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Protein

Delta-actitoxin-Avd2a

Gene
N/A
Organism
Anemonia sulcata (Mediterranean snakelocks sea anemone)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Specific arthropod (crab and insect) toxin that inhibits inactivation of voltage-gated sodium channels. It competes well with the site-3 toxin LqhalphaIT (from the scorpion L.quinquestriatus (AC P17728)) on binding to cockroach neuronal membranes (Ki=21.4 nM), and inhibits the inactivation of D.melanogaster channel (DmNav1), but not that of mammalian Navs expressed in Xenopus oocytes. Its activity is synergically enhanced by ligands of receptor site-4 (Bj-xtrIT (AC P56637)). Its ability to inhibit the channel mutant DmNav1[D1701R] only decreases 5-fold, whereas the inhibition activity is completely lost by LqhalphaIT and Av2 when tested on DmNav1[D1701R].3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-actitoxin-Avd2a1 Publication
Short name:
Delta-AITX-Avd2a1 Publication
Alternative name(s):
ATX III1 Publication
Av31 Publication
Neurotoxin 3
Neurotoxin III2 Publications
OrganismiAnemonia sulcata (Mediterranean snakelocks sea anemone)
Taxonomic identifieri6108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaNynantheaeActiniidaeAnemonia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

Pathology & Biotechi

Toxic dosei

Dose that causes irreversible contraction paralysis (ED(50)) is 1.15 pmol/100 mg (native toxin) or 2.65 pmol/100 mg (recombinant toxin) when injected inter-segmentally into blowfly larvae (S.falculata).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11R → A: Low decrease in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi2 – 21S → A: No change in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi5 – 51P → A: Low decrease in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi7 – 71Y → A: Loss of binding affinity to cockroach neuronal membranes and of toxicity to blowfly larvae. 1 Publication
Mutagenesisi8 – 81W → A: Loss of binding affinity to cockroach neuronal membranes and of toxicity to blowfly larvae. 1 Publication
Mutagenesisi12 – 121P → A: Loss of binding affinity to cockroach neuronal membranes and of toxicity to blowfly larvae. 1 Publication
Mutagenesisi13 – 131W → A: Loss of binding affinity to cockroach neuronal membranes and of toxicity to blowfly larvae. 1 Publication
Mutagenesisi15 – 151Q → A: No change in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi16 – 161N → A: No change in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi18 – 181Y → A: Loss of binding affinity to cockroach neuronal membranes and of toxicity to blowfly larvae. 1 Publication
Mutagenesisi19 – 191P → A: Low decrease in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi20 – 201E → A: Low increase in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi23 – 231S → A: Low increase in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi25 – 251P → A: Low increase in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi26 – 261K → A: No change in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication
Mutagenesisi27 – 271V → A: No change in binding affinity to cockroach neuronal membranes and in toxicity to blowfly larvae. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 2727Delta-actitoxin-Avd2a1 PublicationPRO_0000044860Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 172 Publications
Disulfide bondi4 ↔ 112 Publications
Disulfide bondi6 ↔ 222 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
27
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 104Combined sources
Beta strandi12 – 143Combined sources
Beta strandi22 – 254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ANSNMR-A1-27[»]
ProteinModelPortaliP01535.
SMRiP01535. Positions 1-27.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01535.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR016330. Neurotoxin_3_Actiniidae.
IPR012509. Neurotoxin_3_Anemonia.
[Graphical view]
PfamiPF08098. ATX_III. 1 hit.
[Graphical view]
PIRSFiPIRSF001906. Neurotoxin_III_Actiniidae. 1 hit.
SUPFAMiSSF57419. SSF57419. 1 hit.

Sequencei

Sequence statusi: Complete.

P01535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
RSCCPCYWGG CPWGQNCYPE GCSGPKV
Length:27
Mass (Da):2,938
Last modified:July 21, 1986 - v1
Checksum:iAA4E261FFAF34A7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 232CS → SC AA sequence (PubMed:21843).Curated

Sequence databases

PIRiA91446. TZAZ3.

Cross-referencesi

Sequence databases

PIRiA91446. TZAZ3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ANSNMR-A1-27[»]
ProteinModelPortaliP01535.
SMRiP01535. Positions 1-27.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01535.

Family and domain databases

InterProiIPR016330. Neurotoxin_3_Actiniidae.
IPR012509. Neurotoxin_3_Anemonia.
[Graphical view]
PfamiPF08098. ATX_III. 1 hit.
[Graphical view]
PIRSFiPIRSF001906. Neurotoxin_III_Actiniidae. 1 hit.
SUPFAMiSSF57419. SSF57419. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Toxin III from Anemonia sulcata: primary structure."
    Martinez G., Kopeyan C., Schweitz H., Lazdunski M.
    FEBS Lett. 84:247-252(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Nematoblast.
  2. "Amino acid sequence of toxin III from Anemonia sulcata."
    Beress L., Wunderer G., Wachter E.
    Hoppe-Seyler's Z. Physiol. Chem. 358:985-988(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE.
  3. "Anemonia sulcata toxins modify activation and inactivation of Na+ currents in a crayfish neurone."
    Hartung K., Rathmayer W.
    Pflugers Arch. 404:119-125(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Molecular analysis of the sea anemone toxin Av3 reveals selectivity to insects and demonstrates the heterogeneity of receptor site-3 on voltage-gated Na+ channels."
    Moran Y., Kahn R., Cohen L., Gur M., Karbat I., Gordon D., Gurevitz M.
    Biochem. J. 406:41-48(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TOXIC DOSE, MUTAGENESIS OF ARG-1; SER-2; PRO-5; TYR-7; TRP-8; PRO-12; TRP-13; GLN-15; ASN-16; TYR-18; PRO-19; GLU-20; SER-23; PRO-25; LYS-26 AND VAL-27.
  5. "Fusion and retrotransposition events in the evolution of the sea anemone Anemonia viridis neurotoxin genes."
    Moran Y., Weinberger H., Lazarus N., Gur M., Kahn R., Gordon D., Gurevitz M.
    J. Mol. Evol. 69:115-124(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Development of a rational nomenclature for naming peptide and protein toxins from sea anemones."
    Oliveira J.S., Fuentes-Silva D., King G.F.
    Toxicon 60:539-550(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  7. "1H-NMR study of the solution properties and secondary structure of neurotoxin III from the sea anemone Anemonia sulcata."
    Norton R.S., Cross K., Braach-Maksvytis V., Wachter E.
    Biochem. J. 293:545-551(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
  8. "Three-dimensional structure in solution of neurotoxin III from the sea anemone Anemonia sulcata."
    Manoleras N., Norton R.S.
    Biochemistry 33:11051-11061(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiSTX3_ANESU
AccessioniPrimary (citable) accession number: P01535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 17, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Is inactive on mammals, when tested by subcutaneous injection into mice at a high dose (up to 5940 nmol/kg of mouse). Does not inhibit rNav1.2/SCN2A, rNav1.4/SCN4A, hNav1.5/SCN5A and rNav1.6/SCN8A.1 Publication

Caution

Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. Authors from PubMed:17492942 and PubMed:19609479 consider they are only one species, it is why their studies (on A.viridis) are integrated in this entry on A.sulcata.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.