Hmdb loader
Identification
HMDB Protein ID HMDBP12112
Secondary Accession Numbers None
Name Phosphatidylethanolamine:ceramide ethanolaminephosphotransferase
Synonyms
  1. Ethanolamine-phosphorylceramide synthase
  2. Sphingolipid synthase
  3. EPC synthase
Gene Name SLS2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Bidirectional lipid ethanolaminephosphotransferase capable of converting phosphatidylethanolamine (PE) and ceramide to ethanolamine-phosphorylceramide (EPC) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphoethanolamine acceptors. Does not function strictly as a SM synthase. Essential for viability of the pathogenic bloodstream stage of this human protozoan parasite and, consequently, can be considered as potential drug target (By similarity).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
ethanolamine biosynthetic process
ceramide biosynthetic process
Cellular Component
integral to endoplasmic reticulum membrane
integral to Golgi membrane
membrane
integral to plasma membrane
Molecular Function
ceramide cholinephosphotransferase activity
sphingomyelin synthase activity
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 272
Molecular Weight 36518.8
Theoretical pI 6.875
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 27-47;74-94;148-168;212-232;234-254;258-278;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q38E54
UniProtKB/Swiss-Prot Entry Name SLS2_TRYB2
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. Berriman M, Ghedin E, Hertz-Fowler C, Blandin G, Renauld H, Bartholomeu DC, Lennard NJ, Caler E, Hamlin NE, Haas B, Bohme U, Hannick L, Aslett MA, Shallom J, Marcello L, Hou L, Wickstead B, Alsmark UC, Arrowsmith C, Atkin RJ, Barron AJ, Bringaud F, Brooks K, Carrington M, Cherevach I, Chillingworth TJ, Churcher C, Clark LN, Corton CH, Cronin A, Davies RM, Doggett J, Djikeng A, Feldblyum T, Field MC, Fraser A, Goodhead I, Hance Z, Harper D, Harris BR, Hauser H, Hostetler J, Ivens A, Jagels K, Johnson D, Johnson J, Jones K, Kerhornou AX, Koo H, Larke N, Landfear S, Larkin C, Leech V, Line A, Lord A, Macleod A, Mooney PJ, Moule S, Martin DM, Morgan GW, Mungall K, Norbertczak H, Ormond D, Pai G, Peacock CS, Peterson J, Quail MA, Rabbinowitsch E, Rajandream MA, Reitter C, Salzberg SL, Sanders M, Schobel S, Sharp S, Simmonds M, Simpson AJ, Tallon L, Turner CM, Tait A, Tivey AR, Van Aken S, Walker D, Wanless D, Wang S, White B, White O, Whitehead S, Woodward J, Wortman J, Adams MD, Embley TM, Gull K, Ullu E, Barry JD, Fairlamb AH, Opperdoes F, Barrell BG, Donelson JE, Hall N, Fraser CM, Melville SE, El-Sayed NM: The genome of the African trypanosome Trypanosoma brucei. Science. 2005 Jul 15;309(5733):416-22. doi: 10.1126/science.1112642. [PubMed:16020726 ]