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SLS1_TRYBB
ID   SLS1_TRYBB              Reviewed;         355 AA.
AC   B3A0L9;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Phosphatidylinositol:ceramide inositolphosphotransferase {ECO:0000303|PubMed:20457606};
DE            Short=TbSLS1 {ECO:0000303|PubMed:18699867, 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   Name=SLS1 {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], FUNCTION, DEVELOPMENTAL STAGE, AND
RP   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).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF SER-270.
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).
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:18699867, ECO:0000269|PubMed:20457606}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Found only in procyclic parasites.
CC       {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; B3A0L9; -.
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   1: Evidence at protein level;
KW   Kinase; Lipid metabolism; Membrane; Sphingolipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..355
FT                   /note="Phosphatidylinositol:ceramide
FT                   inositolphosphotransferase"
FT                   /id="PRO_0000413852"
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..89
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..355
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"
FT   MUTAGEN         270
FT                   /note="S->F: Dramatically reduced IPC synthesis."
FT                   /evidence="ECO:0000269|PubMed:20457606"
SQ   SEQUENCE   355 AA;  39854 MW;  0497FB951872845F CRC64;
     MISYPFFSLS PPGLVPPPMA VPPVEMYSGS FWNRMRKPLP LRTQVIRFTV VFVIVSFILA
     VALQITHERM PDPKVTKPLP DLGFELLTKI SFLSVVTDVL IAFLSLLSFF TLWKLYLLHR
     HCVGSGEPEL PCNIPGVSRF FLSVWLCKEN CRIELRNIHT IAWIRFITSY ALLLLFRSLV
     IVMTSMPTPV DKCQDPPKIE NPVKNVILTV LTAGGGSIHC GDLMVSGHTV ILTLHLMFHW
     IYGAMVHWSF RPVVTVVAIF SYYCIVASRS HYTDDVLVAI YLTIATFIAV GHNADGAPWQ
     LQLFIRWLPC CGANSREVTE DSQPVMVAFK SEAVDELRER DDSAGLSGEV STNEV
 
 
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