ID   LAG1_YEAS7              Reviewed;         411 AA.
AC   A6ZSP9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Sphingosine N-acyltransferase LAG1;
DE            EC=2.3.1.24;
DE   AltName: Full=Longevity assurance factor 1;
DE   AltName: Full=Longevity assurance protein 1;
GN   Name=LAG1; ORFNames=SCY_2383;
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 to LAC1. Facilitates ER-to-
CC       Golgi transport of GPI-anchored proteins. Involved in the aging process
CC       (By similarity). {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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFW02000082; EDN62230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZSP9; -.
DR   PRIDE; A6ZSP9; -.
DR   EnsemblFungi; EDN62230; EDN62230; SCY_2383.
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   SMART; SM00724; TLC; 1.
DR   PROSITE; PS50922; TLC; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Phosphoprotein; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..411
FT                   /note="Sphingosine N-acyltransferase LAG1"
FT                   /id="PRO_0000308913"
FT   TOPO_DOM        1..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..134
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..211
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..251
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..296
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        318..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..411
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          168..384
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT   REGION          390..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   411 AA;  48470 MW;  C3A2847B9613EB9E CRC64;
     MTSATDKSID RLVVNAKTRR RNSSVGKIDL GDTVPGFAAM PESAASKNEA KKRMKALTGD
     SKKDSDLLWK VWFSYREMNY RHSWLTPFFI LVCVYSAYFL SGNRTESNPL HMFVAISYQV
     DGTDSYAKGI KDLSFVFFYM IFFTFLREFL MDVVIRPFTV YLNVTSEHRQ KRMLEQMYAI
     FYCGVSGPFG LYIMYHSDLW LFKTKPMYRT YPDITNPFLF KIFYLGQAAF WAQQACVLVL
     QLEKPRKDYK ELVFHHIVTL LLIWSSYVFH FTKMGLAIYI TMDVSDFFLS LSKTLNYLNS
     VFTPFVFGLF VFFWIYLRHV VNIRILWSVL TEFRHEGNYV LNFATQQYKC WISLPIVFVL
     IAALQLVNLY WLFLILRILY RLIWQGIQKD ERSDSDSDES AENEESKEKC E