DEGS_SCHPO
ID DEGS_SCHPO Reviewed; 362 AA.
AC O59715;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Sphingolipid delta(4)-desaturase {ECO:0000250|UniProtKB:Q5AJX2};
DE EC=1.14.19.17 {ECO:0000269|PubMed:12633877};
DE AltName: Full=Delta 4-(E)-sphingolipid desaturase {ECO:0000250|UniProtKB:C4R613};
DE AltName: Full=Dihydroceramide desaturase {ECO:0000303|PubMed:12633877};
GN Name=dsd1; ORFNames=SPBC3B8.07c {ECO:0000312|PomBase:SPBC3B8.07c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12633877; DOI=10.1016/s0014-5793(03)00163-7;
RA Garton S., Michaelson L.V., Beaudoin F., Beale M.H., Napier J.A.;
RT "The dihydroceramide desaturase is not essential for cell viability in
RT Schizosaccharomyces pombe.";
RL FEBS Lett. 538:192-196(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(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 sphingosine biosynthesis. {ECO:0000269|PubMed:12633877}.
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:12633877};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:12633877}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Results in the dramatic reduction in the
CC endogenous levels of sphingosine. {ECO:0000269|PubMed:12633877}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family. DEGS
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA18296.1; -; Genomic_DNA.
DR PIR; T40333; T40333.
DR RefSeq; NP_596407.1; NM_001022326.2.
DR AlphaFoldDB; O59715; -.
DR BioGRID; 277534; 13.
DR STRING; 4896.SPBC3B8.07c.1; -.
DR SwissLipids; SLP:000001867; -.
DR iPTMnet; O59715; -.
DR MaxQB; O59715; -.
DR PaxDb; O59715; -.
DR EnsemblFungi; SPBC3B8.07c.1; SPBC3B8.07c.1:pep; SPBC3B8.07c.
DR GeneID; 2541019; -.
DR KEGG; spo:SPBC3B8.07c; -.
DR PomBase; SPBC3B8.07c; dsd1.
DR VEuPathDB; FungiDB:SPBC3B8.07c; -.
DR eggNOG; KOG2987; Eukaryota.
DR HOGENOM; CLU_032156_0_1_1; -.
DR InParanoid; O59715; -.
DR OMA; FTYIHLL; -.
DR PhylomeDB; O59715; -.
DR BRENDA; 1.14.19.17; 5613.
DR Reactome; R-SPO-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR UniPathway; UPA00222; -.
DR PRO; PR:O59715; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042284; F:sphingolipid delta-4 desaturase activity; IDA:PomBase.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:PomBase.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IDA:PomBase.
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..362
FT /note="Sphingolipid delta(4)-desaturase"
FT /id="PRO_0000185433"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..114
FT /note="Histidine box-1"
FT /evidence="ECO:0000305"
FT MOTIF 147..151
FT /note="Histidine box-2"
FT /evidence="ECO:0000305"
FT MOTIF 290..294
FT /note="Histidine box-3"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41810 MW; 5388DF42687B9429 CRC64;
MAESTATTTA VPPPAEESWN ADSEDVHQFY WTYTEEPHKS RRAAILKAHP EIASLNGYEP
LTKWIVLGVV SLQFTCAYLL SQSSLLSWKF FLTAYFIGAF CNQNLFLAIH ELSHNLGFKK
TLYNRAYCLF ANLPVGAPFA ASFRPYHMEH HAYQGVDGMD TDLPTRAELI LFDNVLGKAF
FCTFQLLFYA FRPLVVRRLP FTLMHFWNII VQFSFDYLVV RYVGWRALAY FFMSSFLAGS
LHPTAGHFLS EHYNMTRTRL IASGPGKETP LETFSYYGPL NFFVYNAGYH IEHHDFPYVA
WTRIGKVREL APEFYDNIPD CKSWCGIIYQ FITDSNVGMW CRVKRKQKHA DIPTKSMHLH
VS
