ID   DEGS1_CAEEL             Reviewed;         360 AA.
AC   O44186;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative sphingolipid delta(4)-desaturase;
DE            EC=1.14.19.17 {ECO:0000250|UniProtKB:O15121};
GN   ORFNames=F33D4.4;
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: Acts as a sphingolipid delta(4)-desaturase. {ECO:0000250}.
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:O15121};
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; FO080445; CCD63769.1; -; Genomic_DNA.
DR   PIR; T32554; T32554.
DR   RefSeq; NP_501256.1; NM_068855.4.
DR   AlphaFoldDB; O44186; -.
DR   STRING; 6239.F33D4.4.1; -.
DR   EPD; O44186; -.
DR   PaxDb; O44186; -.
DR   PeptideAtlas; O44186; -.
DR   EnsemblMetazoa; F33D4.4.1; F33D4.4.1; WBGene00017996.
DR   EnsemblMetazoa; F33D4.4.2; F33D4.4.2; WBGene00017996.
DR   GeneID; 177548; -.
DR   KEGG; cel:CELE_F33D4.4; -.
DR   UCSC; F33D4.4.1; c. elegans.
DR   CTD; 177548; -.
DR   WormBase; F33D4.4; CE17034; WBGene00017996; -.
DR   eggNOG; KOG2987; Eukaryota.
DR   GeneTree; ENSGT00390000013448; -.
DR   HOGENOM; CLU_032156_0_0_1; -.
DR   InParanoid; O44186; -.
DR   OMA; FIWVLLQ; -.
DR   OrthoDB; 1255438at2759; -.
DR   PhylomeDB; O44186; -.
DR   Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   UniPathway; UPA00222; -.
DR   PRO; PR:O44186; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00017996; Expressed in adult organism and 4 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..360
FT                   /note="Putative sphingolipid delta(4)-desaturase"
FT                   /id="PRO_0000421294"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           90..94
FT                   /note="Histidine box-1"
FT                   /evidence="ECO:0000305"
FT   MOTIF           129..133
FT                   /note="Histidine box-2"
FT                   /evidence="ECO:0000305"
FT   MOTIF           260..264
FT                   /note="Histidine box-3"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  41686 MW;  F2ABB45F74FD3E6D CRC64;
     MGQAPAKEED FSWAYTEEPH ASRRKEILAK YPQIKELFGQ DKAFRPVVVC MVIAQIVFAY
     LLRDSDWLLI LFQAYFVSGT INHSLTLAVH EISHNQAFGT NRPLANRIFG FIANLPMCIP
     MSISFKKYHL EHHRNLGEDV IDTDVPTEFE AKVFRTWLGK MIWMSLQPLF YGIRPFMLYP
     KSMTDLELIN VAIQLLFSTF IYTQFGAKSF FFLFGGLVLG MGLHPCAGHF VSEHYVFKKD
     QETYSYYGPI NMVVFNVGYH VEHHDFPYIT GSNLPKVREI APEYYQDWQT HDSWVGMMAD
     FIFNPKMTLR KRIKRKYAKP DQFSFYGTGP YETSHVYQSI ANVVNMLTGF GGRKSVVKCD