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Protein

Kappa-actitoxin-Ael2a

Gene
N/A
Organism
Anthopleura elegantissima (Sea anemone)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Potently and reversibly blocks human Kv11.1/KCNH2/ERG1 (IC50=34 nM) (PubMed:12815161, PubMed:16497878, PubMed:17473056), rat Kv11.1/KCNH2/ERG1 (PubMed:16497878) and Kv11.3/KCNH7/ERG3 (PubMed:17473056) voltage-gated potassium channels in a similar potency. Acts as a gating-modifier toxin that shifts the voltage-dependence of ERG activation in the positive direction and suppresses its current amplitudes elicited by strong depolarizing pulses that maximally activate the channels (PubMed:12815161, PubMed:17473056). Does not induce neurotoxic symptoms when injected into mice (PubMed:12815161).2 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

Protein family/group databases

TCDBi8.B.11.1.1. the sea anemone peptide toxin (apetx) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-actitoxin-Ael2a1 Publication
Short name:
Kappa-AITX-Ael2a1 Publication
Alternative name(s):
Toxin APETx11 Publication
OrganismiAnthopleura elegantissima (Sea anemone)
Taxonomic identifieri6110 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaNynantheaeActiniidaeAnthopleura

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4242Kappa-actitoxin-Ael2a1 PublicationPRO_0000221539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 371 Publication
Disulfide bondi6 ↔ 301 Publication
Disulfide bondi20 ↔ 381 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
42
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi9 – 168Combined sources
Beta strandi28 – 325Combined sources
Beta strandi35 – 406Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WQKNMR-A1-42[»]
ProteinModelPortaliP61541.
SMRiP61541. Positions 1-42.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61541.

Family & Domainsi

Domaini

Has the CSbeta/beta fold, which comprises anti-parallel beta-sheets stabilized by three or four disulfide bonds.1 Publication

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.

P61541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
GTTCYCGKTI GIYWFGTKTC PSNRGYTGSC GYFLGICCYP VD
Length:42
Mass (Da):4,558
Last modified:May 24, 2004 - v1
Checksum:i55069008814B3715
GO

Mass spectrometryi

Molecular mass is 4552.21 Da from positions 1 - 42. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WQKNMR-A1-42[»]
ProteinModelPortaliP61541.
SMRiP61541. Positions 1-42.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi8.B.11.1.1. the sea anemone peptide toxin (apetx) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP61541.

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...

Entry informationi

Entry nameiBDS1_ANTEL
AccessioniPrimary (citable) accession number: P61541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: December 9, 2015
This is version 53 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 block Kv11.2/KCNH6/ERG2 (PubMed:17473056), Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.5/KCNA5, Kv1.6/KCNA6, Kv2.1/KCNB1, Kv3.4/KCNC4, Kv4.2/KCND2, Kv7.1/KCNQ1, Kv7.2/KCNQ2, Kv7.3/KCNQ3, Kv10.1/EAG1/KCNH1 and Kv12.3/ELK1/KCNH4 (PubMed:12815161). Inhibits slightly Kv1.4 KCNA4 (27%) (PubMed:12815161).2 Publications

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.