SLS1_TRYBB
ID SLS1_TRYBB Reviewed; 355 AA.
AC B3A0L9;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase {ECO:0000303|PubMed:20457606};
DE Short=TbSLS1 {ECO:0000303|PubMed:18699867, ECO:0000303|PubMed:20457606};
DE EC=2.7.8.- {ECO:0000269|PubMed:20457606};
DE AltName: Full=Inositol-phosphorylceramide synthase {ECO:0000303|PubMed:20457606};
DE Short=IPC synthase {ECO:0000303|PubMed:20457606};
DE AltName: Full=Sphingolipid synthase {ECO:0000303|PubMed:20457606};
GN Name=SLS1 {ECO:0000303|PubMed:18699867, ECO:0000303|PubMed:20457606};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000269|PubMed:18699867};
RX PubMed=18699867; DOI=10.1111/j.1365-2958.2008.06393.x;
RA Sutterwala S.S., Hsu F.F., Sevova E.S., Schwartz K.J., Zhang K., Key P.,
RA Turk J., Beverley S.M., Bangs J.D.;
RT "Developmentally regulated sphingolipid synthesis in African
RT trypanosomes.";
RL Mol. Microbiol. 70:281-296(2008).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF SER-270.
RC STRAIN=427 {ECO:0000269|PubMed:20457606};
RX PubMed=20457606; DOI=10.1074/jbc.m110.127662;
RA Sevova E.S., Goren M.A., Schwartz K.J., Hsu F.F., Turk J., Fox B.G.,
RA Bangs J.D.;
RT "Cell-free synthesis and functional characterization of sphingolipid
RT synthases from parasitic trypanosomatid protozoa.";
RL J. Biol. Chem. 285:20580-20587(2010).
CC -!- FUNCTION: Bidirectional lipid inositolphosphotransferase capable of
CC converting phosphatidylinositol (PI) and ceramide to inositol-
CC phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa.
CC Direction is dependent on the relative concentrations of DAG and
CC ceramide as phosphoinositol acceptors. Essential for viability of the
CC pathogenic bloodstream stage of this human protozoan parasite and,
CC consequently, can be considered as potential drug target.
CC {ECO:0000269|PubMed:18699867, ECO:0000269|PubMed:20457606}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Found only in procyclic parasites.
CC {ECO:0000269|PubMed:18699867}.
CC -!- DISRUPTION PHENOTYPE: Elevated ceramide levels and growth arrest; cells
CC were arrested in division but replication of DNA and organelles
CC continued giving rise to cells containing multiple nuclei, kinetoplasts
CC and flagella. {ECO:0000269|PubMed:18699867}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000255}.
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DR AlphaFoldDB; B3A0L9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290; PTHR21290; 1.
DR Pfam; PF14360; PAP2_C; 1.
PE 1: Evidence at protein level;
KW Kinase; Lipid metabolism; Membrane; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase"
FT /id="PRO_0000413852"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..275
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 228
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT MUTAGEN 270
FT /note="S->F: Dramatically reduced IPC synthesis."
FT /evidence="ECO:0000269|PubMed:20457606"
SQ SEQUENCE 355 AA; 39854 MW; 0497FB951872845F CRC64;
MISYPFFSLS PPGLVPPPMA VPPVEMYSGS FWNRMRKPLP LRTQVIRFTV VFVIVSFILA
VALQITHERM PDPKVTKPLP DLGFELLTKI SFLSVVTDVL IAFLSLLSFF TLWKLYLLHR
HCVGSGEPEL PCNIPGVSRF FLSVWLCKEN CRIELRNIHT IAWIRFITSY ALLLLFRSLV
IVMTSMPTPV DKCQDPPKIE NPVKNVILTV LTAGGGSIHC GDLMVSGHTV ILTLHLMFHW
IYGAMVHWSF RPVVTVVAIF SYYCIVASRS HYTDDVLVAI YLTIATFIAV GHNADGAPWQ
LQLFIRWLPC CGANSREVTE DSQPVMVAFK SEAVDELRER DDSAGLSGEV STNEV
