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Protein

Delta-actitoxin-Avd1a

Gene
N/A
Organism
Anemonia sulcata (Mediterranean snakelocks sea anemone)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Binds specifically to voltage-gated sodium channels (Nav) and delays their inactivation during signal transduction (when tested on the soma membrane of a crustacean neuron). Has also been observed to affect the activation of the sodium current.1 Publication

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-Avd1a1 Publication
Short name:
Delta-AITX-Avd1a1 Publication
Alternative name(s):
As1
Delta-actitoxin-Avd1b1 Publication
Short name:
Delta-AITX-Avd1b1 Publication
Toxin ATX-I1 Publication
Short name:
ATX I1 Publication
Toxin-11 Publication
OrganismiAnemonia sulcata (Mediterranean snakelocks sea anemone)
Taxonomic identifieri6108 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaNynantheaeActiniidaeAnemonia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4646Delta-actitoxin-Avd1a1 PublicationPRO_0000221512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 431 Publication
Disulfide bondi6 ↔ 341 Publication
Disulfide bondi27 ↔ 441 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
46
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi16 – 2510Combined sources
Beta strandi32 – 343Combined sources
Beta strandi37 – 459Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATXNMR-A1-46[»]
ProteinModelPortaliP01533.
SMRiP01533. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01533.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.20.20.10. 1 hit.
InterProiIPR000693. Anenome_toxin.
IPR023355. Myo_neuro_toxin.
[Graphical view]
PfamiPF00706. Toxin_4. 1 hit.
[Graphical view]
PIRSFiPIRSF001905. Anenome_toxin. 1 hit.

Sequencei

Sequence statusi: Complete.

P01533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
GAACLCKSDG PNTRGNSMSG TIWVFGCPSG WNNCEGRAII GYCCKQ
Length:46
Mass (Da):4,814
Last modified:July 21, 1986 - v1
Checksum:i862C1E21FDA5432D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31A → P in about 20% of the molecules.

Sequence databases

PIRiA01796. TZAZ1.

Cross-referencesi

Sequence databases

PIRiA01796. TZAZ1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATXNMR-A1-46[»]
ProteinModelPortaliP01533.
SMRiP01533. Positions 1-46.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP01533.

Family and domain databases

Gene3Di2.20.20.10. 1 hit.
InterProiIPR000693. Anenome_toxin.
IPR023355. Myo_neuro_toxin.
[Graphical view]
PfamiPF00706. Toxin_4. 1 hit.
[Graphical view]
PIRSFiPIRSF001905. Anenome_toxin. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Amino-acid sequence of toxin I from Anemonia sulcata."
    Wunderer G., Eulitz M.
    Eur. J. Biochem. 89:11-17(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Nematoblast.
  2. "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.
  3. "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.
  4. "The secondary structure of the toxin ATX Ia from Anemonia sulcata in aqueous solution determined on the basis of complete sequence-specific 1H-NMR assignments."
    Widmer H., Wagner G., Schweitz H., Lazdunski M., Wuethrich K.
    Eur. J. Biochem. 171:177-192(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
  5. "Three-dimensional structure of the neurotoxin ATX Ia from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy."
    Widmer H., Billeter M., Wuethrich K.
    Proteins 6:357-371(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiNA11_ANESU
AccessioniPrimary (citable) accession number: P01533
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 9, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Does not have effect on potassium or calcium currents with concentrations up to 5 µM (PubMed:2409523). Is inactive at excitable membranes of frog (Inferred fromPubMed:2409523).1 Publication

Caution

Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species.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.