SLS11_TRYCC
ID SLS11_TRYCC Reviewed; 335 AA.
AC Q4E4I4;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase {ECO:0000303|PubMed:20457606};
DE Short=TcSLS1.1 {ECO:0000303|PubMed:20457606};
DE EC=2.7.8.- {ECO:0000269|PubMed:20457606};
DE AltName: Full=Inositol-phosphorylceramide synthase {ECO:0000303|PubMed:20457606};
DE Short=IPC synthase {ECO:0000303|PubMed:20457606};
DE AltName: Full=Sphingolipid synthase {ECO:0000303|PubMed:20457606};
GN ORFNames=Tc00.1047053506885.124;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CL Brener {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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(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. Essential for viability of the
CC pathogenic bloodstream stage of this human protozoan parasite and,
CC consequently, can be considered as potential drug target.
CC {ECO:0000269|PubMed:20457606}.
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; AAHK01000012; EAN99655.1; -; Genomic_DNA.
DR RefSeq; XP_821506.1; XM_816413.1.
DR AlphaFoldDB; Q4E4I4; -.
DR STRING; 5693.XP_821506.1; -.
DR PaxDb; Q4E4I4; -.
DR EnsemblProtists; EAN99655; EAN99655; Tc00.1047053506885.124.
DR GeneID; 3554461; -.
DR KEGG; tcr:506885.124; -.
DR eggNOG; KOG3058; Eukaryota.
DR OMA; YCILASR; -.
DR OrthoDB; 599210at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Kinase; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="Phosphatidylinositol:ceramide
FT inositolphosphotransferase"
FT /id="PRO_0000413859"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..72
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..98
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 202
FT /evidence="ECO:0000250"
FT ACT_SITE 245
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /evidence="ECO:0000250"
FT CONFLICT 10
FT /note="L -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 69..70
FT /note="HL -> YV (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="F -> V (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> I (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="M -> V (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="F -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="S -> P (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="D -> E (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="N -> H (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> R (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37851 MW; 9EA710EF52528B29 CRC64;
MVLMGPHSAL RLLPLKTQAI RFVLLLLLSV LILAVALLVT NARMPDPKVV RPLPDIGFEV
FPKVGWLEHL TDVCIFILNF LSLLVVFKLY LLHRQNEGLD ELQPFSCCPL IGKIIFGVWD
SGRQSGIEKR DAHLIAWIRY FTTYFIVLLF RAIVVVMTSY PATDNHCQNP MKITNPVKNV
IMTLVTFGSG SIHCGDLMFS GHTVSITLSL LVQWIYGSML HWVFRPASVL LVLLSFYSII
ASRSHYTDDI LVSFYITVTT FLVLRHSPDG APWQLQLLIG WWPCCVSNEE TEDSDRNPTF
VAVEVFLPHG DYQCAERISE EKTTVGPACG NFGHW
