DEGS_CANAL
ID DEGS_CANAL Reviewed; 370 AA.
AC Q5AJX2; A0A1D8PP83;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000303|PubMed:11937514};
DE EC=1.14.19.17 {ECO:0000269|PubMed:11937514};
DE AltName: Full=Delta 4-(E)-sphingolipid desaturase {ECO:0000250|UniProtKB:C4R613};
DE AltName: Full=Dihydroceramide desaturase {ECO:0000303|PubMed:11937514};
GN Name=DES1 {ECO:0000303|PubMed:11937514};
GN OrderedLocusNames=CAALFM_C505480WA; ORFNames=CaO19.11530, CaO19.4048;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=11937514; DOI=10.1074/jbc.m202947200;
RA Ternes P., Franke S., Zaehringer U., Sperling P., Heinz E.;
RT "Identification and characterization of a sphingolipid delta 4-desaturase
RT family.";
RL J. Biol. Chem. 277:25512-25518(2002).
CC -!- FUNCTION: Delta(4)-fatty-acid desaturase which introduces a double bond
CC at the 4-position in the long-chain base (LCB) of ceramides. Required
CC for the formation of the monounsaturated sphingoid base (E)-sphing-4-
CC enine during glucosylceramide (GluCer) biosynthesis.
CC {ECO:0000269|PubMed:11937514}.
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:0000269|PubMed:11937514};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:11937514}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017627; AOW29951.1; -; Genomic_DNA.
DR RefSeq; XP_721956.1; XM_716863.2.
DR AlphaFoldDB; Q5AJX2; -.
DR STRING; 237561.Q5AJX2; -.
DR EnsemblFungi; KHC75437; KHC75437; W5Q_04566.
DR GeneID; 3636529; -.
DR KEGG; cal:CAALFM_C505480WA; -.
DR CGD; CAL0000198792; DES1.
DR VEuPathDB; FungiDB:C5_05480W_A; -.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_1_1; -.
DR InParanoid; Q5AJX2; -.
DR OMA; FTYIHLL; -.
DR OrthoDB; 1255438at2759; -.
DR BRENDA; 1.14.19.17; 1096.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q5AJX2; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; ISA:CGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISA:CGD.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW Lipid metabolism; Membrane; Oxidoreductase; Reference proteome;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..370
FT /note="Sphingolipid delta(4)-desaturase"
FT /id="PRO_0000434803"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 112..116
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 149..153
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 299..303
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 43395 MW; D2B9CB25D097E452 CRC64;
MDAEIKHRNS DKTFKFVTPP ADSSIEVLND FYWTDTDEPH VARRKMILQK YPEVTKLTGH
EPKTKWYVMG VVLLQLGIAY YLRHTPVFSW KFLTLAYVIG ATANQAIFLA IHELSHNLLF
RKPLHNKLFA VFANIPIGVP YSASFQPYHQ LHHKFLGDMY LDTDLPTEYE GRFLSSMPGK
LFFAIFQIFF YALRPMFITQ IKFTYVHLVN VVFQLIFDHV MVTCWGWKAL GYFIVSTFLA
GSLHPCAGHF IAEHYVLNEN NVPRHQKIGG TNISKELLPA ETYSYYGTLN MLTWNVGYHN
EHHDFPYIAW TRLPELRRIA AEFYDPLPQV TSWCGVIWWF IFNDVNTVWN RVKREGKEKH
GYRINRLDEN
