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Protein

Kappa-hexatoxin-Hv1c

Gene
N/A
Organism
Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This excitatory toxin inhibits insect calcium-activated potassium (KCa) channels (Slo-type). Pan-neuronal expression in Drosophila is lethal but flies engineered to express the toxin only in clock neurons have defects in circadian rhythm but a normal lifespan.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2Important for the neurotoxic activity1
Sitei8Critical for the neurotoxic activity1
Sitei9Critical for the neurotoxic activity1
Sitei13Critical for the neurotoxic activity1
Sitei14Critical for the neurotoxic activity1
Sitei29Important for the neurotoxic activity1
Sitei31Critical for the neurotoxic activity1

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium-activated potassium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-hexatoxin-Hv1c
Short name:
Kappa-HXTX-Hv1c
Alternative name(s):
Janus-atracotoxin-Hv1c
Short name:
Janus-AcTx-Hv1c
Kappa-atracotoxin-Hv1c
Short name:
Kappa-AcTx-Hv1c
OrganismiHadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Taxonomic identifieri6904 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeHexathelidaeHadronyche

Organism-specific databases

ArachnoServeriAS000174. kappa-hexatoxin-Hv1c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of recombinant toxin is 320 +-20 pmol/g (according to PubMed:11937509) or 91 +-5 pmol/g (according to PubMed:12220722) when injected into house flies (Musca domestica).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 2Missing : 73-fold decrease in toxicity to flies. 1 Publication2
Mutagenesisi1Missing : No change in toxicity. 1 Publication1
Mutagenesisi2I → A: 7-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi8R → A: 98-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi8R → E: 270-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi9P → A: 269-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi13 – 14CC → SS: 423-fold decrease in toxicity to flies. 1 Publication2
Mutagenesisi29V → A: 13-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi31Y → A: 162-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi31Y → F: 1.8-fold decrease in toxicity to flies. 1 Publication1
Mutagenesisi35 – 37Missing : No change in toxicity to flies. 3
Mutagenesisi36 – 37Missing : No change in toxicity. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000449981 – 37Kappa-hexatoxin-Hv1cAdd BLAST37

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 17
Disulfide bondi10 ↔ 22
Disulfide bondi13 ↔ 14
Disulfide bondi16 ↔ 32

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi20 – 24Combined sources5
Beta strandi30 – 34Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DL0NMR-A1-37[»]
ProteinModelPortaliP82228.
SMRiP82228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82228.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Sequence similaritiesi

Belongs to the Shiva superfamily. Kappa toxin family.Curated

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR012499. Toxin_16.
[Graphical view]
PfamiPF07945. Toxin_16. 1 hit.
[Graphical view]
PROSITEiPS60020. J_ACTX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P82228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
AICTGADRPC AACCPCCPGT SCKAESNGVS YCRKDEP
Length:37
Mass (Da):3,768
Last modified:May 30, 2000 - v1
Checksum:iE4DDF046CC750FFC
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DL0NMR-A1-37[»]
ProteinModelPortaliP82228.
SMRiP82228.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000174. kappa-hexatoxin-Hv1c.

Miscellaneous databases

EvolutionaryTraceiP82228.

Family and domain databases

InterProiIPR012499. Toxin_16.
[Graphical view]
PfamiPF07945. Toxin_16. 1 hit.
[Graphical view]
PROSITEiPS60020. J_ACTX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTK1C_HADVE
AccessioniPrimary (citable) accession number: P82228
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 70 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 affect a wide range of potassium, calcium and sodium voltage-gated channels.1 Publication

Caution

This toxin should be named lambda-hexatoxin-Hv1c (instead of kappa), since lambda is the Greek letter attributed to calcium-activated potassium (KCa) channel impairing toxins (according to the nomenclature of King et al., 2008).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.