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Database: UniProt
Entry: SLS1_TRYB2
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Original site: 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   27-NOV-2024, entry version 77.
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; 185431.Q38E53; -.
DR   SwissPalm; Q38E53; -.
DR   PaxDb; 5691-EAN76917; -.
DR   GeneID; 3660636; -.
DR   KEGG; tbr:Tb09.211.1030; -.
DR   eggNOG; KOG3058; Eukaryota.
DR   InParanoid; Q38E53; -.
DR   OrthoDB; 1343173at2759; -.
DR   Proteomes; UP000008524; Chromosome 9.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISA:GeneDB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:SF65; PHOSPHATIDYLINOSITOL:CERAMIDE INOSITOLPHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 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
//
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