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Protein

DeltaKappa-actitoxin-Avd4a

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

Acts as a gating modifier on both Kv and Nav ion channels. Voltage-dependently inhibits voltage-gated potassium channels Kv3 (Kv3.1/KCNC1, Kv3.2/KCNC2 and Kv3.4/KCNC4) and slows inactivation of the voltage-gated sodium channel Nav1.7/SCN9A (PubMed:16177043, PubMed:22442564, PubMed:9506974). Inhibits all Kv3.1, Kv3.2 and Kv3.4 by about 50% when tested at a voltage of +40 mV (45%, 48% and 56%, respectively). May act by binding residues in voltage-sensing domains S3b and S4 of Kv3 (PubMed:16177043). Tests have been done on human Nav1.7/SCN9A (expressed in HEK293 cells) (EC(50)=3 nM) and rat SCG neurons that mostly carry Nav1.7 channels (EC(50)=300 nM) (PubMed:22442564). This toxin also reduces blood pressure (Ref. 1).4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Protein family/group databases

TCDBi8.B.11.1.3. the sea anemone peptide toxin (apetx) family.

Names & Taxonomyi

Protein namesi
Recommended name:
DeltaKappa-actitoxin-Avd4a1 Publication
Short name:
DeltaKappa-AITX-Avd4a1 Publication
Alternative name(s):
Antihypertensive protein BDS-1
Blood depressing substance I1 Publication
Short name:
BDS-I1 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 – 4343DeltaKappa-actitoxin-Avd4a2 PublicationsPRO_0000221541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 391 Publication
Disulfide bondi6 ↔ 321 Publication
Disulfide bondi22 ↔ 401 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
43
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi14 – 163Combined sources
Beta strandi31 – 344Combined sources
Beta strandi37 – 404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDSNMR-A1-43[»]
2BDSNMR-A1-43[»]
ProteinModelPortaliP11494.
SMRiP11494. Positions 1-43.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11494.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.20.20.10. 1 hit.
InterProiIPR012414. BDS_K_chnl_tox.
IPR023355. Myo_neuro_toxin.
[Graphical view]
PfamiPF07936. Defensin_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11494-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
AAPCFCSGKP GRGDLWILRG TCPGGYGYTS NCYKWPNICC YPH
Length:43
Mass (Da):4,714
Last modified:October 1, 1989 - v1
Checksum:i7C17846E88E2F1D8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181L → F.

Sequence databases

PIRiA33041.

Cross-referencesi

Sequence databases

PIRiA33041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BDSNMR-A1-43[»]
2BDSNMR-A1-43[»]
ProteinModelPortaliP11494.
SMRiP11494. Positions 1-43.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi8.B.11.1.3. the sea anemone peptide toxin (apetx) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11494.

Family and domain databases

Gene3Di2.20.20.10. 1 hit.
InterProiIPR012414. BDS_K_chnl_tox.
IPR023355. Myo_neuro_toxin.
[Graphical view]
PfamiPF07936. Defensin_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Polypeptides, process for their preparation, and their use as hypotensive active compounds."
    Beress L., Doppelfeld I.-S., Etschenberg E., Graf E., Henschen-Edman A., Zwick J.
    Patent number DE3324689, 17-JAN-1985
    Cited for: PROTEIN SEQUENCE, FUNCTION.
  2. "Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4."
    Diochot S., Schweitz H., Beress L., Lazdunski M.
    J. Biol. Chem. 273:6744-6749(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
  3. "Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies."
    Yeung S.Y., Thompson D., Wang Z., Fedida D., Robertson B.
    J. Neurosci. 25:8735-8745(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Modulation of neuronal sodium channels by the sea anemone peptide BDS-I."
    Liu P., Jo S., Bean B.P.
    J. Neurophysiol. 107:3155-3167(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION ON NAV1.7/SCN9A.
  5. "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.
  6. "A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure."
    Driscoll P.C., Clore G.M., Beress L., Gronenborn A.M.
    Biochemistry 28:2178-2187(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
  7. "Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing."
    Driscoll P.C., Gronenborn A.M., Beress L., Clore G.M.
    Biochemistry 28:2188-2198(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiBDS1_ANESU
AccessioniPrimary (citable) accession number: P11494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: December 9, 2015
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

This toxin does not have effect on Nav1.1/SCN1A and Nav1.6/SCN8A sodium channels (PubMed:22442564). It has little or no functional effect on cardiac muscle, as well as on skeletal muscle myotubes, suggesting lack of functional interaction with Nav1.4/SCN4A or Nav1.5/SCN5A (PubMed:9506974).2 Publications

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.