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Protein

Kappa-stichotoxin-She3a

Gene
N/A
Organism
Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits voltage-dependent potassium channels. Inhibits Kv1.3/KCNA3 potently and also blocks Kv1.1/KCNA1, Kv1.4/KCNA4, and Kv1.6/KCNA6 at subnanomolar concentrations.1 Publication

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin, Voltage-gated potassium channel impairing toxin

Protein family/group databases

TCDBi8.B.14.1.2. the sea anemone peptide toxin, class 1 (bgk) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-stichotoxin-She3a1 Publication
Short name:
Kappa-SHTX-She3a1 Publication
Alternative name(s):
Potassium channel toxin ShK1 Publication
OrganismiStichodactyla helianthus (Sun anemone) (Stoichactis helianthus)
Taxonomic identifieri6123 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaHexacoralliaActiniariaStichodactylidaeStichodactyla

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nematocyst, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3535Kappa-stichotoxin-She3a2 PublicationsPRO_0000044866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 354 Publications
Disulfide bondi12 ↔ 284 Publications
Disulfide bondi17 ↔ 324 Publications

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
35
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Helixi9 – 113Combined sources
Helixi14 – 196Combined sources
Helixi21 – 255Combined sources
Turni29 – 335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BEINMR-A1-35[»]
1C2UNMR-A1-35[»]
1ROONMR-A1-35[»]
2K9ENMR-A1-35[»]
4LFQX-ray1.06A1-35[»]
4LFSX-ray0.97A1-35[»]
4Z7PX-ray1.20A1-35[»]
ProteinModelPortaliP29187.
SMRiP29187. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 3533ShKTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232Crucial for binding to potassium channelsBy similarity

Sequence similaritiesi

Contains 1 ShKT domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR003582. ShKT_dom.
[Graphical view]
PROSITEiPS51670. SHKT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
RSCIDTIPKS RCTAFQCKHS MKYRLSFCRK TCGTC
Length:35
Mass (Da):4,061
Last modified:December 1, 1992 - v1
Checksum:iF53EF5D576734B6E
GO

Mass spectrometryi

Molecular mass is 4054.82±0.1 Da from positions 1 - 35. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BEINMR-A1-35[»]
1C2UNMR-A1-35[»]
1ROONMR-A1-35[»]
2K9ENMR-A1-35[»]
4LFQX-ray1.06A1-35[»]
4LFSX-ray0.97A1-35[»]
4Z7PX-ray1.20A1-35[»]
ProteinModelPortaliP29187.
SMRiP29187. Positions 1-35.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi8.B.14.1.2. the sea anemone peptide toxin, class 1 (bgk) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP29187.

Family and domain databases

InterProiIPR003582. ShKT_dom.
[Graphical view]
PROSITEiPS51670. SHKT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus."
    Castaneda O., Sotolongo V., Amor A.M., Stoecklin R., Anderson A.J., Harvey A.L., Engstrom A., Wernstedt C., Karlsson E.
    Toxicon 33:603-613(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY.
    Tissue: Nematoblast.
  2. Karlsson E., Harvey A.L., Aneiros A., Castaneda O.
    (In) Xeme congres europeen de toxinologie, pp.35-35, Paris (1992)
    Cited for: PROTEIN SEQUENCE.
  3. Stoecklin R., Harvey A.L., Karlsson E.
    (In) 11th congress on animal, plant and microbial toxins, International Society on Toxinology, pp.132-132, Tel Aviv University, Tel Aviv (1994)
    Cited for: DISULFIDE BONDS, SIMILARITY.
  4. "Assignment of the three disulfide bonds in ShK toxin. A potent potassium channel inhibitor from the sea anemone Stichodactyla helianthus."
    Pohl J., Hubalek F., Byrnes M.E., Nielsen K.R., Woods A., Pennington M.W.
    Lett. Pept. Sci. 1:291-297(1995)
    Cited for: DISULFIDE BONDS.
  5. "Development of a rational nomenclature for naming peptide and protein toxins from sea anemones."
    Oliveira J.S., Fuentes-Silva D., King G.F.
    Toxicon 60:539-550(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  6. "Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone."
    Tudor J.E., Pallaghy P.K., Pennington M.W., Norton R.S.
    Nat. Struct. Biol. 3:317-320(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
  7. Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Entry informationi

Entry nameiK1A_STIHL
AccessioniPrimary (citable) accession number: P29187
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 9, 2015
This is version 97 of the entry and version 1 of the sequence. [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. SIMILARITY comments
    Index of protein domains and families

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 one 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.