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Protein

Potassium channel toxin alpha-KTx 5.1

Gene
N/A
Organism
Leiurus quinquestriatus hebraeus (Yellow scorpion)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Blocker for the small conductance calcium-activated potassium channels (PubMed:2839478, PubMed:2307683, PubMed:11527975). Shows the best affinity for KCa2.2/KCNN2 (Kd=0.2 nM), followed by KCa2.3/KCNN3 (Kd=1.1 nM) and KCa2.1/KCNN1 (Kd=325 nM) (PubMed:11527975).3 Publications

Miscellaneous

A mutant [R7diaminobutanoic acid] has been developed that discriminates KCa2.2/KCNN2 (Kd=3.8 nM) from KCa2.3/KCNN3 (Kd=2500 nM).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN31 Publication1
Sitei2Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN31 Publication1
Sitei7Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN31 Publication1
Sitei24Interacts with KCa2.2/KCNN2 and KCa2.3/KCNN31 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionCalcium-activated potassium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium channel toxin alpha-KTx 5.1
Alternative name(s):
Leiurotoxin I3 Publications
Short name:
LeTx I
Short name:
Lei-I
Leiurotoxin-1Curated
Scyllatoxin2 Publications
Short name:
ScyTx
OrganismiLeiurus quinquestriatus hebraeus (Yellow scorpion)
Taxonomic identifieri6884 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeLeiurus

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6 – 7RM → MR: 50-fold and 60-fold decrease in potency of inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively. 1 Publication2
Mutagenesisi6R → K: 20-fold and 30-fold decrease in potency of inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively. 1 Publication1
Mutagenesisi6R → L: 75-fold and 165-fold decrease in potency of inhibition of KCa2.2/KCNN2 and KCa2.3/KCNN3, respectively. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000449241 – 31Potassium channel toxin alpha-KTx 5.11 PublicationAdd BLAST31

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 212 PublicationsImported
Disulfide bondi8 ↔ 262 PublicationsImported
Disulfide bondi12 ↔ 282 PublicationsImported
Modified residuei31Histidine amide1 Publication1

Post-translational modificationi

Two disulfide bonds are the minimal requirement needed to produce a nativelike and bio-active conformation in this toxin. The third disulfide provides an additional contribution to structure stabilization and can modulate biological potency depending on its position and the structural regions involved in biological activity.1 Publication

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Beta strandi18 – 21Combined sources4
Beta strandi23 – 29Combined sources7

3D structure databases

ProteinModelPortaliP16341
SMRiP16341
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16341

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 9[R/K]XCQ motifCurated4

Domaini

Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).1 Publication

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR036574 Scorpion_toxin-like_sf
IPR001947 Scorpion_toxinS_K_inh
PfamiView protein in Pfam
PF00451 Toxin_2, 1 hit
SUPFAMiSSF57095 SSF57095, 1 hit
PROSITEiView protein in PROSITE
PS01138 SCORP_SHORT_TOXIN, 1 hit

Sequencei

Sequence statusi: Complete.

P16341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
AFCNLRMCQL SCRSLGLLGK CIGDKCECVK H
Length:31
Mass (Da):3,430
Last modified:April 1, 1990 - v1
Checksum:iBB3183DC5CEA53A7
GO

Sequence databases

PIRiA28805

Similar proteinsi

Entry informationi

Entry nameiKAX51_LEIQH
AccessioniPrimary (citable) accession number: P16341
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 28, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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

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