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P55927 (KAX71_PANIM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Potassium channel toxin alpha-KTx 7.1
Alternative name(s):
Pandinotoxin-alpha
Potassium channel-blocking toxin 2
Short name=Pi-2
Short name=Pi2
Toxin PiTX-K-alpha
Gene names
Name:PTX-1
OrganismPandinus imperator (Emperor scorpion)
Taxonomic identifier55084 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

Protein attributes

Sequence length47 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.3

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 7 subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIonic channel inhibitor
Neurotoxin
Potassium channel inhibitor
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

   Molecular functionpotassium channel inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1 – 12›12 Ref.2 Ref.3
Peptide13 – 4735Potassium channel toxin alpha-KTx 7.1 Ref.2 Ref.3
PRO_0000035328

Sites

Site361Basic residue of the functional dyad By similarity
Site451Aromatic residue of the functional dyad By similarity

Amino acid modifications

Disulfide bond16 ↔ 37 Ref.4
Disulfide bond22 ↔ 42 Ref.4
Disulfide bond26 ↔ 44 Ref.4

Experimental info

Non-terminal residue11

Secondary structure

....... 47
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P55927 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 21B8BF110A37BD7C

FASTA475,434
        10         20         30         40 
RGSVDYKDDD DKTISCTNPK QCYPHCKKET GYPNAKCMNR KCKCFGR 

« Hide

References

[1]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.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 8913348] [Abstract]
Cited for: PROTEIN SEQUENCE OF 13-47.
Tissue: Venom.
[3]"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: 8660410] [Abstract]
Cited for: PROTEIN SEQUENCE OF 13-47, FUNCTION.
Tissue: Venom.
[4]"Solution structure for Pandinus toxin K-alpha (PiTX-K alpha), a selective blocker of A-type potassium channels."
Tenenholz T.C., Rogowski R.S., Collins J.H., Blaustein M.P., Weber D.J.
Biochemistry 36:2763-2771(1997) [PubMed: 9062103] [Abstract]
Cited for: STRUCTURE BY NMR OF 13-47, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U79579 mRNA. Translation: AAB52576.1.
PIRT10471.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PTANMR-A13-47[»]
ProteinModelPortalP55927.
SMRP55927. Positions 13-47.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001947. Scorpion_toxinS.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSPR00286. CHARYBDTOXIN.
ProDomPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAX71_PANIM
AccessionPrimary (citable) accession number: P55927
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: November 16, 2011
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

Scorpion potassium channel toxins

Nomenclature of scorpion potassium channel toxins and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families