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P46114 (KAX41_TITSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 75. 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 4.1
Alternative name(s):
TSK4
Tityustoxin K-alpha
Short name=TsTX-K-alpha
Toxin II-9
OrganismTityus serrulatus (Brazilian scorpion)
Taxonomic identifier6887 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Protein attributes

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

General annotation (Comments)

Function

Blocks calcium-activated potassium channels and voltage-gated non-inactivating potassium channels and unblocks inactivating potassium channels blocked by alpha-dendrotoxin in synaptosomes. Binds to a site on the inactivating potassium channel that does not occlude the pore. Its binding apparently prevents alpha-DTX, but not charybdotoxin, from blocking the pore. Ref.1

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

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

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 4 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionion channel inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3737Potassium channel toxin alpha-KTx 4.1
PRO_0000044923

Regions

Region26 – 338Interaction with Ca(2+)-activated K(+) channels Potential

Sites

Site271Basic residue of the functional dyad By similarity
Site361Aromatic residue of the functional dyad By similarity

Amino acid modifications

Disulfide bond7 ↔ 28 Ref.4
Disulfide bond13 ↔ 33 Ref.4
Disulfide bond17 ↔ 35 Ref.4

Experimental info

Mutagenesis271K → A, E or R: Significant loss of affinity for squid Kv1A channel. Ref.4

Secondary structure

....... 37
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46114 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 639B98A977335929

FASTA373,948
        10         20         30 
VFINAKCRGS PECLPKCKEA IGKAAGKCMN GKCKCYP 

« Hide

References

[1]"Tityustoxin K alpha blocks voltage-gated noninactivating K+ channels and unblocks inactivating K+ channels blocked by alpha-dendrotoxin in synaptosomes."
Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.
Proc. Natl. Acad. Sci. U.S.A. 91:1475-1479(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION.
Tissue: Venom.
[2]Erratum
Rogowski R.S., Krueger B.K., Collins J.H., Blaustein M.P.
Proc. Natl. Acad. Sci. U.S.A. 93:12051-12051(1996)
[3]"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 OF 1-30.
Tissue: Venom.
[4]"Interaction of a toxin from the scorpion Tityus serrulatus with a cloned K+ channel from squid (sqKv1A)."
Ellis K.C., Tenenholz T.C., Jerng H., Hayhurst M., Dudlak C.S., Gilly W.F., Blaustein M.P., Weber D.J.
Biochemistry 40:5942-5953(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS, MUTAGENESIS OF LYS-27.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HP2NMR-A1-37[»]
ProteinModelPortalP46114.
SMRP46114. Positions 1-37.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR003614. Scorpion_toxin-like.
IPR001947. Scorpion_toxinS_K_inh.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSPR00286. CHARYBDTOXIN.
ProDomPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF57095. SSF57095. 1 hit.
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46114.

Entry information

Entry nameKAX41_TITSE
AccessionPrimary (citable) accession number: P46114
Secondary accession number(s): P08816
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 75 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

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