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Protein

Omega-hexatoxin-Hv2a

Gene
N/A
Organism
Hadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Potent inhibitor of insect (bee brain), but not mammalian (rat trigeminal neurons), voltage-gated calcium channels (Cav). As for omega-AcTx-Hv1a, the phenotypic effect of injection of this toxin into lone star ticks (Amblyomma americanum) is curling of all eight legs into closed loops, followed by death.1 Publication

GO - Molecular functioni

  • calcium channel inhibitor activity Source: CACAO
  • sodium channel inhibitor activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated calcium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-hexatoxin-Hv2a
Short name:
Omega-HXTX-Hv2a
Alternative name(s):
Omega-atracotoxin-Hv2a
Short name:
AcTx-Hv2
Short name:
Omega-AcTx-Hv2a
OrganismiHadronyche versuta (Blue mountains funnel-web spider) (Atrax versutus)
Taxonomic identifieri6904 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeHexathelidaeHadronyche

Organism-specific databases

ArachnoServeriAS000204. omega-hexatoxin-Hv2a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4545Omega-hexatoxin-Hv2aPRO_0000087669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 181 Publication
Disulfide bondi11 ↔ 241 Publication
Disulfide bondi17 ↔ 291 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
45
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Helixi14 – 163Combined sources
Beta strandi23 – 253Combined sources
Beta strandi28 – 303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G9PNMR-A1-45[»]
1HP3NMR-A1-32[»]
ProteinModelPortaliP82852.
SMRiP82852. Positions 1-32.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82852.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the omega-atracotoxin type 2 family.Curated

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR013139. Omega_atracotoxin_CS2.
IPR012628. Toxin_23.
[Graphical view]
PfamiPF08093. Toxin_23. 1 hit.
[Graphical view]
PROSITEiPS60017. OMEGA_ACTX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P82852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
LLACLFGNGR CSSNRDCCEL TPVCKRGSCV SSGPGLVGGI LGGIL
Length:45
Mass (Da):4,484
Last modified:September 26, 2001 - v1
Checksum:iD9D25DC007A129B7
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G9PNMR-A1-45[»]
1HP3NMR-A1-32[»]
ProteinModelPortaliP82852.
SMRiP82852. Positions 1-32.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000204. omega-hexatoxin-Hv2a.

Miscellaneous databases

EvolutionaryTraceiP82852.

Family and domain databases

InterProiIPR013139. Omega_atracotoxin_CS2.
IPR012628. Toxin_23.
[Graphical view]
PfamiPF08093. Toxin_23. 1 hit.
[Graphical view]
PROSITEiPS60017. OMEGA_ACTX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Discovery and structure of a potent and highly specific blocker of insect calcium channels."
    Wang X.-H., Connor M., Wilson D., Wilson H.I., Nicholson G.M., Smith R., Shaw D., Mackay J.P., Alewood P.F., Christie M.J., King G.F.
    J. Biol. Chem. 276:40306-40312(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS.
    Tissue: Venom.
  2. "Orally active acaricidal peptide toxins from spider venom."
    Mukherjee A.K., Sollod B.L., Wikel S.K., King G.F.
    Toxicon 47:182-187(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTOT2A_HADVE
AccessioniPrimary (citable) accession number: P82852
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: May 11, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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.