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Protein

Beta-mammal/insect toxin Ts1

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

Functioni

Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. In addition, it stimulates the release of NO, IL-6 and TNF-alpha in J774.1 cells (PubMed:21549737). This toxin is active against both mammals and insects.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mammal/insect toxin Ts1
Alternative name(s):
PT-Mice-Ins-beta NaTx6.1
Tityustoxin VII
Short name:
Ts VII
Short name:
Ts7
Short name:
TsTX-VII
Toxin II-11
Toxin III-10
Toxin T2-IV
Toxin gamma
TsTX-I
OrganismiTityus serrulatus (Brazilian scorpion)
Taxonomic identifieri6887 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 826 +/- 156 µg/kg by intravenous injection into mice.1 Publication
LD50 is 11 +/- 9 µg/kg by intracistenal injection into mice.1 Publication
LD50 is 0.6 ng, intracerebroventricular.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi81C → CG: Decrease of affinity of this non amidated toxin (Ts1-G) for sodium channel. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 205 PublicationsAdd BLAST20
ChainiPRO_000003530521 – 81Beta-mammal/insect toxin Ts1Add BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 811 Publication
Disulfide bondi35 ↔ 571 Publication
Disulfide bondi43 ↔ 621 Publication
Disulfide bondi47 ↔ 641 Publication
Modified residuei81Cysteine amide1

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi42 – 49Combined sources8
Beta strandi53 – 58Combined sources6
Beta strandi61 – 66Combined sources6
Turni76 – 78Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B7DX-ray1.73A21-81[»]
1NPIX-ray1.16A21-81[»]
ProteinModelPortaliP15226.
SMRiP15226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15226.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamiPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSiPR00285. SCORPNTOXIN.
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGMILFISC LLLIGIVVEC KEGYLMDHEG CKLSCFIRPS GYCGRECGIK
60 70 80
KGSSGYCAWP ACYCYGLPNW VKVWDRATNK CGKK
Length:84
Mass (Da):9,382
Last modified:July 1, 1993 - v2
Checksum:i430F3FCA74823E77
GO

Mass spectrometryi

Molecular mass is 6879.4 Da from positions 21 - 81. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66256 mRNA. Translation: CAA46982.1.
S66941 Genomic DNA. Translation: AAB29128.1.
PIRiS21158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66256 mRNA. Translation: CAA46982.1.
S66941 Genomic DNA. Translation: AAB29128.1.
PIRiS21158.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B7DX-ray1.73A21-81[»]
1NPIX-ray1.16A21-81[»]
ProteinModelPortaliP15226.
SMRiP15226.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP15226.

Family and domain databases

Gene3Di3.30.30.10. 1 hit.
InterProiIPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamiPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSiPR00285. SCORPNTOXIN.
SMARTiSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMiSSF57095. SSF57095. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSCX1_TITSE
AccessioniPrimary (citable) accession number: P15226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Miscellaneous

Is the main neurotoxin of the venom of T.serrulatus.

Caution

The "mutant" Ts1-G was isolated from the venom before the last step maturation (i.e. amidation) thanks to a right purification technique (PubMed:24560880). It is indicated here as a mutant, since it does not correspond to the mature toxin.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.