Beta-mammal/insect toxin Ts1 precursor - Tityus serrulatus (Brazilian scorpion)

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P15226 (SCX7_TITSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	Recommended name: Beta-mammal/insect toxin Ts1 Alternative name(s): PT-Mice-Ins-beta NaTx6.1 Tityustoxin VII Short name=Ts VII Short name=TsTX-VII Toxin II-11 Toxin III-10 Toxin T2-IV Toxin gamma Ts7
Organism	Tityus serrulatus (Brazilian scorpion)
Taxonomic identifier	6887 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Tityus

Protein attributes

Sequence length	84 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. This toxin is active against both mammals and insects.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Toxic dose	LD₅₀ is 0.6 ng, intracerebroventricular.
Sequence similarities	Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Ion channel impairing toxin Neurotoxin Sodium channel inhibitor Toxin
PTM	Amidation Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	defense response Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sodium channel inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

20

Ref.3 Ref.4 Ref.5 Ref.6

Chain

61

Beta-mammal/insect toxin Ts1

PRO_0000035305

Amino acid modifications

Modified residue

1

Cysteine amide

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

1

.

.

.

.

.

.

.

.

.

84

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P15226 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 430F3FCA74823E77
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84

9,382

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

        70         80 
ACYCYGLPNW VKVWDRATNK CGKK

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.
[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]. Tissue: Venom.
[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]	"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.
[8]	"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.
[9]	"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.
[10]	"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.

PIR

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B7D	X-ray	1.73	A	21-81	[»]
1NPI	X-ray	1.16	A	21-81	[»]

ProteinModelPortal

SMR

P15226. Positions 21-81.

ModBase

Protocols and materials databases

StructuralBiologyKnowledgebase

Family and domain databases

Gene3D

3.30.30.10. 1 hit.

InterPro

IPR003614. Scorpion_toxin-like.
IPR018218. Scorpion_toxinL.
IPR002061. Scorpion_toxinL/defesin.
[Graphical view]

Pfam

PF00537. Toxin_3. 1 hit.
[Graphical view]

PRINTS

PR00285. SCORPNTOXIN.

SMART

SM00505. Knot1. 1 hit.
[Graphical view]

SUPFAM

SSF57095. SSF57095. 1 hit.

ProtoNet

Other

EvolutionaryTrace

Entry information

Entry name

SCX7_TITSE

Accession

Primary (citable) accession number: P15226

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents