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P0C1Z0

- TXFA2_DENAN

UniProt

P0C1Z0 - TXFA2_DENAN

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
  1. 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

    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

    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-2PRO_0000253031Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi3 ↔ 22
    Disulfide bondi17 ↔ 39
    Disulfide bondi41 ↔ 52
    Disulfide bondi53 ↔ 59

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.

    Structurei

    Secondary structure

    1
    61
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    « Hide

    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: October 1, 2014
    This is version 38 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