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Reviewed, UniProtKB/Swiss-Prot Q9NII5 (KAX16_MESMA)

Last modified June 16, 2009. Version 59. 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 1.6
Alternative name(s):
    BmTX2
    Neurotoxin TX2
OrganismMesobuthus martensii (Manchurian scorpion) (Buthus martensii)
Taxonomic identifier34649 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaScorpionesButhidaButhoideaButhidaeMesobuthus

Protein attributes

Sequence length58 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Potent blocker of both large-conductance calcium-activated potassium channels (BKCa channels) and voltage-gated potassium channels (Kv1.3/KCNA3).

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 1 subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionIonic channel inhibitor
Neurotoxin
Potassium channel inhibitor
Toxin
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   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 – 2121 Ref.3
Chain22 – 5837Potassium channel toxin alpha-KTx 1.6
PRO_0000035318

Amino acid modifications

Modified residue221Pyrrolidone carboxylic acid
Disulfide bond28 ↔ 49 Ref.4
Disulfide bond34 ↔ 54 Ref.4
Disulfide bond38 ↔ 56 Ref.4

Secondary structure

.......... 58
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NII5-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: F19AA7351B9708B8

FASTA586,507
        10         20         30         40         50 
MKISFLLLLA IVICSIGWTE AQFTNVSCSA SSQCWPVCKK LFGTYRGKCM NSKCRCYS 

« Hide

References

[1]"Genomic organization of three novel toxins from the scorpion Buthus martensi Karsch that are active on potassium channels."
Dai L., Wu J.-J., Gu Y.-H., Lan Z.-D., Ling M.-H., Chi C.-W.
Biochem. J. 346:805-809(2000) [PubMed: 10698710] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning and genomic organization of a K(+) channel toxin from the Chinese scorpion Buthus martensii Karsch."
Zeng X.-C., Zhu Z.-H., Li W.-X., Zhu S.-Y., Peng F., Mao X., Liu H.
Toxicon 39:407-410(2001) [PubMed: 10978761] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels."
Romi-Lebrun R., Lebrun B., Martin-Eauclaire M.-F., Ishiguro M., Escoubas P., Wu F.Q., Hisada M., Pongs O., Nakajima T.
Biochemistry 36:13473-13482(1997) [PubMed: 9354615] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-58, SYNTHESIS, CHARACTERIZATION.
[4]"Solution structure of two new toxins from the venom of the Chinese scorpion Buthus martensi Karsch blockers of potassium channels."
Blanc E., Romi-Lebrun R., Bornet O., Nakajima T., Darbon H.
Biochemistry 37:12412-12418(1998) [PubMed: 9730813] [Abstract]
Cited for: STRUCTURE BY NMR OF 22-58, DISULFIDE BONDS.

Cross-references

Sequence databases

AF208300 Genomic DNA. Translation: AAF63972.1.
AF151537 mRNA. Translation: AAQ13576.1.
AF247058 Genomic DNA. Translation: AAK73518.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2BMTNMR-A23-58[»]
ModBaseSearch...

Family and domain databases

InterProIPR001947. Scorpion_toxinS.
[Graphical view]
PfamPF00451. Toxin_2. 1 hit.
[Graphical view]
PRINTSPR00286. CHARYBDTOXIN.
ProDomPD003586. Scorpion_toxinS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01138. SCORP_SHORT_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAX16_MESMA
AccessionPrimary (citable) accession number: Q9NII5
Secondary accession number(s): P58489
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 59 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