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Reviewed, UniProtKB/Swiss-Prot P08815 (KAX21_CENNO)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Potassium channel toxin alpha-KTx 2.1
Alternative name(s):
    Noxiustoxin
      Short name=NTx
    Toxin II.11
OrganismCentruroides noxius (Mexican scorpion)
Taxonomic identifier6878 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeCentruroides

Protein attributes

Sequence length39 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Blocks voltage-gated non-inactivating potassium channels and unblocks inactivating potassium channels blocked by alpha-dendrotoxin in synaptosomes. Also displaces the alpha-dendrotoxin homolog dendrotoxin I from its receptor on brain synaptic membranes.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

The N-terminus is probably essential for channel affinity.

Miscellaneous

Is more effective than NTX2.

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 2 subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionIonic channel inhibitor
Neurotoxin
Potassium channel inhibitor
Toxin
   PTMAmidation
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Peptide1 – 3939Potassium channel toxin alpha-KTx 2.1
PRO_0000044905

Regions

Region26 – 349Interaction with Ca(2+)-activated K(+) channels Potential

Amino acid modifications

Modified residue391Asparagine amide
Disulfide bond7 ↔ 29 Ref.4
Disulfide bond13 ↔ 34 Ref.4
Disulfide bond17 ↔ 36 Ref.4

Secondary structure

........ 39
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08815-1 [UniParc].

Last modified July 19, 2004. Version 3.
Checksum: 131DC4A78D497E0D

FASTA394,202
        10         20         30 
TIINVKCTSP KQCSKPCKEL YGSSAGAKCM NGKCKCYNN 

« Hide

References

[1]"The primary structure of noxiustoxin. A K channel blocking peptide, purified from the venom of the scorpion Centruroides noxius Hoffmann."
Possani L.D., Martin B.M., Svendsen I.
Carlsberg Res. Commun. 47:285-289(1982)
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Synthetic peptides corresponding to the sequence of noxiustoxin indicate that the active site of this K+ channel blocker is located on its amino-terminal portion."
Gurrola G.B., Molinar-Rode R., Sitges M., Bayon A., Possani L.D.
J. Neural Transm. 77:11-20(1989) [PubMed: 2746197] [Abstract]
Cited for: SYNTHESIS OF 1-9 AND 30-39.
[3]"Structure revision of the scorpion toxin noxiustoxin through total chemical synthesis."
Nutt R.F., Arison B.H., Smith J.S.
(In) Schneider C.H., Eberles A.N. (eds.); Peptides 1992, pp.101-102, Escom Science Publishers, Leiden (1993)
Cited for: SYNTHESIS, AMIDATION.
[4]"Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins."
Dauplais M., Gilquin B., Possani L.D., Gurrola-Briones G., Roumestand C., Menez A.
Biochemistry 34:16563-16573(1995) [PubMed: 8527429] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SXMNMR-A1-39[»]
ModBaseSearch...

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 nameKAX21_CENNO
AccessionPrimary (citable) accession number: P08815
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 19, 2004
Last modified: June 16, 2009
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Scorpion potassium channel toxins

Nomenclature of scorpion potassium channel toxins and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents