LAC1_YEAS7
ID LAC1_YEAS7 Reviewed; 418 AA.
AC A6ZZV7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Sphingosine N-acyltransferase LAC1;
DE EC=2.3.1.24;
GN Name=LAC1; ORFNames=SCY_3367;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Component of the ceramide synthase complex required for C26-
CC CoA-dependent ceramide synthesis. Redundant with LAG1. Facilitates ER-
CC to-Golgi transport of GPI-anchored proteins (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + sphing-4-enine = an N-acylsphing-4-enine +
CC CoA + H(+); Xref=Rhea:RHEA:23768, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57287, ChEBI:CHEBI:57756,
CC ChEBI:CHEBI:77636; EC=2.3.1.24;
CC -!- SUBUNIT: Composed of the ceramide synthase complex composed of at least
CC LAC1, LAG1 and LIP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sphingosine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AAFW02000152; EDN59900.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZV7; -.
DR EnsemblFungi; EDN59900; EDN59900; SCY_3367.
DR HOGENOM; CLU_028277_4_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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:UniProtKB-EC.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:InterPro.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 3: Inferred from homology;
KW Acetylation; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P28496"
FT CHAIN 2..418
FT /note="Sphingosine N-acyltransferase LAC1"
FT /id="PRO_0000308912"
FT TOPO_DOM 2..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..134
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..221
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..296
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..418
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 168..384
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P28496"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38703"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38703"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 418 AA; 48992 MW; 7691BA623AC0460A CRC64;
MSTIKPSPSN NNLKVRSRPR RKSSIGKIDL GDTVPSLGTM FETKESKTAA KRRMQRLSEA
TKNDSDLVKK IWFSFREISY RHAWIAPLMI LIAVYSAYFT SGNTTKTNVL HRFVAVSYQI
GDTNAYGKGI NDLCFVFYYM IFFTFLREFL MDVVIRPFAI RLHVTSKHRI KRIMEQMYAI
FYTGVSGPFG IYCMYHSDLW FFNTKAMYRT YPDFTNPFLF KVFYLGQAAF WAQQACILVL
QLEKPRKDHN ELTFHHIVTL LLIWSSYVFH FTKMGLPIYI TMDVSDFLLS FSKTLNYLDS
GLAFFSFAIF VVAWIYLRHY INLKILWSVL TQFRTEGNYV LNFATQQYKC WISLPIVFVL
IGALQLVNLY WLFLIFRVLY RILWRGILKD DRSDSESDEE SDESSTTPTD STPTKKDI
