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Reviewed, UniProtKB/Swiss-Prot P56852 (TXHN1_GRARO)

Last modified November 25, 2008. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Hanatoxin-1
      Short name=HaTx1
OrganismGrammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
Taxonomic identifier432528 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataArachnidaAraneaeMygalomorphaeTheraphosidaeGrammostola

Protein attributes

Sequence length35 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Inhibits Kv2.1 (KCNB1) and Kv4.2 (KCND2) voltage-gated potassium channels. Acts as a gating modifier by shifting channel openings to more depolarized voltages and acts via the occupancy of multiple binding sites on the channel. The toxin binding sites are situated on the S3-S4 extracellular linker of the channel. At least two hanatoxin molecules can occupy the Kv2.1 channel, and maybe more (three or four). Can also inhibit calcium channels (Cav2.1 / CACNA1A). Need to partition into the membrane in order to bind to the channel.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Domain

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Miscellaneous

Blockers of Kv2.1 potassium channels, such as hanatoxin, may be a useful approach to the design of novel therapeutic agents for the treatment of type 2 diabetes.

Sequence similarities

Belongs to the huwentoxin-1 superfamily. Hanatoxin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 3535Hanatoxin-1
PRO_0000045012

Regions

Region4 – 63Involved in active face By similarity

Sites

Site31May be involved in interaction with voltage sensor By similarity
Site221May be involved in interaction with voltage sensor By similarity
Site301Involved in active face By similarity

Amino acid modifications

Disulfide bond2 ↔ 16
Disulfide bond9 ↔ 21
Disulfide bond15 ↔ 28

Secondary structure

......... 35
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56852-1 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: D401AC8A9B14DB12

FASTA354,121
        10         20         30 
ECRYLFGGCK TTSDCCKHLG CKFRDKYCAW DFTFS 

« Hide

References

[1]"An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula."
Swartz K.J., MacKinnon R.
Neuron 15:941-949(1995) [PubMed: 7576642] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites."
Swartz K.J., MacKinnon R.
Neuron 18:665-673(1997) [PubMed: 9136774] [Abstract]
Cited for: FUNCTION.
[3]"Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels."
Swartz K.J., MacKinnon R.
Neuron 18:675-682(1997) [PubMed: 9136775] [Abstract]
Cited for: FUNCTION.
[4]"Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels."
Li-Smerin Y., Swartz K.J.
Proc. Natl. Acad. Sci. U.S.A. 95:8585-8589(1998) [PubMed: 9671721] [Abstract]
Cited for: FUNCTION.
[5]"Voltage-sensor activation with a tarantula toxin as cargo."
Phillips L.R., Milescu M., Li-Smerin Y., Mindell J.A., Kim J.I., Swartz K.J.
Nature 436:857-860(2005) [PubMed: 16094370] [Abstract]
Cited for: MEMBRANE-PARTITIONING.
[6]"Gating modifier peptides as probes of pancreatic beta-cell physiology."
Herrington J.
Toxicon 49:231-238(2007) [PubMed: 17101164] [Abstract]
Cited for: FUNCTION ON PANCREATIC BETA-CELLS.
[7]"Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins."
Takahashi H., Kim J.I., Min H.J., Sato K., Swartz K.J., Shimada I.
J. Mol. Biol. 297:771-780(2000) [PubMed: 10731427] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Cross-references

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1D1HNMR-A1-35[»]
ModBaseSearch...

Family and domain databases

InterProIPR011696. Toxin_12.
[Graphical view]
PfamPF07740. Toxin_12. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTXHN1_GRARO
AccessionPrimary (citable) accession number: P56852
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 25, 2008
This is version 46 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

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