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P15226 (SCX1_TITSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismTityus serrulatus (Brazilian scorpion)
Taxonomic identifier6887 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeTityus

Protein attributes

Sequence length84 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 (Ref.8). This toxin is active against both mammals and insects. Ref.8

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is 826 +/- 156 µg/kg by intravenous injection into mice (Ref.7). Ref.7

LD50 is 11 +/- 9 µg/kg by intracistenal injection into mice (Ref.7). Ref.7

LD50 is 0.6 ng, intracerebroventricular. Ref.7

Miscellaneous

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

Sequence similarities

Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.

Caution

The "mutant" Ts1-G was isolated from the venom before the last step maturation (i.e. amidation) thanks to a right purification technique (Ref.10). It is indicated here as a mutant, since it does not correspond to the mature toxin.

Mass spectrometry

Molecular mass is 6879.4 Da from positions 21 - 81. Determined by MALDI. Ref.10

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIon channel impairing toxin
Neurotoxin
Toxin
Voltage-gated sodium channel impairing toxin
   PTMAmidation
Disulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionion channel inhibitor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.3 Ref.4 Ref.5 Ref.6
Chain21 – 8161Beta-mammal/insect toxin Ts1
PRO_0000035305

Amino acid modifications

Modified residue811Cysteine amide
Disulfide bond31 ↔ 81 Ref.13
Disulfide bond35 ↔ 57 Ref.13
Disulfide bond43 ↔ 62 Ref.13
Disulfide bond47 ↔ 64 Ref.13

Experimental info

Mutagenesis811C → CG: Decrease of affinity of this non amidated toxin (Ts1-G) for sodium channel. Ref.10

Secondary structure

......... 84
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15226 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 430F3FCA74823E77

FASTA849,382
        10         20         30         40         50         60 
MKGMILFISC LLLIGIVVEC KEGYLMDHEG CKLSCFIRPS GYCGRECGIK KGSSGYCAWP 

        70         80 
ACYCYGLPNW VKVWDRATNK CGKK 

« Hide

References

[1]"Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main beta-neurotoxin from the venom of the South American scorpion Tityus serrulatus."
Martin-Eauclaire M.-F., Ceard B., Ribeiro A.M., Diniz C.R., Rochat H., Bougis P.E.
FEBS Lett. 302:220-222(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"The genomic region encoding toxin gamma from the scorpion Tityus serrulatus contains an intron."
Becerril B., Corona M., Mejia M.C., Martin B.M., Lucas S., Bolivar F., Possani L.D.
FEBS Lett. 335:6-8(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Amino acid sequence of toxin VII, a beta-toxin from the venom of the scorpion Tityus serrulatus."
Bechis G., Sampieri F., Yuan P.-M., Brando T., Martin M.-F., Diniz C.R., Rochat H.
Biochem. Biophys. Res. Commun. 122:1146-1153(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-81.
Tissue: Venom.
[4]"Discharge effect on pancreatic exocrine secretion produced by toxins purified from Tityus serrulatus scorpion venom."
Possani L.D., Martin B.M., Fletcher M.D., Fletcher P.L. Jr.
J. Biol. Chem. 266:3178-3185(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-81.
Tissue: Venom.
[5]"Purification and chemical characterization of the major toxins from the venom of the Brazilian scorpion Titus serrulatus Lutz and Mello."
Possani L.D., Martin B.M., Mochca-Morales J., Svendsen I.
Carlsberg Res. Commun. 46:195-205(1981)
Cited for: PROTEIN SEQUENCE OF 21-62.
Tissue: Venom.
[6]"Further characterization of toxins T1IV (TsTX-III) and T2IV from Tityus serrulatus scorpion venom."
Sampaio S.V., Arantes E.C., Prado W.A., Riccioppo Neto F., Giglio J.R.
Toxicon 29:663-672(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-46.
Tissue: Venom.
[7]"A simplified procedure for the fractionation of Tityus serrulatus venom: isolation and partial characterization of TsTX-IV, a new neurotoxin."
Arantes E.C., Prado W.A., Sampaio S.V., Giglio J.R.
Toxicon 27:907-916(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: AMINO ACID COMPOSITION, LETHAL DOSE.
Tissue: Venom.
[8]"Tityus serrulatus venom and toxins Ts1, Ts2 and Ts6 induce macrophage activation and production of immune mediators."
Zoccal K.F., Bitencourt C.S., Secatto A., Sorgi C.A., Bordon K.C., Sampaio S.V., Arantes E.C., Faccioli L.H.
Toxicon 57:1101-1108(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Role of lysine and tryptophan residues in the biological activity of toxin VII (Ts gamma) from the scorpion Tityus serrulatus."
Hassani O., Mansuelle P., Cestele S., Bourdeaux M., Rochat H., Sampieri F.
Eur. J. Biochem. 260:76-86(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPORTANCE OF LYS-12; TRP-39 AND TRP-54.
[10]"Functional and structural study comparing the C-terminal amidated beta-neurotoxin Ts1 with its isoform Ts1-G isolated from Tityus serrulatus venom."
Coelho V.A., Cremonez C.M., Anjolette F.A., Aguiar J.F., Varanda W.A., Arantes E.C.
Toxicon 83C:15-21(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-81, MASS SPECTROMETRY.
[11]"Tityus serrulatus scorpion venom and toxins: an overview."
Cologna C.T., Marcussi S., Giglio J.R., Soares A.M., Arantes E.C.
Protein Pept. Lett. 16:920-932(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[12]"Crystal structure of neurotoxin Ts1 from Tityus serrulatus provides insights into the specificity and toxicity of scorpion toxins."
Polikarpov I., Junior M.S.M., Marangoni S., Toyama M.H., Teplyakov A.
J. Mol. Biol. 290:175-184(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 21-81.
[13]"Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with Na+ channels."
Pinheiro C.B., Marangoni S., Toyama M.H., Polikarpov I.
Acta Crystallogr. D 59:405-415(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) OF 21-81, DISULFIDE BONDS.
[14]"Identification and phylogenetic analysis of Tityus pachyurus and Tityus obscurus novel putative Na+-channel scorpion toxins."
Guerrero-Vargas J.A., Mourao C.B., Quintero-Hernandez V., Possani L.D., Schwartz E.F.
PLoS ONE 7:E30478-E30478(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66256 mRNA. Translation: CAA46982.1.
S66941 Genomic DNA. Translation: AAB29128.1.
PIRS21158.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7DX-ray1.73A21-81[»]
1NPIX-ray1.16A21-81[»]
ProteinModelPortalP15226.
SMRP15226. Positions 21-81.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.30.10. 1 hit.
InterProIPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defensin.
[Graphical view]
PfamPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSPR00285. SCORPNTOXIN.
SMARTSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP15226.

Entry information

Entry nameSCX1_TITSE
AccessionPrimary (citable) accession number: P15226
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references