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P15223 (SCX1_CENNO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Toxin Cn1
Alternative name(s):
Toxin II.14
Short name=Toxin 1
OrganismCentruroides noxius (Mexican scorpion)
Taxonomic identifier6878 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeCentruroides

Protein attributes

Sequence length86 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 By similarity.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIon channel impairing toxin
Neurotoxin
Sodium channel inhibitor
Toxin
   PTMAmidation
Disulfide bond
   Technical termDirect 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_functionsodium channel inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.2
Chain20 – 8465Toxin Cn1
PRO_0000035279

Amino acid modifications

Modified residue841Serine amide Ref.1
Disulfide bond30 ↔ 83 By similarity
Disulfide bond34 ↔ 59 By similarity
Disulfide bond43 ↔ 64 By similarity
Disulfide bond47 ↔ 66 By similarity

Experimental info

Sequence conflict791P → T AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P15223 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: AB8C1EA742F17222

FASTA869,586
        10         20         30         40         50         60 
MNSLLMITAC FVLIGTVWAK DGYLVDAKGC KKNCYKLGKN DYCNRECRMK HRGGSYGYCY 

        70         80 
GFGCYCEGLS DSTPTWPLPN KTCSGK 

« Hide

References

[1]"Cloning and characterization of the cDNAs encoding Na+ channel-specific toxins 1 and 2 of the scorpion Centruroides noxius Hoffmann."
Vazquez A., Tapia J.V., Eliason W.K., Martin B.M., Lebreton F., Delepierre M., Possani L.D., Becerril B.
Toxicon 33:1161-1170(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT SER-84.
Tissue: Venom gland.
[2]"Scorpion toxins from Centruroides noxius and Tityus serrulatus. Primary structures and sequence comparison by metric analysis."
Possani L.D., Martin B.M., Svendsen I., Rode G.S., Erickson B.W.
Biochem. J. 229:739-750(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-84.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S81093 mRNA. Translation: AAB36085.2.
PIRS32789.

3D structure databases

ProteinModelPortalP15223.
SMRP15223. Positions 20-83.
ModBaseSearch...

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/defesin.
[Graphical view]
PfamPF00537. Toxin_3. 1 hit.
[Graphical view]
PRINTSPR00285. SCORPNTOXIN.
SMARTSM00505. Knot1. 1 hit.
[Graphical view]
SUPFAMSSF57095. SSF57095. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSCX1_CENNO
AccessionPrimary (citable) accession number: P15223
Secondary accession number(s): Q26460
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: December 15, 1998
Last modified: May 1, 2013
This is version 80 of the entry and version 3 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