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P30288

- TOG4A_AGEAP

UniProt

P30288 - TOG4A_AGEAP

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Protein

Omega-agatoxin-Aa4a

Gene
N/A
Organism
Agelenopsis aperta (North American funnel-web spider) (Agelenopsis gertschi)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

GO - Molecular functioni

  1. sodium channel inhibitor activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel impairing toxin, Ion channel impairing toxin, Neurotoxin, Presynaptic neurotoxin, Toxin, Voltage-gated calcium channel impairing toxin

Protein family/group databases

TCDBi8.B.6.1.1. the ca(2+) channel-targeting spider toxin (cst) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-agatoxin-Aa4a
Short name:
Omega-AGTX-Aa4a
Alternative name(s):
Omega-agatoxin IVA
Short name:
Omega-Aga-IVA
Omega-agatoxin-4A
OrganismiAgelenopsis aperta (North American funnel-web spider) (Agelenopsis gertschi)
Taxonomic identifieri6908 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeEntelegynaeAgelenidaeAgelenopsis

Organism-specific databases

ArachnoServeriAS000182. omega-agatoxin-Aa4a.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. other organism presynaptic membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4848Omega-agatoxin-Aa4aPRO_0000087610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi4 ↔ 20
Disulfide bondi12 ↔ 25
Disulfide bondi19 ↔ 36
Disulfide bondi27 ↔ 34

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

1
48
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi7 – 115
Beta strandi20 – 223
Beta strandi24 – 263
Beta strandi29 – 335
Beta strandi35 – 384
Turni41 – 444
Turni45 – 473

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IVANMR-A1-48[»]
1OAVNMR-A1-48[»]
1OAWNMR-A1-48[»]
ProteinModelPortaliP30288.
SMRiP30288. Positions 1-48.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30288.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Knottin

Family and domain databases

Gene3Di4.10.40.10. 1 hit.
InterProiIPR008017. Atracotoxin_delta.
IPR004169. Spidertoxin.
[Graphical view]
PfamiPF02819. Toxin_9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30288-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40
KKKCIAKDYG RCKWGGTPCC RGRGCICSIM GTNCECKPRL IMEGLGLA
Length:48
Mass (Da):5,210
Last modified:April 1, 1993 - v1
Checksum:i945054B55EAE81FD
GO

Sequence databases

PIRiS20256.

Cross-referencesi

Sequence databases

PIRi S20256.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IVA NMR - A 1-48 [» ]
1OAV NMR - A 1-48 [» ]
1OAW NMR - A 1-48 [» ]
ProteinModelPortali P30288.
SMRi P30288. Positions 1-48.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 8.B.6.1.1. the ca(2+) channel-targeting spider toxin (cst) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

ArachnoServeri AS000182. omega-agatoxin-Aa4a.

Miscellaneous databases

EvolutionaryTracei P30288.

Family and domain databases

Gene3Di 4.10.40.10. 1 hit.
InterProi IPR008017. Atracotoxin_delta.
IPR004169. Spidertoxin.
[Graphical view ]
Pfami PF02819. Toxin_9. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiTOG4A_AGEAP
AccessioniPrimary (citable) accession number: P30288
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 1, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3