SLS2_TRYBB
ID SLS2_TRYBB Reviewed; 323 AA.
AC B3A0M0;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase {ECO:0000303|PubMed:20457606};
DE Short=TbSLS2 {ECO:0000303|PubMed:18699867, ECO:0000303|PubMed:20457606};
DE EC=2.7.8.- {ECO:0000269|PubMed:20457606};
DE AltName: Full=Ethanolamine-phosphorylceramide synthase {ECO:0000303|PubMed:20457606};
DE Short=EPC synthase {ECO:0000303|PubMed:20457606};
DE AltName: Full=Sphingolipid synthase {ECO:0000303|PubMed:20457606};
GN Name=SLS2 {ECO:0000303|PubMed:18699867, ECO:0000303|PubMed:20457606};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=427 {ECO:0000269|PubMed:20457606};
RX PubMed=20457606; DOI=10.1074/jbc.m110.127662;
RA Sevova E.S., Goren M.A., Schwartz K.J., Hsu F.F., Turk J., Fox B.G.,
RA Bangs J.D.;
RT "Cell-free synthesis and functional characterization of sphingolipid
RT synthases from parasitic trypanosomatid protozoa.";
RL J. Biol. Chem. 285:20580-20587(2010).
RN [2] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=427 {ECO:0000269|PubMed:18699867};
RX PubMed=18699867; DOI=10.1111/j.1365-2958.2008.06393.x;
RA Sutterwala S.S., Hsu F.F., Sevova E.S., Schwartz K.J., Zhang K., Key P.,
RA Turk J., Beverley S.M., Bangs J.D.;
RT "Developmentally regulated sphingolipid synthesis in African
RT trypanosomes.";
RL Mol. Microbiol. 70:281-296(2008).
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. {ECO:0000269|PubMed:18699867,
CC ECO:0000269|PubMed:20457606}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in both bloodstream and procyclic stage
CC parasites. {ECO:0000269|PubMed:18699867}.
CC -!- DISRUPTION PHENOTYPE: Elevated ceramide levels and growth arrest; cells
CC were arrested in division but replication of DNA and organelles
CC continued giving rise to cells containing multiple nuclei, kinetoplasts
CC and flagella. {ECO:0000269|PubMed:18699867}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000255}.
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DR AlphaFoldDB; B3A0M0; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; 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 2: Evidence at transcript level;
KW Kinase; Lipid metabolism; Membrane; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..323
FT /note="Phosphatidylethanolamine:ceramide
FT ethanolaminephosphotransferase"
FT /id="PRO_0000413854"
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..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..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"
SQ SEQUENCE 323 AA; 36515 MW; B848D4DF3A1AC82A CRC64;
MAVPPVEMYS GSFWNRMRKP LPLRTQVIRF TVVFVIVSFI LVVALQITHE RMPDPKVTKP
LPDLGFELLT KVPGMYVLAD CCIGFLNILS VFTAFKLYLL HRHCVGSGEP ELPCNIPGVS
RFFLSVWLCK ENCRIELRNI HTIAWIRFIT SYALLLLSRS IIMVVTSLPN PDDLCQNPPK
IENRVKDILL TVLTAGAGSI HCGDLMYSGH TVILTLHLMF HWIYGAMVHW SFRPVVTVVA
IFGYYCIVAS RFHYTDDVLV AIYLTIATFI AVGHNADGAP WQLQLFIRWW PCCGANSREV
AEDGVPVAIV IKNEEMMNFE GKS
