Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C1Z0 (TXFA2_DENAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 24, 2013. Version 37. 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:
Fasciculin-2

Short name=Fas-2
Short name=Fas2
Alternative name(s):
Acetylcholinesterase toxin F-VII
Fasciculin-II
Short name=FAS-II
Toxin TA1
OrganismDendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
Taxonomic identifier8618 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Protein attributes

Sequence length61 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This three-finger toxin selectively binds and inhibits with a 1:1 stoichiometry the mammalian and electric fish acetylcholinesterase (AChE) at picomolar concentrations. It is highly specific for the peripheral site on acetylcholinesterase. It has been called fasciculin since after injection into mice it cause severe, generalized and long-lasting (5-7 hours) fasciculations. The whole venom has anticoagulant activity, and the various components seem to act synergistically.

Subcellular location

Secreted.

Tissue specificity

Expressed by the venom gland.

Toxic dose

LD50 is >20 mg/kg by intravenous injection.

Sequence similarities

Belongs to the snake three-finger toxin family. Acn-esterase inhibitor subfamily.

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionToxin
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processmodification of morphology or physiology of other organism

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6161Fasciculin-2
PRO_0000253031

Sites

Site271May interact with AChE
Site301May interact with AChE
Site311May interact with AChE

Amino acid modifications

Disulfide bond3 ↔ 22 Ref.5 Ref.6 Ref.7
Disulfide bond17 ↔ 39 Ref.5 Ref.6 Ref.7
Disulfide bond41 ↔ 52 Ref.5 Ref.6 Ref.7
Disulfide bond53 ↔ 59 Ref.5 Ref.6 Ref.7

Experimental info

Mutagenesis8 – 92TT → AA: 18-fold increase in inhibition potency.
Mutagenesis111R → Q: 6-fold increase in inhibition potency. Ref.3
Mutagenesis241R → T: 13-fold decrease in inhibition potency. Ref.3
Mutagenesis251K → L: No significant difference in inhibition potency. Ref.3
Mutagenesis271R → W: 49-fold decrease in inhibition potency. Ref.3
Mutagenesis281R → D: No significant difference in inhibition potency. Ref.3
Mutagenesis291H → D: 73-fold increase in inhibition potency. Ref.3
Mutagenesis301Missing: 192-fold decrease in inhibition potency. Ref.3
Mutagenesis311P → R: 625-fold decrease in inhibition potency. Ref.3
Mutagenesis321K → G: 3-fold decrease in inhibition potency. Ref.3
Mutagenesis331M → A: 8-fold decrease in inhibition potency. Ref.3
Mutagenesis34 – 352VL → AA: No significant difference in inhibition potency.
Mutagenesis451D → K: No significant difference in inhibition potency. Ref.3
Mutagenesis511K → S: No significant difference in inhibition potency. Ref.3

Secondary structure

............... 61
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C1Z0 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 50A38EF3633C383F

FASTA616,758
        10         20         30         40         50         60 
TMCYSHTTTS RAILTNCGEN SCYRKSRRHP PKMVLGRGCG CPPGDDNLEV KCCTSPDKCN 


Y 

« Hide

References

[1]"Snake venom toxins. The purification and amino acid sequence of toxin F-VII from Dendroaspis angusticeps venom."
Viljoen C.C., Botes D.P.
J. Biol. Chem. 248:4915-4919(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Venom.
[2]"Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps."
Karlsson E., Mbugua P.M., Rodriguez-Ithurralde D.
J. Physiol. (Paris) 79:232-240(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Expression and activity of mutants of fasciculin, a peptidic acetylcholinesterase inhibitor from mamba venom."
Marchot P., Prowse C.N., Kanter J., Camp S., Ackermann E.J., Radic Z., Bougis P.E., Taylor P.
J. Biol. Chem. 272:3502-3510(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS, MUTAGENESIS OF 8-THR-THR-9; ARG-11; ARG-24; LYS-25; ARG-27; ARG-28; HIS-29; PRO-30; PRO-31; LYS-32; MET-33; 34-VAL-LEU-35; ASP-45 AND LYS-51.
[4]"Crystals of fasciculin 2 from green mamba snake venom. Preparation and preliminary X-ray analysis."
le Du M.H., Marchot P., Bougis P.E., Fontecilla-Camps J.-C.
J. Biol. Chem. 264:21401-21402(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[5]"Structure of fasciculin 2 from green mamba snake venom: evidence for unusual loop flexibility."
le Du M.-H., Housset D., Marchot P., Bougis P.E., Navaza J., Fontecilla-Camps J.-C.
Acta Crystallogr. D 52:87-92(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DISULFIDE BONDS.
[6]"Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target."
Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.
Structure 3:1355-1366(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH ACHE, DISULFIDE BONDS.
[7]"Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex."
Bourne Y., Taylor P., Marchot P.
Cell 83:503-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH ACHE, DISULFIDE BONDS.
[8]"Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II."
Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I., Sussman J.L.
Acta Crystallogr. D 56:1385-1394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS).
[9]"Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site."
Bourne Y., Taylor P., Radic Z., Marchot P.
EMBO J. 22:1-12(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRT4EP1A. A01674.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B41X-ray2.76B1-61[»]
1F8UX-ray2.90B1-61[»]
1FSCX-ray2.00A1-61[»]
1FSSX-ray3.00B1-61[»]
1KU6X-ray2.50B1-61[»]
1MAHX-ray3.20F1-61[»]
2X8BX-ray2.95B1-61[»]
4BDTX-ray3.10B1-61[»]
4EY8X-ray2.60B1-61[»]
ProteinModelPortalP0C1Z0.
SMRP0C1Z0. Positions 1-61.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006553.

Family and domain databases

InterProIPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view]
PfamPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C1Z0.

Entry information

Entry nameTXFA2_DENAN
AccessionPrimary (citable) accession number: P0C1Z0
Secondary accession number(s): P01403
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: July 24, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references