Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mu-agatoxin-Aa1c

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

Functioni

Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insects. Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Names & Taxonomyi

Protein namesi
Recommended name:
Mu-agatoxin-Aa1c
Short name:
Mu-AGTX-Aa1c
Alternative name(s):
Mu-agatoxin III
Mu-agatoxin-3
OrganismiAgelenopsis aperta (North American funnel-web spider) (Agelenopsis gertschi)
Taxonomic identifieri6908 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAraneaeAraneomorphaeEntelegynaeAgelenidaeAgelenopsis

Organism-specific databases

ArachnoServeriAS000379. mu-agatoxin-Aa1c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

Lethal dose is 28 +-12 mg/kg into third stadium larvae of M.sexta.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 3838Mu-agatoxin-Aa1cPRO_0000044955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 19By similarity
Disulfide bondi10 ↔ 24By similarity
Disulfide bondi18 ↔ 34By similarity
Disulfide bondi26 ↔ 32By similarity
Modified residuei38 – 381Serine amide

Keywords - PTMi

Amidation, Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

3D structure databases

ProteinModelPortaliP60178.
SMRiP60178. Positions 3-38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the beta/delta-agatoxin family.Curated

Keywords - Domaini

Knottin

Family and domain databases

InterProiIPR016328. Curtatoxin.
IPR009243. Toxin_7.
[Graphical view]
PIRSFiPIRSF001882. Curtatoxin. 1 hit.
PROSITEiPS60015. MU_AGATOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30 
ADCVGDGQRC ADWAGPYCCS GYYCSCRSMP YCRCRSDS
Length:38
Mass (Da):4,197
Last modified:December 15, 2003 - v1
Checksum:i6031DFF4DB386AD0
GO

Sequence databases

PIRiC32038.

Cross-referencesi

Sequence databases

PIRiC32038.

3D structure databases

ProteinModelPortaliP60178.
SMRiP60178. Positions 3-38.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ArachnoServeriAS000379. mu-agatoxin-Aa1c.

Family and domain databases

InterProiIPR016328. Curtatoxin.
IPR009243. Toxin_7.
[Graphical view]
PIRSFiPIRSF001882. Curtatoxin. 1 hit.
PROSITEiPS60015. MU_AGATOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification and characterization of two classes of neurotoxins from the funnel web spider, Agelenopsis aperta."
    Skinner W.S., Adams M.E., Quistad G.B., Kataoka H., Cesarin B.J., Enderlin F.E., Schooley D.A.
    J. Biol. Chem. 264:2150-2155(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, LETHAL DOSE.
    Tissue: Venom.
  2. "Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta."
    Adams M.E.
    Toxicon 43:509-525(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiTXMG3_AGEAP
AccessioniPrimary (citable) accession number: P60178
Secondary accession number(s): P11059
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 22, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.