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P82228 (TJT1C_HADVE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Taxonomic identifier6904 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeHexathelidaeHadronyche

Protein attributes

Sequence length37 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This excitatory toxin inhibits insect calcium-activated potassium 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. Ref.1 Ref.4 Ref.5 Ref.6

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

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

Toxic dose

LD50 of recombinant toxin is 320 +-20 pmol/g (according to Ref.2) or 91 +-5 pmol/g (according to Ref.3) when injected into house flies (Musca domestica). Ref.2 Ref.3

Sequence similarities

Belongs to the janus-atracotoxin family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainKnottin
   Molecular functionIon channel impairing toxin
Neurotoxin
Potassium channel impairing toxin
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3737Kappa-hexatoxin-Hv1c
PRO_0000044998

Sites

Site21Important for the neurotoxic activity
Site81Critical for the neurotoxic activity
Site91Critical for the neurotoxic activity
Site131Critical for the neurotoxic activity
Site141Critical for the neurotoxic activity
Site291Important for the neurotoxic activity
Site311Critical for the neurotoxic activity

Amino acid modifications

Disulfide bond3 ↔ 17
Disulfide bond10 ↔ 22
Disulfide bond13 ↔ 14
Disulfide bond16 ↔ 32

Experimental info

Mutagenesis1 – 22Missing: 73-fold decrease in toxicity to flies. Ref.2 Ref.3
Mutagenesis11Missing: No change in toxicity. Ref.3
Mutagenesis21I → A: 7-fold decrease in toxicity to flies. Ref.2
Mutagenesis81R → A: 98-fold decrease in toxicity to flies. Ref.2
Mutagenesis81R → E: 270-fold decrease in toxicity to flies. Ref.2
Mutagenesis91P → A: 269-fold decrease in toxicity to flies. Ref.2
Mutagenesis13 – 142CC → SS: 423-fold decrease in toxicity to flies.
Mutagenesis291V → A: 13-fold decrease in toxicity to flies. Ref.2
Mutagenesis311Y → A: 162-fold decrease in toxicity to flies. Ref.2
Mutagenesis311Y → F: 1.8-fold decrease in toxicity to flies. Ref.2
Mutagenesis35 – 373Missing: No change in toxicity to flies.
Mutagenesis36 – 372Missing: No change in toxicity.

Secondary structure

..... 37
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82228 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: E4DDF046CC750FFC

FASTA373,768
        10         20         30 
AICTGADRPC AACCPCCPGT SCKAESNGVS YCRKDEP 

« Hide

References

[1]"Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge."
Wang X.-H., Connor M., Smith R., Maciejewski M.W., Howden M.E.H., Nicholson G.M., Christie M.J., King G.F.
Nat. Struct. Biol. 7:505-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, STRUCTURE BY NMR.
Tissue: Venom.
[2]"Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function."
Maggio F., King G.F.
J. Biol. Chem. 277:22806-22813(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ILE-2; ARG-8; PRO-9; 13-CYS-CYS-14; VAL-29 AND TYR-31, LETHAL DOSE.
[3]"Role of the structurally disordered N- and C-terminal residues in the Janus-faced atracotoxins."
Maggio F., King G.F.
Toxicon 40:1355-1361(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ALA-1; 1-ALA-ILE-2 AND 36-GLU-PRO-37, LETHAL DOSE.
[4]"A model genetic system for testing the in vivo function of peptide toxins."
Tedford H.W., Maggio F., Reenan R.A., King G.
Peptides 28:51-56(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Phase coupling of a circadian neuropeptide with rest/activity rhythms detected using a membrane-tethered spider toxin."
Wu Y., Cao G., Pavlicek B., Luo X., Nitabach M.N.
PLoS Biol. 6:E273-E273(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels."
Gunning S.J., Maggio F., Windley M.J., Valenzuela S.M., King G.F., Nicholson G.M.
FEBS J. 275:4045-4059(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DL0NMR-A1-37[»]
ProteinModelPortalP82228.
SMRP82228. Positions 1-37.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ArachnoServerAS000174. kappa-hexatoxin-Hv1c.

Family and domain databases

InterProIPR012499. Toxin_16.
[Graphical view]
PfamPF07945. Toxin_16. 1 hit.
[Graphical view]
PROSITEPS60020. J_ACTX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP82228.

Entry information

Entry nameTJT1C_HADVE
AccessionPrimary (citable) accession number: P82228
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 16, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references