SLS1_TRYB2
ID SLS1_TRYB2 Reviewed; 355 AA.
AC Q38E53;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase {ECO:0000250|UniProtKB:B3A0L9};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:B3A0L9};
DE AltName: Full=Inositol-phosphorylceramide synthase {ECO:0000250|UniProtKB:B3A0L9};
DE Short=IPC synthase {ECO:0000250|UniProtKB:B3A0L9};
DE AltName: Full=Sphingolipid synthase {ECO:0000250|UniProtKB:B3A0L9};
GN Name=SLS1 {ECO:0000250|UniProtKB:B3A0L9}; ORFNames=Tb09.211.1030;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1] {ECO:0000312|EMBL:EAN76917.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
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. Does not function strictly as a
CC SM synthase. Essential for viability of the pathogenic bloodstream
CC stage of this human protozoan parasite and, consequently, can be
CC considered as potential drug target (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000255}.
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DR EMBL; CM000207; EAN76917.1; -; Genomic_DNA.
DR RefSeq; XP_827247.1; XM_822154.1.
DR AlphaFoldDB; Q38E53; -.
DR STRING; 5691.EAN76917; -.
DR SwissPalm; Q38E53; -.
DR PaxDb; Q38E53; -.
DR GeneID; 3660636; -.
DR KEGG; tbr:Tb09.211.1030; -.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; Q38E53; -.
DR Proteomes; UP000008524; Chromosome 9.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISA:GeneDB.
DR GO; GO:0047493; F:ceramide cholinephosphotransferase activity; ISA:GeneDB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISA:GeneDB.
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 3: Inferred from homology;
KW Kinase; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase"
FT /id="PRO_0000413851"
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..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..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"
SQ SEQUENCE 355 AA; 39893 MW; 1D68D735E8662E99 CRC64;
MISYPFFSLS PPGLVPPPMA VPPVEMYSGS FWNRMRKPLP LRTQVIRFTV VFVIVSFILA
VALQITHERM PDPKVTKPLP DLGFELLTKI SFLSVVTDVL IAFLSSLSFF TLWKLYLLHR
HCVGSGEPEL PCNIPGVSRF FLSVWLCKEN CRIELRNVHT IAWIRFITSY ALLLLFRSLV
IVMTSMPTPV DKCQNPPKIE NPVKNVILTV LTAGGGSIHC GDLMYSGHTV ILTLHLMFHW
IYGAMVHWSF RPVVTVVAIF GYYCIVASRS HYTDDVLVAI YLTIATFIAV GHNADGAPWQ
LQLFIRWLPC CGANSREVTE DSQPVMVAFK SEAVDELRER DDSAGLSCEV STNEV
