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Acetylcholinesterase toxin C (Fasciculin)

 3SEC_DENPO              Reviewed;          61 AA.
P25681;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
05-JUN-2019, entry version 70.
RecName: Full=Acetylcholinesterase toxin C;
AltName: Full=Fasciculin;
Dendroaspis polylepis polylepis (Black mamba).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
NCBI_TaxID=8620;
[1]
PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND LETHAL DOSE.
TISSUE=Venom;
Joubert F.J., Taljaard N.;
"The complete primary structure of toxin C from Dendroaspis polylepis
polylepis (black mamba) venom.";
S. Afr. J. Chem. 31:107-110(1978).
-!- FUNCTION: Inhibits acetylcholinesterase.
{ECO:0000250|UniProtKB:P0C1Z0}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
-!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
-!- TOXIC DOSE: LD(50) is 2.1 +/- 0.2 mg/kg by intravenous injection.
{ECO:0000269|Ref.1}.
-!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-
chain subfamily. Acn-esterase inhibitor sub-subfamily.
{ECO:0000305}.
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SMR; P25681; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
CDD; cd00206; snake_toxin; 1.
InterPro; IPR003571; Snake_3FTx.
InterPro; IPR018354; Snake_toxin_con_site.
PROSITE; PS00272; SNAKE_TOXIN; 1.
1: Evidence at protein level;
Direct protein sequencing; Disulfide bond; Secreted; Toxin.
CHAIN 1 61 Acetylcholinesterase toxin C.
{ECO:0000269|Ref.1}.
/FTId=PRO_0000093656.
DISULFID 3 22 {ECO:0000250|UniProtKB:P0C1Z0}.
DISULFID 17 39 {ECO:0000250|UniProtKB:P0C1Z0}.
DISULFID 41 52 {ECO:0000250|UniProtKB:P0C1Z0}.
DISULFID 53 59 {ECO:0000250|UniProtKB:P0C1Z0}.
SEQUENCE 61 AA; 6817 MW; 66625EF767341F3A CRC64;
TICYSHTTTS RAILKDCGEN SCYRKSRRHP PKMVLGRGCG CPPGDDYLEV KCCTSPDKCN
Y


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[ACHE] Acetylcholinesterase (AChE) (EC 3.1.1.7)
[ache] Acetylcholinesterase (AChE) (EC 3.1.1.7)
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[plc cpa CPE0036] Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)
[Rac1] Ras-related C3 botulinum toxin substrate 1 (EC 3.6.5.2) (p21-Rac1)
[ACHE] Acetylcholinesterase (AChE) (EC 3.1.1.7)
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[Oprm1 Mor Oprm] Mu-type opioid receptor (M-OR-1) (MOR-1)
[TY2B-OR1 YORCTy2-1 POL YOR192C-B O4785] Transposon Ty2-OR1 Gag-Pol polyprotein (TY2A-TY2B) (Transposon Ty2 TYA-TYB polyprotein) [Cleaved into: Capsid protein (CA); Ty2 protease (PR) (EC 3.4.23.-); Integrase (IN); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4)]
[ACHE] Acetylcholinesterase (AChE) (EC 3.1.1.7)
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[Akr1c21] Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3)
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[APN1 YKL114C YKL513] DNA-(apurinic or apyrimidinic site) lyase 1 (EC 4.2.99.18) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1)
[Kmt2c Mll3] Histone-lysine N-methyltransferase 2C (Lysine N-methyltransferase 2C) (EC 2.1.1.43) (Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog)
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[HIR2 YOR038C OR26.31] Protein HIR2 (Histone transcription regulator 2)
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Bibliography :
[19115961] Stabilization of Torpedo californica acetylcholinesterase by reversible inhibitors.
[16856180] Electrostatic contribution to the binding stability of protein-protein complexes.
[15214439] Synthesis and characterization of a chimeric peptide derived from fasciculin that inhibits acetylcholinesterase.
[12522088] Butyrylcholinesterase and acetylcholinesterase activity and quantal transmitter release at normal and acetylcholinesterase knockout mouse neuromuscular junctions.
[11237623] Protein-protein association: investigation of factors influencing association rates by brownian dynamics simulations.
[10849442] Do structural deviations between toxins adopting the same fold reflect functional differences?
[10686100] Stability of a structural scaffold upon activity transfer: X-ray structure of a three fingers chimeric protein.
[8845756] Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
[8547248] Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site.
[8747462] Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.