Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30288

- TOG4A_AGEAP

UniProt

P30288 - TOG4A_AGEAP

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
  1. 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

    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

    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

    KKKCIAKDYG RCKWGGTPCC RGRGCICSIM GTNCECKPRL IMEGLGLA     48
    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