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Reviewed, UniProtKB/Swiss-Prot Q9U8D2 (KAX82_MESMA)

Last modified November 24, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Potassium channel toxin alpha-KTx 8.2
Alternative name(s):
    Neurotoxin BmP01
    Potassium ion channel blocker P01
OrganismMesobuthus martensii (Manchurian scorpion) (Buthus martensii)
Taxonomic identifier34649 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeMesobuthus

Protein attributes

Sequence length57 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Blocks small conductance calcium-activated potassium channels (KCNN, SK). Low toxicity by intracerebroventricular injection into mice.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Sequence similarities

Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 8 subfamily.

Mass spectrometry

Molecular mass is 3177.47 Da from positions 29 - 57. Determined by MALDI. Ref.3

Molecular mass is 3177 Da from positions 29 - 57. Determined by ESI. Ref.4

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIonic channel inhibitor
Neurotoxin
Potassium channel inhibitor
Toxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpotassium 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 – 2828 Ref.3 Ref.4
Peptide29 – 5729Potassium channel toxin alpha-KTx 8.2 Ref.3
PRO_0000035348

Amino acid modifications

Disulfide bond31 ↔ 47 Ref.4
Disulfide bond34 ↔ 52 Ref.4
Disulfide bond38 ↔ 54 Ref.4

Experimental info

Sequence conflict171V → I in AAF24057. Ref.2
Sequence conflict211T → I in AAF24057. Ref.2

Secondary structure

........... 57
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9U8D2-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4265970F1250B53A

FASTA576,318
        10         20         30         40         50 
MSRLYAIILI ALVFNVVMTI TPDMKVEAAT CEDCPEHCAT QNARAKCDND KCVCEPK 

« Hide

References

[1]"Genomic organization of three neurotoxins active on small conductance Ca2+-activated potassium channels from the scorpion Buthus martensi Karsch."
Wu J.-J., Dai L., Lan Z.-D., Chi C.-W.
FEBS Lett. 452:360-364(1999) [PubMed: 10386622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Venom gland.
[2]"Molecular characterization of a K+ channel blocker from Buthus martensii."
Zhu S.-Y., Zeng X.-C., Li W.-X., Jiang D.-H.
Kexue Tongbao 44:2295-2299(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[3]"Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels."
Romi-Lebrun R., Martin-Eauclaire M.-F., Escoubas P., Wu F.Q., Lebrun B., Hisada M., Nakajima T.
Eur. J. Biochem. 245:457-464(1997) [PubMed: 9151979] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-57, MASS SPECTROMETRY.
[4]"Solution structure of BmP01 from the venom of scorpion Buthus martensii Karsch."
Wu G., Li Y., Wei D., He F., Jiang S., Hu G., Wu H.
Biochem. Biophys. Res. Commun. 276:1148-1154(2000) [PubMed: 11027603] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-38, STRUCTURE BY NMR OF 29-57, DISULFIDE BONDS, MASS SPECTROMETRY.

Cross-references

Sequence databases

AF095781 Genomic DNA. Translation: AAF03045.1.
AF114024 mRNA. Translation: AAF24057.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1WM7NMR-A29-57[»]
ModBaseSearch...

Family and domain databases

InterProIPR008911. Toxin_6.
[Graphical view]
PfamPF05453. Toxin_6. 1 hit.
[Graphical view]
PROSITEPS01138. SCORP_SHORT_TOXIN. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAX82_MESMA
AccessionPrimary (citable) accession number: Q9U8D2
Secondary accession number(s): Q9U522
Entry history
Integrated into UniProtKB/Swiss-Prot: December 19, 2001
Last sequence update: May 1, 2000
Last modified: November 24, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectTox-Prot (Toxin Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Scorpion potassium channel toxins

Nomenclature of scorpion potassium channel toxins and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents