| Identification |
|---|
| HMDB Protein ID
| HMDBP13911 |
| Secondary Accession Numbers
| None |
| Name
| Dermonecrotic toxin LiSicTox-alphaIVA1 |
| Synonyms
|
- Dermonecrotic toxin 7
- LiRecDT7
- Phospholipase D
- Sphingomyelin phosphodiesterase D 7
- DT7
- PLD
- SMD 7
- SMase D 7
- Sphingomyelinase D 7
|
| Gene Name
| Not Available |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) with high activity (PubMed:23733617). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Has hemolytic activity in human erythrocytes in a dose-dependent manner (PubMed:23733617). In vivo, this toxin induces dermonecrosis, edema, hemorrhage, massive inflammatory response, as well as vascular permeability (PubMed:23733617). In addition, thrombus formation has also been detected in dermal blood vessels (PubMed:23733617). It also induces platelet aggregation (By similarity). It is noteworthy that a Glu-248 replaces the Asp present in paralogs, without decrease in catalytic and hemolytic activities (PubMed:23733617). |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| lipid catabolic process |
| hemolysis in other organism |
| Cellular Component |
| extracellular region |
| Molecular Function |
| metal ion binding |
| lyase activity |
| toxin activity |
| phosphoric diester hydrolase 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
| Not Available |
| Molecular Weight
| 34103.89 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
Not Available |
| Signals
|
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P0DM60 |
| UniProtKB/Swiss-Prot Entry Name
| A4A1_LOXIN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Vuitika L, Gremski LH, Belisario-Ferrari MR, Chaves-Moreira D, Ferrer VP, Senff-Ribeiro A, Chaim OM, Veiga SS: Brown spider phospholipase-D containing a conservative mutation (D233E) in the catalytic site: identification and functional characterization. J Cell Biochem. 2013 Nov;114(11):2479-92. doi: 10.1002/jcb.24594. [PubMed:23733617 ]
|
