| Tag |
Content |
LipidDB ID |
LipidDB-185431-00414 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
7.14 |
Molecular Weight |
39892.98 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Phosphatidylinositol:ceramide inositolphosphotransferase |
Protein Synonyms/Alias |
2.7.8.-; Inositol-phosphorylceramide synthase; IPC synthase; Sphingolipid synthase; |
Gene Name |
SLS1 |
Gene Synonyms/Alias |
Tb09.211.1030; |
Created Date |
16-NOV-2011 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
310 | Canonical | LFIRWLPCCGANSRE | [1] | S-Palmitoylation | 311 | Canonical | FIRWLPCCGANSREV | [1] | S-Palmitoylation |
|
Organism |
Trypanosoma brucei brucei (strain 927/4 GUTat10.1) |
NCBI Taxa ID |
185431 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
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. 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). |
Sequence Annotation |
Topological domain: 1 44 Cytoplasmic.
Transmembrane: 45 65 Helical.
Topological domain: 66 89 Extracellular.
Transmembrane: 90 110 Helical.
Topological domain: 111 165 Cytoplasmic.
Transmembrane: 166 186 Helical.
Topological domain: 187 205 Extracellular.
Transmembrane: 206 226 Helical.
Topological domain: 227 251 Cytoplasmic.
Transmembrane: 252 272 Helical.
Topological domain: 273 275 Extracellular.
Transmembrane: 276 296 Helical.
Topological domain: 297 355 Cytoplasmic.
Active site: 228 228
Active site: 271 271
Active site: 275 275
|
Protein Length |
355 AA. |
Protein Sequence
(Canonical) |
MISYPFFSLS PPGLVPPPMA VPPVEMYSGS FWNRMRKPLP LRTQVIRFTV VFVIVSFILA 60
VALQITHERM PDPKVTKPLP DLGFELLTKI SFLSVVTDVL IAFLSSLSFF TLWKLYLLHR 120
HCVGSGEPEL PCNIPGVSRF FLSVWLCKEN CRIELRNVHT IAWIRFITSY ALLLLFRSLV 180
IVMTSMPTPV DKCQNPPKIE NPVKNVILTV LTAGGGSIHC GDLMYSGHTV ILTLHLMFHW 240
IYGAMVHWSF RPVVTVVAIF GYYCIVASRS HYTDDVLVAI YLTIATFIAV GHNADGAPWQ 300
LQLFIRWLPC CGANSREVTE DSQPVMVAFK SEAVDELRER DDSAGLSCEV STNEV 355
|
FASTA
(Canonical) |
>LipidDB-185431-00414|Q38E53
MISYPFFSLSPPGLVPPPMAVPPVEMYSGSFWNRMRKPLPLRTQVIRFTVVFVIVSFILA
VALQITHERMPDPKVTKPLPDLGFELLTKISFLSVVTDVLIAFLSSLSFFTLWKLYLLHR
HCVGSGEPELPCNIPGVSRFFLSVWLCKENCRIELRNVHTIAWIRFITSYALLLLFRSLV
IVMTSMPTPVDKCQNPPKIENPVKNVILTVLTAGGGSIHCGDLMYSGHTVILTLHLMFHW
IYGAMVHWSFRPVVTVVAIFGYYCIVASRSHYTDDVLVAIYLTIATFIAVGHNADGAPWQ
LQLFIRWLPCCGANSREVTEDSQPVMVAFKSEAVDELRERDDSAGLSCEVSTNEV
|
Gene Ontology |
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0016301; F:kinase activity; IEA:UniProtKB-KW GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW |
Interpro |
InterPro; IPR025749; Sphingomyelin_synth-like_dom |
Pfam |
|
SMART |
|
PROSITE |
|
PRINTS |
|