SLS3_TRYB2
ID SLS3_TRYB2 Reviewed; 329 AA.
AC Q38E55;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Phosphatidylcholine:ceramide cholinephosphotransferase 3 {ECO:0000250|UniProtKB:B3A0M1};
DE EC=2.7.8.27 {ECO:0000250|UniProtKB:B3A0M1};
DE AltName: Full=Ethanolamine-phosphorylceramide synthase {ECO:0000250|UniProtKB:B3A0M1};
DE Short=EPC synthase {ECO:0000250|UniProtKB:B3A0M1};
DE AltName: Full=Sphingolipid synthase {ECO:0000250|UniProtKB:B3A0M1};
DE AltName: Full=Sphingomyelin synthase {ECO:0000250|UniProtKB:B3A0M1};
DE Short=SM synthase {ECO:0000250|UniProtKB:B3A0M1};
GN Name=SLS3 {ECO:0000250|UniProtKB:B3A0M1}; ORFNames=Tb09.211.1010;
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:EAN76915.1}
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:B3A0M1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAN76915.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM000207; EAN76915.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_827245.1; XM_822152.1.
DR AlphaFoldDB; Q38E55; -.
DR STRING; 5691.EAN76915; -.
DR PaxDb; Q38E55; -.
DR GeneID; 3660634; -.
DR KEGG; tbr:Tb09.211.1010; -.
DR VEuPathDB; TriTrypDB:Tb927.9.9390; -.
DR eggNOG; KOG3058; Eukaryota.
DR InParanoid; Q38E55; -.
DR Proteomes; UP000008524; Chromosome 9.
DR GO; GO:0020016; C:ciliary pocket; IDA:GeneDB.
DR GO; GO:0005768; C:endosome; IDA: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; IDA: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..329
FT /note="Phosphatidylcholine:ceramide
FT cholinephosphotransferase 3"
FT /id="PRO_0000413855"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 210
FT /evidence="ECO:0000250"
FT ACT_SITE 253
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 37180 MW; 7D86FED1E393C76C CRC64;
MAVPPVEMYS GSFWNRMRKP LPLRTQVIRF TVVFVIVSFI LAVALQITHE RMPDPKVTKP
LPDLGFELLT KVPGMYVLAD CCIGFLNILS VFTAFKLYLL HRHCVGSGEP ELPCNIPGVS
RFFLSVWLCK ENCRIELRNV HTIAWIRFIT SYALLLLFRS VVIVMTSFPA PDDLCQNPPK
IENPVKNVIL TVLTAGGGSI HCGDLMYSGH TVILTLHLMF HWIYGAMVHW SFRPVVTVVA
IFSYYCIVAS RFHYTDDVLV AIYLTIATFI AVGHNADGAP WQLQLFIRWW PCCGANSREM
TEDSQPVMVA FKSEAAGQSS RKVVDERNH
