ID   LAGR1_CAEEL             Reviewed;         360 AA.
AC   Q9XWE9;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Probable ceramide synthase lagr-1;
DE            EC=2.3.1.24;
GN   Name=lagr-1; ORFNames=Y6B3B.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the acylation of sphingosine to form ceramides.
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   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sphingosine N-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL032655; CAA21723.1; -; Genomic_DNA.
DR   PIR; T27324; T27324.
DR   RefSeq; NP_493403.1; NM_061002.1.
DR   AlphaFoldDB; Q9XWE9; -.
DR   STRING; 6239.Y6B3B.10; -.
DR   PaxDb; Q9XWE9; -.
DR   EnsemblMetazoa; Y6B3B.10.1; Y6B3B.10.1; WBGene00006505.
DR   GeneID; 189370; -.
DR   KEGG; cel:CELE_Y6B3B.10; -.
DR   UCSC; Y6B3B.10; c. elegans.
DR   CTD; 189370; -.
DR   WormBase; Y6B3B.10; CE20184; WBGene00006505; lagr-1.
DR   eggNOG; KOG1607; Eukaryota.
DR   GeneTree; ENSGT01030000234515; -.
DR   HOGENOM; CLU_028277_0_0_1; -.
DR   InParanoid; Q9XWE9; -.
DR   OMA; LATEKCH; -.
DR   OrthoDB; 987268at2759; -.
DR   PhylomeDB; Q9XWE9; -.
DR   Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:Q9XWE9; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006505; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050291; F:sphingosine N-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR016439; Lag1/Lac1-like.
DR   InterPro; IPR006634; TLC-dom.
DR   PANTHER; PTHR12560; PTHR12560; 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   Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW   Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="Probable ceramide synthase lagr-1"
FT                   /id="PRO_0000421293"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..321
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
SQ   SEQUENCE   360 AA;  42743 MW;  CD9AFCA5CC9378DF CRC64;
     MLGPEYNITH PSIYRTSTAN PIVLAGLVFE SIPHWFRRYA RLRPDYSFPS SMISDFKKVS
     LSNSELYTVL ILASIFTFLR YYLQIRLESW TQQHNIYPRF AHKVPESFWK LTYYGTVWIF
     AFYFHMCVDS HDIFNDPLSM WIEWESGGRP KMHWQVQVIY AVQSAFYIHS IYATLFMDLW
     RKDSWLMFVH HFIALGLLFL SYVDNFTLPG ALVLFLHDNS DATLEITKLS FYLKKRTNRQ
     YYKYYFLMGN AAFILFAIIW VIFRLYWYTC KLLYATIYGA VYLGPQDAPF FPLLGAMLLI
     IFAMNVYWFN FIARMIWRVA LTGEDPEDNR EWDTTAVSGL NQQKLDELAT EKCHLKPKNV