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Showing Protein Phosphatidylinositol:ceramide inositolphosphotransferase (HMDBP12087)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP12087
Secondary Accession Numbers None
Name Phosphatidylinositol:ceramide inositolphosphotransferase
Synonyms
  1. TcSLS1.1
  2. Inositol-phosphorylceramide synthase
  3. Sphingolipid synthase
  4. IPC synthase
Gene Name (REFSEQ) PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Bidirectional lipid inositolphosphotransferase capable of converting phosphatidylinositol (PI) and ceramide to inositol-phosphorylceramide (IPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoinositol acceptors. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target.
Pathways
  • sphingolipid metabolism
Reactions Not Available
GO Classification
Biological Process
sphingolipid metabolic process
Cellular Component
integral to membrane
Molecular Function
kinase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 335
Molecular Weight 37850.18
Theoretical pI 6.93
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 22-42;73-93;99-119;140-160;180-200;204-224;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q4E4I4
UniProtKB/Swiss-Prot Entry Name SLS11_TRYCC
PDB IDs Not Available
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Sevova ES, Goren MA, Schwartz KJ, Hsu FF, Turk J, Fox BG, Bangs JD: Cell-free synthesis and functional characterization of sphingolipid synthases from parasitic trypanosomatid protozoa. J Biol Chem. 2010 Jul 2;285(27):20580-7. doi: 10.1074/jbc.M110.127662. Epub 2010 May 10. [PubMed:20457606 ]
  2. El-Sayed NM, Myler PJ, Bartholomeu DC, Nilsson D, Aggarwal G, Tran AN, Ghedin E, Worthey EA, Delcher AL, Blandin G, Westenberger SJ, Caler E, Cerqueira GC, Branche C, Haas B, Anupama A, Arner E, Aslund L, Attipoe P, Bontempi E, Bringaud F, Burton P, Cadag E, Campbell DA, Carrington M, Crabtree J, Darban H, da Silveira JF, de Jong P, Edwards K, Englund PT, Fazelina G, Feldblyum T, Ferella M, Frasch AC, Gull K, Horn D, Hou L, Huang Y, Kindlund E, Klingbeil M, Kluge S, Koo H, Lacerda D, Levin MJ, Lorenzi H, Louie T, Machado CR, McCulloch R, McKenna A, Mizuno Y, Mottram JC, Nelson S, Ochaya S, Osoegawa K, Pai G, Parsons M, Pentony M, Pettersson U, Pop M, Ramirez JL, Rinta J, Robertson L, Salzberg SL, Sanchez DO, Seyler A, Sharma R, Shetty J, Simpson AJ, Sisk E, Tammi MT, Tarleton R, Teixeira S, Van Aken S, Vogt C, Ward PN, Wickstead B, Wortman J, White O, Fraser CM, Stuart KD, Andersson B: The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease. Science. 2005 Jul 15;309(5733):409-15. doi: 10.1126/science.1112631. [PubMed:16020725 ]