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Protein

Imperatoxin-A

Gene
N/A
Organism
Pandinus imperator (Emperor scorpion)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Affects the activity of ryanodine-sensitive calcium-release channels RyR1, RyR2 and RyR3. At lower concentrations the toxin increases full openings of the RyRs, and at higher concentrations it inhibits full openings and induce openings to subconductance levels and reduces the number of full conductance openings. The different actions may be attributed to the toxins binding at different sites on the RyRs, with binding at a high-affinity site mediating the increase in full openings and the induction of subconductance states evoked upon binding to a lower-affinity site.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei6Important for RYR1 activation1
Sitei7Essential for RYR1 activation1
Sitei11Important for RYR1 activation1
Sitei30Important for RYR1 activation1
Sitei31Essential for RYR1 activation1
Sitei33Essential for RYR1 activation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalcium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Ryanodine-sensitive calcium-release channel impairing toxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Imperatoxin-A
Short name:
IpTxa
Alternative name(s):
Imperatoxin activator
OrganismiPandinus imperator (Emperor scorpion)
Taxonomic identifieri55084 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesIuridaScorpionoideaScorpionidaeScorpioninaePandinus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1G → A: 1.18-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi2D → A: 2.33-fold increase of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi4L → A: 1.93-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi5P → A: 1.43-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi6H → A: 20.72-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi7L → A: 97.51-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi8K → A: 4.60-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi9R → A: 25.62-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi11K → A: 6.83-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi13D → A: 3.08-fold increase of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi14N → A: 1.14-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi15D → A: 2.73-fold increase of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi18G → A: 1.16-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi19K → A: 4.96-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi20K → A: 16.91-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi22K → A: 69.92-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi23R → A: 418.48-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi24R → A: Complete inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi25G → A: 23.96-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi26T → A: 11.52-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi27N → A: 20.09-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi29E → A: 2.35-fold increase of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi30K → A: 21.69-fold inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi31R → A: Complete inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1
Mutagenesisi33R → A: Complete inhibition of specific [3H]ryanodine binding to RYR1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_00000449491 – 33Imperatoxin-AAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi3 ↔ 171 Publication
Disulfide bondi10 ↔ 211 Publication
Disulfide bondi16 ↔ 321 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 15Combined sources3
Beta strandi16 – 19Combined sources4
Beta strandi24 – 32Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IE6NMR-A1-33[»]
ProteinModelPortaliP59868.
SMRiP59868.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59868.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 9Important for RYR1 activation2
Regioni19 – 20Important for RYR1 activation2
Regioni22 – 24Essential for RYR1 activation3
Regioni25 – 27Important for RYR1 activation3

Domaini

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

Sequence similaritiesi

Belongs to the scorpion calcine family.Curated

Keywords - Domaini

Knottin

Family and domain databases

InterProiView protein in InterPro
IPR012632. Scorpion_calcine.
PfamiView protein in Pfam
PF08099. Toxin_27. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD874489. Scorpion_calcine. 1 hit.
PROSITEiView protein in PROSITE
PS60028. SCORPION_CALCINE. 1 hit.

Sequencei

Sequence statusi: Complete.

P59868-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
GDCLPHLKRC KADNDCCGKK CKRRGTNAEK RCR
Length:33
Mass (Da):3,764
Last modified:September 26, 2003 - v1
Checksum:iD0DF8EFFFE294537
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IE6NMR-A1-33[»]
ProteinModelPortaliP59868.
SMRiP59868.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP59868.

Family and domain databases

InterProiView protein in InterPro
IPR012632. Scorpion_calcine.
PfamiView protein in Pfam
PF08099. Toxin_27. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD874489. Scorpion_calcine. 1 hit.
PROSITEiView protein in PROSITE
PS60028. SCORPION_CALCINE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIPTXA_PANIM
AccessioniPrimary (citable) accession number: P59868
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: November 2, 2016
This is version 59 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. 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.