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P0C1Z0

- TXFA2_DENAN

UniProt

P0C1Z0 - TXFA2_DENAN

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Protein
Fasciculin-2
Gene
N/A
Organism
Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei27 – 271May interact with AChE
Sitei30 – 301May interact with AChE
Sitei31 – 311May interact with AChE

GO - Biological processi

  1. modification of morphology or physiology of other organism Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Toxin

Names & Taxonomyi

Protein namesi
Recommended 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
OrganismiDendroaspis angusticeps (Eastern green mamba) (Naja angusticeps)
Taxonomic identifieri8618 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeDendroaspis

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is >20 mg/kg by intravenous injection.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 92TT → AA: 18-fold increase in inhibition potency.
Mutagenesisi11 – 111R → Q: 6-fold increase in inhibition potency. 1 Publication
Mutagenesisi24 – 241R → T: 13-fold decrease in inhibition potency. 1 Publication
Mutagenesisi25 – 251K → L: No significant difference in inhibition potency. 1 Publication
Mutagenesisi27 – 271R → W: 49-fold decrease in inhibition potency. 1 Publication
Mutagenesisi28 – 281R → D: No significant difference in inhibition potency. 1 Publication
Mutagenesisi29 – 291H → D: 73-fold increase in inhibition potency. 1 Publication
Mutagenesisi30 – 301Missing: 192-fold decrease in inhibition potency. 1 Publication
Mutagenesisi31 – 311P → R: 625-fold decrease in inhibition potency. 1 Publication
Mutagenesisi32 – 321K → G: 3-fold decrease in inhibition potency. 1 Publication
Mutagenesisi33 – 331M → A: 8-fold decrease in inhibition potency. 1 Publication
Mutagenesisi34 – 352VL → AA: No significant difference in inhibition potency.
Mutagenesisi45 – 451D → K: No significant difference in inhibition potency. 1 Publication
Mutagenesisi51 – 511K → S: No significant difference in inhibition potency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6161Fasciculin-2
PRO_0000253031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi3 ↔ 223 Publications
Disulfide bondi17 ↔ 393 Publications
Disulfide bondi41 ↔ 523 Publications
Disulfide bondi53 ↔ 593 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Beta strandi8 – 103
Beta strandi13 – 164
Beta strandi22 – 3110
Beta strandi34 – 407
Beta strandi46 – 538
Turni57 – 604

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0C1Z0.
SMRiP0C1Z0. Positions 1-61.

Miscellaneous databases

EvolutionaryTraceiP0C1Z0.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

InterProiIPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view]
PfamiPF00087. Toxin_1. 1 hit.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C1Z0-1 [UniParc]FASTAAdd to Basket

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TMCYSHTTTS RAILTNCGEN SCYRKSRRHP PKMVLGRGCG CPPGDDNLEV   50
KCCTSPDKCN Y 61
Length:61
Mass (Da):6,758
Last modified:October 17, 2006 - v1
Checksum:i50A38EF3633C383F
GO

Sequence databases

PIRiA01674. T4EP1A.

Cross-referencesi

Sequence databases

PIRi A01674. T4EP1A.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B41 X-ray 2.76 B 1-61 [» ]
1F8U X-ray 2.90 B 1-61 [» ]
1FSC X-ray 2.00 A 1-61 [» ]
1FSS X-ray 3.00 B 1-61 [» ]
1KU6 X-ray 2.50 B 1-61 [» ]
1MAH X-ray 3.20 F 1-61 [» ]
2X8B X-ray 2.95 B 1-61 [» ]
4BDT X-ray 3.10 B 1-61 [» ]
4EY8 X-ray 2.60 B 1-61 [» ]
ProteinModelPortali P0C1Z0.
SMRi P0C1Z0. Positions 1-61.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG006553.

Miscellaneous databases

EvolutionaryTracei P0C1Z0.

Family and domain databases

InterProi IPR003571. Snake_toxin.
IPR018354. Snake_toxin_BS.
[Graphical view ]
Pfami PF00087. Toxin_1. 1 hit.
[Graphical view ]
PROSITEi PS00272. SNAKE_TOXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiTXFA2_DENAN
AccessioniPrimary (citable) accession number: P0C1Z0
Secondary accession number(s): P01403
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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