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6  structures 12  species 0  interactions 29  sequences 1  architecture

Family: Toxin_9 (PF02819)

Summary: Spider toxin

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This is the Wikipedia entry entitled "Spider toxin". More...

Spider toxin Edit Wikipedia article

Spider toxin
1IVA.pdb.png
Solution structure of omega-agatoxin-Aa4a from Agelenopsis aperta.[1]
Identifiers
Symbol Toxin_9
Pfam PF02819
Pfam clan CL0083
InterPro IPR004169
SCOP 1oav
SUPERFAMILY 1oav
OPM superfamily 120
OPM protein 1agg
Delta Atracotoxin
Identifiers
Symbol Atracotoxin
Pfam PF05353
InterPro IPR008017
SCOP 1qdp
SUPERFAMILY 1qdp
OPM protein 1vtx
Spider toxin CSTX family
Identifiers
Symbol Toxin_35
Pfam PF10530
InterPro IPR011142
PROSITE PDOC60029
Spider potassium channel inhibitory toxin
Identifiers
Symbol Toxin_12
Pfam PF07740
Pfam clan CL0083
InterPro IPR011696
SCOP 1d1h
SUPERFAMILY 1d1h
OPM protein 1qk6

Spider toxins are a family of proteins produced by spiders which function as neurotoxins. The mechanism of many spider toxins is through blockage of calcium channels.

A remotely related group of atracotoxins operate by opening sodium channels. Delta atracotoxin produces potentially fatal neurotoxic symptoms in primates by slowing the inactivation of voltage-gated sodium channels.[2] The structure of atracotoxin comprises a core beta region containing a triple-stranded a thumb-like extension protruding from the beta region and a C-terminal helix. The beta region contains a cystine knot motif, a feature seen in other neurotoxic polypeptides[2] and other spider toxins, of the CSTX family.

Spider potassium channel inhibitory toxins is another group of spider toxins. A representative of this group is hanatoxin, a 35 amino acid peptide toxin which was isolated from Chilean rose tarantula (Grammostola rosea, syn. G. spatulata) venom. It inhibits the drk1 voltage-gated potassium channel by altering the energetics of gating.[3] See also Huwentoxin-1 IPR013140.

See also[edit]

References[edit]

  1. ^ PDB 1IVA; Reily MD, Holub KE, Gray WR, Norris TM, Adams ME (December 1994). "Structure-activity relationships for P-type calcium channel-selective omega-agatoxins". Nat. Struct. Biol. 1 (12): 853–6. doi:10.1038/nsb1294-853. PMID 7773772. 
  2. ^ a b Mackay JP, King GF, Fletcher JI, Chapman BE, Howden ME (1997). "The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel". Structure 5 (11): 1525–1535. doi:10.1016/S0969-2126(97)00301-8. PMID 9384567. 
  3. ^ Shimada I, Sato K, Takahashi H, Kim JI, Min HJ, Swartz KJ (2000). "Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins". J. Mol. Biol. 297 (3): 771–780. doi:10.1006/jmbi.2000.3609. PMID 10731427. 

Further reading[edit]

  • Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, Shimada I, Sato K, Arata Y (July 1995). "Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers". J. Mol. Biol. 250 (5): 659–71. doi:10.1006/jmbi.1995.0406. PMID 7623383. 

This article incorporates text from the public domain Pfam and InterPro IPR008017


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Spider toxin Provide feedback

This family of spider neurotoxins are thought to be calcium ion channel inhibitors.

Literature references

  1. Kim JI, Konishi S, Iwai H, Kohno T, Gouda H, Shimada I, Sato K, Arata Y; , J Mol Biol 1995;250:659-671.: Three-dimensional solution structure of the calcium channel antagonist omega-agatoxin IVA: consensus molecular folding of calcium channel blockers. PUBMED:7623383 EPMC:7623383


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004169

This family of spider neurotoxins are thought to be calcium ion channel inhibitors.

Gene Ontology

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Domain organisation

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Alignments

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(6)
Full
(29)
Representative proteomes NCBI
(49)
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(1)
RP35
(2)
RP55
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RP75
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  Seed
(6)
Full
(29)
Representative proteomes NCBI
(49)
Meta
(0)
RP15
(1)
RP35
(2)
RP55
(5)
RP75
(5)
Alignment:
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  Seed
(6)
Full
(29)
Representative proteomes NCBI
(49)
Meta
(0)
RP15
(1)
RP35
(2)
RP55
(5)
RP75
(5)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

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Curation and family details

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Curation View help on the curation process

Seed source: Homstrad
Previous IDs: spidertoxin;
Type: Family
Author: Griffiths-Jones SR
Number in seed: 6
Number in full: 29
Average length of the domain: 39.90 aa
Average identity of full alignment: 38 %
Average coverage of the sequence by the domain: 58.82 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.5 21.7
Noise cut-off 21.0 21.0
Model length: 44
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toxin_9 domain has been found. There are 6 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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