A0A0D4WV12 · BIB11_SICTE
- ProteinDermonecrotic toxin StSicTox-betaIB1i
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids279 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:25752604).
This toxin acts on lysophosphatidylethanolamine (LPE) and ceramide phosphoethanolamine (CPE) with high activity (PubMed:25752604).
This toxin acts on sphingomyelin (SM) with very low activity and is not active on lysophosphatidylserine (LPS), lysophosphatidylcholine (LPC) and lysophosphatidylglycerol (LPG) (PubMed:25752604).
It acts by transphosphatidylation, releasing exclusively cyclic phosphate as second products (PubMed:25752604).
It is not surprising that spider toxins have affinity for ethanolamine-containing sphingolipids since they are common in insect prey (PubMed:25752604).
Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
This toxin acts on lysophosphatidylethanolamine (LPE) and ceramide phosphoethanolamine (CPE) with high activity (PubMed:25752604).
This toxin acts on sphingomyelin (SM) with very low activity and is not active on lysophosphatidylserine (LPS), lysophosphatidylcholine (LPC) and lysophosphatidylglycerol (LPG) (PubMed:25752604).
It acts by transphosphatidylation, releasing exclusively cyclic phosphate as second products (PubMed:25752604).
It is not surprising that spider toxins have affinity for ethanolamine-containing sphingolipids since they are common in insect prey (PubMed:25752604).
Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity).
Catalytic activity
- an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + choline
- N-hexanoyl-sphing-4-enine-1-phosphocholine = choline + N-(hexanoyl)-sphing-4-enine-1,3-cyclic phosphate
- an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-sphingosyl-1,3-cyclic phosphate + ethanolamine
- N-dodecanoyl-heptadecasphing-4-enine-1-phosphoethanolamine = ethanolamine + N-dodecanoyl-heptadecasphing-4-enine-1,3-cyclic phosphate
- a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-glycero-2,3-cyclic phosphate + ethanolamine
- 1-tetradecanoyl-sn-glycero-3-phosphoethanolamine = 1-tetradecanoyl-sn-glycero-2,3-cyclic phosphate + ethanolamine
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 12 | |||||
Sequence: H | ||||||
Binding site | 32 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 34 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 48 | Nucleophile | ||||
Sequence: H | ||||||
Binding site | 92 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 96 | May prevent sphingomyelin recognition | ||||
Sequence: N | ||||||
Site | 135 | May prevent sphingomyelin recognition | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoric diester hydrolase activity | |
Molecular Function | toxin activity | |
Biological Process | killing of cells of another organism | |
Biological Process | lipid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameDermonecrotic toxin StSicTox-betaIB1i
- EC number
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Araneae > Araneomorphae > Haplogynae > Scytodoidea > Sicariidae > Sicarius
Accessions
- Primary accessionA0A0D4WV12
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 96 | Has limited impact on substrate specificity and does not alter it qualitatively; when associated with P-135. | ||||
Sequence: N → S | ||||||
Mutagenesis | 135 | Has limited impact on substrate specificity and does not alter it qualitatively; when associated with S-192. Has limited impact on substrate specificity and does not alter it qualitatively; when associated with S-96. | ||||
Sequence: E → P | ||||||
Mutagenesis | 192 | Has limited impact on substrate specificity and does not alter it qualitatively; when associated with P-135. | ||||
Sequence: G → S |
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000447765 | 1-279 | Dermonecrotic toxin StSicTox-betaIB1i | |||
Sequence: GDSRRPIWNIAHMVNDLDLVDEYLDDGANSLELDVEFSKSGTALRTYHGVPCDCFRSCTRSEKFSKYLDYIRQLTTPGNSKFRSRLILLVLDLKLNPLSSSAAYNAGADVARNLLDNYWQRGDSKARAYIVLSLETIAGAEFITGFKDTMKKEGFDEKYYDKIGWDFSGNEDLGKIRDVLESHGIREHIWQGDGITNCLPRDDNRLKQAISRRYSPTYVYADKVYTWSIDKESSIENALRLGVDGVMTNYPARVISVLGEREFSGKLRLATYDDNPWEK | ||||||
Disulfide bond | 52↔58 | |||||
Sequence: CDCFRSC | ||||||
Disulfide bond | 54↔198 | |||||
Sequence: CFRSCTRSEKFSKYLDYIRQLTTPGNSKFRSRLILLVLDLKLNPLSSSAAYNAGADVARNLLDNYWQRGDSKARAYIVLSLETIAGAEFITGFKDTMKKEGFDEKYYDKIGWDFSGNEDLGKIRDVLESHGIREHIWQGDGITNC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Structure
Family & Domains
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length279
- Mass (Da)31,815
- Last updated2015-05-27 v1
- Checksum6A715A8DCA641759
Keywords
- Technical term