HYL1_CAEEL
ID HYL1_CAEEL Reviewed; 368 AA.
AC G5ED45;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Ceramide synthase hyl-1 {ECO:0000303|PubMed:19372430};
DE Short=HYL-1 {ECO:0000303|PubMed:19372430};
DE EC=2.3.1.24 {ECO:0000305|PubMed:19372430};
GN Name=hyl-1; ORFNames=C09G4.1;
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 [MRNA].
RX PubMed=9872981; DOI=10.1101/gr.8.12.1259;
RA Jiang J.C., Kirchman P.A., Zagulski M., Hunt J., Jazwinski S.M.;
RT "Homologs of the yeast longevity gene LAG1 in Caenorhabditis elegans and
RT human.";
RL Genome Res. 8:1259-1272(1998).
RN [2]
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19372430; DOI=10.1126/science.1168532;
RA Menuz V., Howell K.S., Gentina S., Epstein S., Riezman I.,
RA Fornallaz-Mulhauser M., Hengartner M.O., Gomez M., Riezman H.,
RA Martinou J.C.;
RT "Protection of C. elegans from anoxia by HYL-2 ceramide synthase.";
RL Science 324:381-384(2009).
CC -!- FUNCTION: Catalyzes the acylation of sphingoid bases to form ceramides.
CC Sphingolipids from Caenorhabditis elegans contain exclusively
CC isosphingoid bases. Exhibits substrate preference for fatty acyl-coA
CC chains containing 24 and 26 carbons. {ECO:0000269|PubMed:19372430}.
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 Evidence={ECO:0000305|PubMed:19372430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23769;
CC Evidence={ECO:0000305|PubMed:19372430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-methylhexadecasphinganine + a fatty acyl-CoA = CoA + H(+) +
CC N-acyl-15-methylhexadecasphinganine; Xref=Rhea:RHEA:34603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:70829,
CC ChEBI:CHEBI:70845, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:19372430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34604;
CC Evidence={ECO:0000269|PubMed:19372430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + sphinganine = an N-acylsphinganine + CoA +
CC H(+); Xref=Rhea:RHEA:34735, ChEBI:CHEBI:15378, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57817, ChEBI:CHEBI:77636;
CC Evidence={ECO:0000269|PubMed:19372430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34736;
CC Evidence={ECO:0000269|PubMed:19372430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=sphinganine + tetradecanoyl-CoA = CoA + H(+) + N-
CC (tetradecanoyl)-sphinganine; Xref=Rhea:RHEA:36571, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:67045; Evidence={ECO:0000269|PubMed:19372430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36572;
CC Evidence={ECO:0000269|PubMed:19372430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexacosanoyl-CoA + sphinganine = CoA + H(+) + N-
CC hexacosanoylsphinganine; Xref=Rhea:RHEA:33351, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:52962, ChEBI:CHEBI:57287, ChEBI:CHEBI:57817,
CC ChEBI:CHEBI:64868; Evidence={ECO:0000269|PubMed:19372430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33352;
CC Evidence={ECO:0000269|PubMed:19372430};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:19372430}.
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; AF105010; AAD16893.1; -; mRNA.
DR EMBL; FO080478; CCD63994.1; -; Genomic_DNA.
DR RefSeq; NP_501459.1; NM_069058.6.
DR AlphaFoldDB; G5ED45; -.
DR STRING; 6239.C09G4.1.2; -.
DR SwissLipids; SLP:000000002; -.
DR SwissLipids; SLP:000000177; -.
DR SwissLipids; SLP:000000180; -.
DR SwissLipids; SLP:000000182; -.
DR EPD; G5ED45; -.
DR PaxDb; G5ED45; -.
DR PeptideAtlas; G5ED45; -.
DR EnsemblMetazoa; C09G4.1a.1; C09G4.1a.1; WBGene00002043.
DR GeneID; 177660; -.
DR CTD; 177660; -.
DR WormBase; C09G4.1a; CE27675; WBGene00002043; hyl-1.
DR eggNOG; KOG1607; Eukaryota.
DR HOGENOM; CLU_028277_1_0_1; -.
DR InParanoid; G5ED45; -.
DR PhylomeDB; G5ED45; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:G5ED45; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002043; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; G5ED45; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:WormBase.
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; ISS:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 2.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..368
FT /note="Ceramide synthase hyl-1"
FT /id="PRO_0000421291"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 90..303
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 306..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 43851 MW; 4DC64ABA6C5046FE CRC64;
MWRMSYFWHE PYWLPRNVTW PEVPAKFVDL LVPIYLAIPL VIIRILWEST IGVTYLYFRT
NAYASRKNIT LLGCMWEHMT GGFASVSRAK KILECFWRFS YYTFAFLYGL YVMKNSSWLY
DVKQCWIGYP FHPVPDTIWW YYMIETGFYY SLLIGSTFDV RRSDFWQLMV HHVITIFLLS
SSWTINFVRV GTLILLSHDV SDVFLEGGKL VRYDAHNKNM TNFMFVLFFS SWVATRLIYY
PFIVIRSAVT EAAALIQPDY ILWDYQLSPP YAPRLIVFAL ILLFFLHIFW TFIILRIAYR
TSTGGQAKDV RSDSDSDYDE EEMARRERTR LLKKKKNKVS PSTDDDDDEG EEEKNDRKAR
HRRAPRKE
