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P30288 (TOG4A_AGEAP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Omega-agatoxin-Aa4a

Short name=Omega-AGTX-Aa4a
Alternative name(s):
Omega-agatoxin IVA
Short name=Omega-Aga-IVA
Omega-agatoxin-4A
OrganismAgelenopsis aperta (North American funnel-web spider) (Agelenopsis gertschi)
Taxonomic identifier6908 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeEntelegynaeAgelenidaeAgelenopsis

Protein attributes

Sequence length48 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Omega-agatoxins inhibit neuronal voltage-gated calcium channels. This toxin acts by modifying the gating of the high voltage activated P-type Cav2.1/CACNA1A channel. Is a potent blocker in both insect and mammalian central neurons. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Secreted Ref.1.

Tissue specificity

Expressed by the venom gland. Ref.1

Domain

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

Miscellaneous

This toxin is a diagnostic ligand for P-type channels Ca2.1/CACNA1A in the mammalian brain.

The binding site for this toxin has been localized in part to the extracellular S3-S4 loop in repeat IV of the alpha1 subunit of mammalian Cav2.1/CACNA1A channels, which is proximal to the S4 sensor domain.

Sequence similarities

Belongs to the plectoxin superfamily. Type IV omega-agatoxin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4848Omega-agatoxin-Aa4a
PRO_0000087610

Amino acid modifications

Disulfide bond4 ↔ 20 Ref.2 Ref.8 Ref.9
Disulfide bond12 ↔ 25 Ref.2 Ref.8 Ref.9
Disulfide bond19 ↔ 36 Ref.2 Ref.8 Ref.9
Disulfide bond27 ↔ 34 Ref.2 Ref.8 Ref.9

Secondary structure

................ 48
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30288 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 945054B55EAE81FD

FASTA485,210
        10         20         30         40 
KKKCIAKDYG RCKWGGTPCC RGRGCICSIM GTNCECKPRL IMEGLGLA 

« Hide

References

[1]"P-type calcium channels blocked by the spider toxin omega-Aga-IVA."
Mintz I.M., Venema V.J., Swiderek K.M., Lee T.D., Bean B.P., Adams M.E.
Nature 355:827-829(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOXIN TARGET.
Tissue: Venom.
[2]"Synthesis of omega-agatoxin IVA and its related peptides."
Nishio H., Kumagaye K.Y., Kubo S., Chen Y.N., Momiyama A., Takahashi T., Kimura T., Sakakibara S.
Biochem. Biophys. Res. Commun. 196:1447-1453(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS, FUNCTION, DISULFIDE BONDS.
[3]"Omega AGA toxin IVA blocks high-voltage-activated calcium channel currents in cultured pars intercerebralis neurosecretory cells of adult locusta migratoria."
Bickmeyer U., Rossler W., Wiegand H.
Neurosci. Lett. 181:113-116(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOXIN TARGET.
[4]"Alteration of P-type calcium channel gating by the spider toxin omega-Aga-IVA."
McDonough S.I., Mintz I.M., Bean B.P.
Biophys. J. 72:2117-2128(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Ca2+ currents in central insect neurons: electrophysiological and pharmacological properties."
Wicher D., Penzlin H.
J. Neurophysiol. 77:186-199(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A hot spot for the interaction of gating modifier toxins with voltage-dependent ion channels."
Winterfield J.R., Swartz K.J.
J. Gen. Physiol. 116:637-644(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Discovery and structure of a potent and highly specific blocker of insect calcium channels."
Wang X.-H., Connor M., Wilson D., Wilson H.I., Nicholson G.M., Smith R., Shaw D., Mackay J.P., Alewood P.F., Christie M.J., King G.F.
J. Biol. Chem. 276:40306-40312(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TOXIN TARGET.
[8]"Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers."
Kim J.I., Konishi S., Iwai H., Kohno T., Gouda H., Shimada I., Sato K., Arata Y.
J. Mol. Biol. 250:659-671(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.
[9]"Structure-activity relationships for P-type calcium channel-selective omega-agatoxins."
Reily M.D., Holub K.E., Gray W.R., Norris T.M., Adams M.E.
Nat. Struct. Biol. 1:853-856(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BONDS.

Cross-references

Sequence databases

PIRS20256.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVANMR-A1-48[»]
1OAVNMR-A1-48[»]
1OAWNMR-A1-48[»]
ProteinModelPortalP30288.
SMRP30288. Positions 1-48.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB8.B.6.1.1. the ca(2+) channel-targeting spider toxin (cst) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

ArachnoServerAS000182. omega-agatoxin-Aa4a.

Family and domain databases

Gene3D4.10.40.10. 1 hit.
InterProIPR008017. Atracotoxin_delta.
IPR004169. Spidertoxin.
[Graphical view]
PfamPF02819. Toxin_9. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP30288.

Entry information

Entry nameTOG4A_AGEAP
AccessionPrimary (citable) accession number: P30288
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 77 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references