LIP1_CANGA
ID LIP1_CANGA Reviewed; 144 AA.
AC Q6FIK6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Ceramide synthase subunit LIP1;
GN Name=LIP1; OrderedLocusNames=CAGL0M13673g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62918.1; -; Genomic_DNA.
DR RefSeq; XP_449938.1; XM_449938.1.
DR AlphaFoldDB; Q6FIK6; -.
DR STRING; 5478.XP_449938.1; -.
DR EnsemblFungi; CAG62918; CAG62918; CAGL0M13673g.
DR GeneID; 2891229; -.
DR KEGG; cgr:CAGL0M13673g; -.
DR CGD; CAL0136939; CAGL0M13673g.
DR VEuPathDB; FungiDB:CAGL0M13673g; -.
DR eggNOG; ENOG502S1YW; Eukaryota.
DR HOGENOM; CLU_1759093_0_0_1; -.
DR InParanoid; Q6FIK6; -.
DR OMA; CDKRGEL; -.
DR Proteomes; UP000002428; Chromosome M.
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; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..144
FT /note="Ceramide synthase subunit LIP1"
FT /id="PRO_0000308779"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..144
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 144 AA; 16478 MW; C8B3781AEA74AC38 CRC64;
MSTPYTPAPQ IFNLFKVLAV SLALIAAVEY FKYGTRINYE WFHCTPVMER VGGPDSSVLK
IWARGGPSCD KRGEYKTILK RISRDYEPND EHLSFCIKEN MSVDPVHYPI HEDKGEPGYI
AYVGYDSDKR TVDELCEGTT VFHF