGENOM; CLU_1759093_0_0_1; -.
DR   InParanoid; Q6CXA2; -.
DR   OMA; CDKRGEL; -.
DR   Proteomes; UP000000598; Chromosome A.
DR   GO; GO:0061576; C:acyl-CoA ceramide synthase complex; IEA:EnsemblFungi.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050291; F:sphingosine N-acyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IEA:EnsemblFungi.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..147
FT                   /note="Ceramide synthase subunit LIP1"
FT                   /id="PRO_0000308780"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        10..30
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..147
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   147 AA;  16768 MW;  13BA15322BB5B5E0 CRC64;
     MATQQNKNRV YILLQYVLAA LVLIAAVEYF KYKTRISYEW FHCTVQSEEL FDHPEGSPLK
     LWAIGGPSCD KRGELKTIMK RITMDFDPNV EPVKFCIVED TKVKSIHYPI EDGNKGDPGY
     ISFVGYERDS DVVEQACASY AATVFNL