DEGS2_CAEEL
ID DEGS2_CAEEL Reviewed; 362 AA.
AC G5EC63;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Putative sphingolipid delta(4)-desaturase/C4-monooxygenase;
DE EC=1.14.18.5;
DE EC=1.14.19.17;
DE AltName: Full=Sphingolipid 4-desaturase;
DE AltName: Full=Sphingolipid C4-monooxygenase;
GN Name=ttm-5; ORFNames=Y54E5A.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 [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: Bifunctional enzyme which acts as both a sphingolipid
CC delta(4)-desaturase and a sphingolipid C4-monooxygenase.
CC {ECO:0000250|UniProtKB:Q8R2F2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dihydroceramide + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = a
CC phytoceramide + 2 Fe(III)-[cytochrome b5] + H2O;
CC Xref=Rhea:RHEA:55808, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:139048,
CC ChEBI:CHEBI:139051; EC=1.14.18.5;
CC Evidence={ECO:0000250|UniProtKB:Q8R2F2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O;
CC Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:52639; EC=1.14.19.17;
CC Evidence={ECO:0000250|UniProtKB:Q8R2F2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N-octanoylsphinganine + O2
CC = 2 Fe(III)-[cytochrome b5] + H2O + N-octanoyl-4-hydroxysphinganine;
CC Xref=Rhea:RHEA:43116, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:82841,
CC ChEBI:CHEBI:82842; Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43117;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2
CC = an N-acyl-(4R)-4-hydroxysphinganine + 2 Fe(III)-[cytochrome b5] +
CC H2O; Xref=Rhea:RHEA:46364, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:31488,
CC ChEBI:CHEBI:31998; EC=1.14.18.5;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46365;
CC Evidence={ECO:0000250|UniProtKB:Q6QHC5};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; BX284601; CAA21659.2; -; Genomic_DNA.
DR PIR; G87999; G87999.
DR PIR; T27158; T27158.
DR RefSeq; NP_493549.1; NM_061148.3.
DR AlphaFoldDB; G5EC63; -.
DR BioGRID; 38712; 4.
DR IntAct; G5EC63; 2.
DR STRING; 6239.Y54E5A.1; -.
DR EPD; G5EC63; -.
DR PaxDb; G5EC63; -.
DR PeptideAtlas; G5EC63; -.
DR EnsemblMetazoa; Y54E5A.1.1; Y54E5A.1.1; WBGene00013197.
DR EnsemblMetazoa; Y54E5A.1.2; Y54E5A.1.2; WBGene00013197.
DR GeneID; 173327; -.
DR KEGG; cel:CELE_Y54E5A.1; -.
DR CTD; 173327; -.
DR WormBase; Y54E5A.1; CE28791; WBGene00013197; ttm-5.
DR eggNOG; KOG2987; Eukaryota.
DR GeneTree; ENSGT00390000013448; -.
DR HOGENOM; CLU_032156_0_0_1; -.
DR InParanoid; G5EC63; -.
DR OMA; SYYGLWN; -.
DR OrthoDB; 1255438at2759; -.
DR PhylomeDB; G5EC63; -.
DR BRENDA; 1.14.19.17; 1045.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR UniPathway; UPA00222; -.
DR PRO; PR:G5EC63; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013197; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR CDD; cd03508; Delta4-sphingolipid-FADS-like; 1.
DR InterPro; IPR011388; DES1/DES2.
DR InterPro; IPR005804; FA_desaturase_dom.
DR InterPro; IPR013866; Sphingolipid_d4-desaturase_N.
DR Pfam; PF00487; FA_desaturase; 1.
DR Pfam; PF08557; Lipid_DES; 1.
DR PIRSF; PIRSF017228; Sphnglp_dlt4_des; 1.
DR SMART; SM01269; Lipid_DES; 1.
PE 3: Inferred from homology;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Putative sphingolipid delta(4)-desaturase/C4-
FT monooxygenase"
FT /id="PRO_0000421295"
FT TRANSMEM 45..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 89..93
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 128..132
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 259..263
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 42316 MW; 23AFEE5C847EDD76 CRC64;
MGQSVSRDDF IWTLTEQPHM SRREEIVKKY PEVKKLFGVD PSLKYVVSSL VIFQIFMCWL
LQDADWILII LEAYFCGGII NHAMTLAIHD ISHNTAFGNK YPLKNRFFGM WANLPIAVPI
SVSFKKYHVE HHRYLGEDGL DTDVPTTFEA EFFTTAPRKL LWLALQPFFY GFRPLIIYKK
APTDMEILNA IIQISFDLLI LHFFGVKSLF YLLFGTIISM GLHPSAGHFI SEHYAFKEDQ
ETFSYYGLWN LCTFNVGYHV EHHDFPYIPG RDLPKLRAMA PEYYENLLKH TSMMQILTEF
VVNPAMGPYA RLKRKPRVAQ EFYGNYQLFE YVEGFLHHIG VYRLQKFAVN VFDLNNNSKK
LN
