P55902 (SIX1_BUTOC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Alpha-insect toxin BotIT1
Organism	Buthus occitanus tunetanus (Common European scorpion)
Taxonomic identifier	6871 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Chelicerata › Arachnida › Scorpiones › Buthida › Buthoidea › Buthidae › Buthus › Buthus occitanus

Protein attributes

Sequence length	65 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. This contractive toxin is highly toxic to insects and barely toxic to mammals.
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Toxic dose	LD50 is 50 µg/kg in mouse by intracerebroventricular injection and 600 ng/g in Blatella germanica. Ref.1
Sequence similarities	Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.
Mass spectrometry	Molecular mass is 7334.93±0.23 Da from positions 1 - 65. Determined by ESI. Ref.1

Ontologies

Keywords
Cellular component	Secreted
Molecular function	Ion channel impairing toxin Neurotoxin Sodium channel inhibitor Toxin
PTM	Disulfide bond
Technical term	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	ATP-activated nucleotide receptor activity Inferred from mutant phenotype PubMed 18048695. Source: BHF-UCL 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
	Chain	1 – 65	65	Alpha-insect toxin BotIT1		PRO_0000066713
Amino acid modifications
	Disulfide bond	12 ↔ 63		By similarity
	Disulfide bond	16 ↔ 36		By similarity
	Disulfide bond	22 ↔ 46		By similarity
	Disulfide bond	26 ↔ 48		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55902 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 93A1371D877D7123	FASTA	65	7,343
	10 20 30 40 50 60 VRDAYIAQNY NCVYFCMKDD YCNDLCTKNG ASSGYCQWAG KYGNACWCYA LPDNVPIRIP GKCHS

References

[1]

"Purification, structure and activity of three insect toxins from Buthus occitanus tunetanus venom." Borchani L., Stankiewicz M., Kopeyan C., Mansuelle P., Kharrat R., Cestele S., Karoui H., Rochat H., Pelhate M., el Ayeb M. Toxicon 35:365-382(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, LETHAL DOSE, MASS SPECTROMETRY. Tissue: Venom.

Cross-references

3D structure databases
ProteinModelPortal	P55902.
SMR	P55902. Positions 1-64.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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	Search...

Entry information

Entry name

SIX1_BUTOC

Accession

Primary (citable) accession number: P55902

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Animal Toxin Annotation Program