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Protein

Potassium channel toxin alpha-KTx 7.2

Gene
N/A
Organism
Pandinus imperator (Emperor scorpion)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Potent inhibitor of the A-type voltage-gated potassium channels. Most potent inhibitor of Kv1.2/KCNA2 channels. Reversibly block the Shaker B potassium-channels (Kv1.1 sub-family), but with a lower affinity than PiTX-K alpha.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei24 – 241Basic residue of the functional dyadBy similarity
Sitei33 – 331Aromatic residue of the functional dyadBy similarity

GO - Molecular functioni

  1. ion channel inhibitor activity Source: InterPro

GO - Biological processi

  1. defense response Source: InterPro
  2. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel toxin alpha-KTx 7.2
Alternative name(s):
Pandinotoxin-beta
Potassium channel-blocking toxin 3
Short name:
Pi-3
Short name:
Pi3
Toxin PiTX-K-beta
OrganismiPandinus imperator (Emperor scorpion)
Taxonomic identifieri55084 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3535Potassium channel toxin alpha-KTx 7.2PRO_0000044911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 251 Publication
Disulfide bondi10 ↔ 301 Publication
Disulfide bondi14 ↔ 321 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
35
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104Combined sources
Helixi11 – 177Combined sources
Beta strandi23 – 264Combined sources
Beta strandi29 – 324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C49NMR-A1-35[»]
ProteinModelPortaliP55928.
SMRiP55928. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55928.

Family & Domainsi

Domaini

Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).

Sequence similaritiesi

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamiPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSiPR00286. CHARYBDTOXIN.
ProDomiPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57095. SSF57095. 1 hit.
PROSITEiPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55928-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30 
TISCTNEKQC YPHCKKETGY PNAKCMNRKC KCFGR
Length:35
Mass (Da):4,072
Last modified:November 1, 1997 - v1
Checksum:iDFCC26880D4C792A
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C49NMR-A1-35[»]
ProteinModelPortaliP55928.
SMRiP55928. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP55928.

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamiPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSiPR00286. CHARYBDTOXIN.
ProDomiPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57095. SSF57095. 1 hit.
PROSITEiPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Three new toxins from the scorpion Pandinus imperator selectively block certain voltage-gated K+ channels."
    Rogowski R.S., Collins J.H., O'Neill T.J., Gustafson T.A., Werkman T.R., Rogawski M.A., Tenenholz T.C., Weber D.J., Blaustein M.P.
    Mol. Pharmacol. 50:1167-1177(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Venom.
  2. "Two novel toxins from the venom of the scorpion Pandinus imperator show that the N-terminal amino acid sequence is important for their affinities towards Shaker B K+ channels."
    Gomez-Lagunas F., Olamendi-Portugal T., Zamudio F.Z., Possani L.D.
    J. Membr. Biol. 152:49-56(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Venom.
  3. "Structural and functional differences of two toxins from the scorpion Pandinus imperator."
    Klenk K.C., Tenenholz T.C., Matteson D.R., Rogowski R.S., Blaustein M.P., Weber D.J.
    Proteins 38:441-449(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiKAX72_PANIM
AccessioniPrimary (citable) accession number: P55928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 78 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. Scorpion potassium channel toxins
    Nomenclature of scorpion potassium channel toxins and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.