SLS2_TRYB2
ID SLS2_TRYB2 Reviewed; 323 AA.
AC Q38E54;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase {ECO:0000250|UniProtKB:B3A0M0};
DE EC=2.7.8.- {ECO:0000250|UniProtKB:B3A0M0};
DE AltName: Full=Ethanolamine-phosphorylceramide synthase {ECO:0000250|UniProtKB:B3A0M0};
DE Short=EPC synthase {ECO:0000250|UniProtKB:B3A0M0};
DE AltName: Full=Sphingolipid synthase {ECO:0000250|UniProtKB:B3A0M0};
GN Name=SLS2 {ECO:0000250|UniProtKB:B3A0M0}; ORFNames=Tb09.211.1020;
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:EAN76916.1}
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 ethanolaminephosphotransferase capable of
CC converting phosphatidylethanolamine (PE) and ceramide to ethanolamine-
CC phosphorylceramide (EPC) and diacylglycerol (DAG) and vice versa.
CC Direction is dependent on the relative concentrations of DAG and
CC ceramide as phosphoethanolamine acceptors. Does not function strictly
CC as a 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAN76916.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM000207; EAN76916.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_827246.1; XM_822153.1.
DR AlphaFoldDB; Q38E54; -.
DR STRING; 185431.Q38E54; -.
DR PaxDb; Q38E54; -.
DR GeneID; 3660635; -.
DR KEGG; tbr:Tb09.211.1020; -.
DR InParanoid; Q38E54; -.
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; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:GeneDB.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046335; P:ethanolamine biosynthetic process; IDA:GeneDB.
DR GO; GO:0016310; P:phosphorylation; 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 3: Inferred from homology;
KW Kinase; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Phosphatidylethanolamine:ceramide
FT ethanolaminephosphotransferase"
FT /id="PRO_0000413853"
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..73
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..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..323
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 323 AA; 36519 MW; FB65BC47E63E5CA3 CRC64;
MAVPPVEMYS GSFWNRMRKP LPLRTQVIRF TVVFVIVSFI LAVALQITHE RMPDPKVTKP
LPDLGFEVLH KYPFLFSVAD CCIGFLNILS VFTAFKLYLL HRHCVGSGEP ELPCNIPGVS
RFFLSVWLCK ENCRIELRNV HTIAWIRFIT SYALLLLSRS VIMVVTSLPN PDDLCQDPPK
IENRVKDVIL TVLTAGAGSI HCGDLMYSGH TVILTLHLMF HWIYGAMVHW SFRPVVTVVA
IFGYYCIVAS RFHYTDDVLV AIYLTIATFI AVGHNADGAP WQLQLFIRWL PCCGANSREV
TEDGVPVAIV IKNEEMMNFE GKS
