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Protein

Potassium channel toxin alpha-KTx 4.1

Gene
N/A
Organism
Tityus serrulatus (Brazilian scorpion)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Potently blocks Kv1.1/KCNA1 (85%), Kv1.2/KCNA2 (91%), Kv1.3/KCNA3 (89%), Kv1.6/KCNA6 (94%), and Shaker (97%).3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271Basic residue of the functional dyadBy similarity
Sitei36 – 361Aromatic 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

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel toxin alpha-KTx 4.1
Alternative name(s):
TSK4
Tityustoxin K-alpha
Short name:
TsTX-K-alpha
Toxin II-9
Ts7
OrganismiTityus serrulatus (Brazilian scorpion)
Taxonomic identifieri6887 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271K → A, E or R: Significant loss of affinity for squid Kv1A channel. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3737Potassium channel toxin alpha-KTx 4.1PRO_0000044923Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi7 ↔ 281 Publication
Disulfide bondi13 ↔ 331 Publication
Disulfide bondi17 ↔ 351 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
37
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2011Combined sources
Beta strandi26 – 294Combined sources
Beta strandi32 – 354Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HP2NMR-A1-37[»]
ProteinModelPortaliP46114.
SMRiP46114. Positions 1-37.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46114.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 338Interaction with Ca(2+)-activated K(+) channelsSequence Analysis

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.

P46114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
VFINAKCRGS PECLPKCKEA IGKAAGKCMN GKCKCYP
Length:37
Mass (Da):3,948
Last modified:November 1, 1995 - v1
Checksum:i639B98A977335929
GO

Mass spectrometryi

Molecular mass is 3942 Da from positions 1 - 37. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HP2NMR-A1-37[»]
ProteinModelPortaliP46114.
SMRiP46114. Positions 1-37.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP46114.

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. "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. "Electrophysiological characterization of Ts6 and Ts7, K+ channel toxins isolated through an improved Tityus serrulatus venom purification procedure."
    Cerni F.A., Pucca M.B., Peigneur S., Cremonez C.M., Bordon K.C., Tytgat J., Arantes E.C.
    Toxins 6:892-913(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION.
    Tissue: Venom.
  5. "Tityustoxin-K(alpha) blockade of the voltage-gated potassium channel Kv1.3."
    Rodrigues A.R., Arantes E.C., Monje F., Stuehmer W., Varanda W.A.
    Br. J. Pharmacol. 139:1180-1186(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS KV1.3 CHANNEL BLOCKER, MASS SPECTROMETRY.
  6. "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.

Entry informationi

Entry nameiKAX41_TITSE
AccessioniPrimary (citable) accession number: P46114
Secondary accession number(s): P08816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Inhibits with low efficiency Kv1.5/KCNA5, Kv2.1/KCNB1, Kv7.1/KCNQ1 and ERG/KCNH2. Does not inhibit Kv1.4/KCNA4, Kv3.1/KCNC1, Kv7.2/KCNQ2 (PubMed:24590385).1 Publication

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.