SLS4_TRYB2
ID SLS4_TRYB2 Reviewed; 365 AA.
AC Q38E56;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 4 {ECO:0000250|UniProtKB:B3A0M2};
DE EC=2.7.8.27 {ECO:0000250|UniProtKB:B3A0M2};
DE AltName: Full=Ethanolamine-phosphorylceramide synthase {ECO:0000250|UniProtKB:B3A0M2};
DE Short=EPC synthase {ECO:0000250|UniProtKB:B3A0M2};
DE AltName: Full=Sphingolipid synthase {ECO:0000250|UniProtKB:B3A0M2};
DE AltName: Full=Sphingomyelin synthase {ECO:0000250|UniProtKB:B3A0M2};
DE Short=SM synthase {ECO:0000250|UniProtKB:B3A0M2};
GN Name=SLS4 {ECO:0000250|UniProtKB:B3A0M2}; ORFNames=Tb09.211.1000;
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:EAN76914.1}
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 cholinephosphotransferase capable of
CC converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM)
CC and diacylglycerol (DAG) and vice versa. Direction is dependent on the
CC relative concentrations of DAG and ceramide as phosphocholine
CC acceptors. Directly and specifically recognizes the choline head group
CC on the substrate. Also requires two fatty chains on the choline-P donor
CC molecule in order to be recognized efficiently as a substrate. Does not
CC function strictly as a SM synthase. Essential for viability of the
CC pathogenic bloodstream stage of this human protozoan parasite and,
CC consequently, can be considered as potential drug target (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + an N-acylsphing-4-
CC enine = a 1,2-diacyl-sn-glycerol + a sphingomyelin;
CC Xref=Rhea:RHEA:18765, ChEBI:CHEBI:17636, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:57643; EC=2.7.8.27;
CC Evidence={ECO:0000250|UniProtKB:B3A0M2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:B3A0M2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:B3A0M2}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000255}.
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DR EMBL; CM000207; EAN76914.1; -; Genomic_DNA.
DR RefSeq; XP_827244.1; XM_822151.1.
DR AlphaFoldDB; Q38E56; -.
DR STRING; 5691.EAN76914; -.
DR PaxDb; Q38E56; -.
DR GeneID; 3660633; -.
DR KEGG; tbr:Tb09.211.1000; -.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; Q38E56; -.
DR OMA; LIVWIRY; -.
DR Proteomes; UP000008524; Chromosome 9.
DR GO; GO:0005794; C:Golgi apparatus; EXP:GeneDB.
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:0004307; F:ethanolaminephosphotransferase activity; IDA: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; IDA:GeneDB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; EXP: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 Golgi apparatus; Kinase; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 4"
FT /id="PRO_0000413857"
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..92
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..229
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 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="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..365
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 365 AA; 40857 MW; 483DC4A8785804AC CRC64;
MISYPFFSLS PPGLVPPPMA VPPVEMYSGS FWNRMRKPLP LRTQVIRFTV VFVIVSFILA
VALQITHERM PDPKVTKPLP DLGFELLTKV PGMYVLADCC IGFLNILSVF TAFKLYLLHR
HCVGSGEPEL PCNIPGVSRF FLSVWLCKEN CRIELRNVHT IAWIRFITSY ALLLLFRSVV
IVMTSLPAPD DLCQDPPKIE NPVKNVILTV LTAGGGSIHC GDLMYSGHTV ILTLHLMFHW
IYGAMVHWSF RPVVTVVAIF GYYCIVASRF HYTDDVLVAI YLTIATFIAV GHNADGAPWQ
LQLFIRWLPC CGANSREMTE DSQPVMVAFK SEELDEMNGV LEGRQKKHGG VGDGEALMFK
CGAYV
