| Identification |
|---|
| HMDB Protein ID
| HMDBP13910 |
| Secondary Accession Numbers
| None |
| Name
| Dermonecrotic toxin LgSicTox-alphaIC1 |
| Synonyms
|
- Phospholipase D
- Phospholipase D LgRec1
- Sphingomyelin phosphodiesterase D
- PLD
- SMD
- SMase D
- Sphingomyelinase D
|
| 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:23770445). 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). Induces platelet aggregation in platelet rich plasma, but not in washed platelet, indicating that this activity is dependent on plasma components (PubMed:23770445). Also induces hemolysis (PubMed:23770445). In vivo, the recombinant protein evokes an intense inflammatory reaction and dermonecrosis, similar to those induced by L.gaucho total venom (PubMed:23770445). Is a good immunogen, capable of inducing immunoprotection in test animals (PubMed:23770445).anionic antimicrobial peptides that shows antimicrobial activity against Gram-negative bacteria (MIC=1.15-4.6 uM) (tested on E.coli, P.aeruginosa, and E.cloacae), but not on Gram-negative bacteria (M.luteus, S.aureus, and B.subtilis), neither on fungi and yeasts (A.niger, C.albicans and C.krusei). Does not show hemolytic effects against human erythrocytes, and has no cytotoxic effects against human cervical carcinoma cells (HeLa). |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| defense response to bacterium |
| lipid catabolic process |
| hemolysis in other organism |
| Cellular Component |
| extracellular region |
| Molecular Function |
| phosphoric diester hydrolase activity |
| metal ion binding |
| toxin activity |
| lyase 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
| 31447.095 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
Not Available |
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| K9USW8 |
| UniProtKB/Swiss-Prot Entry Name
| A1O_LOXGA |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Magalhaes GS, Caporrino MC, Della-Casa MS, Kimura LF, Prezotto-Neto JP, Fukuda DA, Portes-Junior JA, Neves-Ferreira AG, Santoro ML, Barbaro KC: Cloning, expression and characterization of a phospholipase D from Loxosceles gaucho venom gland. Biochimie. 2013 Sep;95(9):1773-83. doi: 10.1016/j.biochi.2013.06.002. Epub 2013 Jun 14. [PubMed:23770445 ]
- Segura-Ramirez PJ, Silva Junior PI: Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents. Toxins (Basel). 2018 Dec 6;10(12). pii: toxins10120522. doi: 10.3390/toxins10120522. [PubMed:30563217 ]
- Lajoie DM, Roberts SA, Zobel-Thropp PA, Delahaye JL, Bandarian V, Binford GJ, Cordes MH: Variable Substrate Preference among Phospholipase D Toxins from Sicariid Spiders. J Biol Chem. 2015 Apr 24;290(17):10994-1007. doi: 10.1074/jbc.M115.636951. Epub 2015 Mar 9. [PubMed:25752604 ]
|
