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Protein

Kappa-theraphotoxin-Ps1a

Gene
N/A
Organism
Paraphysa scrofa (Chilean copper tarantula) (Phrixotrichus auratus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Potently blocks A-type potassium currents. Specifically blocks Kv4.2/KCND2 and Kv4.3/KCND3 channels by altering the gating properties of these channels.1 Publication

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-theraphotoxin-Ps1a
Short name:
Kappa-TRTX-Ps1a
Alternative name(s):
PaTX1
Phrixotoxin-1
OrganismiParaphysa scrofa (Chilean copper tarantula) (Phrixotrichus auratus)
Taxonomic identifieri269635 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeParaphysa

Organism-specific databases

ArachnoServeriAS000399. kappa-theraphotoxin-Ps1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 2929Kappa-theraphotoxin-Ps1aPRO_0000044555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi2 ↔ 161 Publication
Disulfide bondi9 ↔ 211 Publication
Disulfide bondi15 ↔ 251 Publication
Modified residuei29 – 291Isoleucine amide1 Publication

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

1
29
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 267Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V7FNMR-A1-29[»]
ProteinModelPortaliP61230.
SMRiP61230. Positions 1-29.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61230.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Sequence similaritiesi

Belongs to the phrixotoxin family.Curated

Keywords - Domaini

Knottin

Sequencei

Sequence statusi: Complete.

P61230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
YCQKWMWTCD SARKCCEGLV CRLWCKKII
Length:29
Mass (Da):3,555
Last modified:May 10, 2004 - v1
Checksum:i3B80CAB68C1B9B36
GO

Mass spectrometryi

Molecular mass is 3547.60 Da from positions 1 - 29. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V7FNMR-A1-29[»]
ProteinModelPortaliP61230.
SMRiP61230. Positions 1-29.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000399. kappa-theraphotoxin-Ps1a.

Miscellaneous databases

EvolutionaryTraceiP61230.

Family and domain databases

ProtoNetiSearch...

Entry informationi

Entry nameiTXP1_PARSR
AccessioniPrimary (citable) accession number: P61230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: December 9, 2015
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

This toxin does not inhibit Kv1/KCNA, Kv2/KCNB, Kv3/KCNC, and Kv11/KCNH channels.1 Publication

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.