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P46114

- KAX41_TITSE

UniProt

P46114 - KAX41_TITSE

Protein

Potassium channel toxin alpha-KTx 4.1

Gene
N/A
Organism
Tityus serrulatus (Brazilian scorpion)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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 – 2011
    Beta strandi26 – 294
    Beta strandi32 – 354

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    VFINAKCRGS PECLPKCKEA IGKAAGKCMN GKCKCYP                 37
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HP2 NMR - A 1-37 [» ]
    ProteinModelPortali P46114.
    SMRi P46114. Positions 1-37.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P46114.

    Family and domain databases

    Gene3Di 3.30.30.10. 1 hit.
    InterProi IPR003614. Scorpion_toxin-like.
    IPR001947. Scorpion_toxinS_K_inh.
    [Graphical view ]
    Pfami PF00451. Toxin_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00286. CHARYBDTOXIN.
    ProDomi PD003586. Scorpion_toxinS. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF57095. SSF57095. 1 hit.
    PROSITEi PS01138. SCORP_SHORT_TOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 77 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