Peptide Information

General Information of This Peptide
Peptide ID
BTDP003846
Peptide Name
Basic phospholipase A2 ammodytoxin A
Symonym
Phosphatidylcholine 2-acylhydrolase
Species
Vipera ammodytes ammodytes (Western sand viper)
Uniprot Name
PA2BA_VIPAA
Alphafold ID
P00626
3D Structure
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2D Sequence
3D Structure
Source
RSCB PDB: 3G8G
Sequence
MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCC
FVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYN
YIYRNYPDFLCKKESEKC
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Sequence Length
138
Mass (Da)
15531
Signal Sequence
MRTLWIVAVCLIGVEG
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Sequence Removed Signal Peptide
SLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPK
TDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDFLCKKESE
KC
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Disulfide Bond
42-131;44-60;59-111;65-138;66-104;73-97;91-102
PDB ID
3G8G
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Lepidosauria
Order: Squamata
Family: Viperidae
Genus: Vipera
Species: Vipera ammodytes
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    CaM IC50
6 nM
 . . [1- 17]
 Target Info    activated protein C (APC) IC50
20 nM
 . . [1- 17]
References
Ref 1 Cloning and nucleotide sequence of a cDNA encoding ammodytoxin A, the most toxic phospholipase A2 from the venom of long-nosed viper (Vipera ammodytes). Toxicon. 1991;29(2):269-73. doi: 10.1016/0041-0101(91)90112-5.
Ref 2 Ammodytoxin A, a highly lethal phospholipase A2 from Vipera ammodytes ammodytes venom. Biochim Biophys Acta. 1985 Apr 29;828(3):306-12. doi: 10.1016/0167-4838(85)90312-7.
Ref 3 An aromatic, but not a basic, residue is involved in the toxicity of group-II phospholipase A2 neurotoxins. Biochem J. 1999 Jul 1;341 ( Pt 1)(Pt 1):139-45.
Ref 4 The amino acid region 115-119 of ammodytoxins plays an important role in neurotoxicity. Biochem Biophys Res Commun. 2000 Oct 5;276(3):1229-34. doi: 10.1006/bbrc.2000.3605.
Ref 5 Charge reversal of ammodytoxin A, a phospholipase A2-toxin, does not abolish its neurotoxicity. Biochem J. 2000 Dec 1;352 Pt 2(Pt 2):251-5. doi: 10.1042/0264-6021:3520251.
Ref 6 The facilitatory actions of snake venom phospholipase A(2) neurotoxins at the neuromuscular junction are not mediated through voltage-gated K(+) channels. Toxicon. 2001 Dec;39(12):1871-82. doi: 10.1016/s0041-0101(01)00170-2.
Ref 7 Phenylalanine-24 in the N-terminal region of ammodytoxins is important for both enzymic activity and presynaptic toxicity. Biochem J. 2002 Apr 15;363(Pt 2):353-8. doi: 10.1042/0264-6021:3630353.
Ref 8 The C-terminal region of ammodytoxins is important but not sufficient for neurotoxicity. Eur J Biochem. 2002 Dec;269(23):5759-64. doi: 10.1046/j.1432-1033.2002.03301.x.
Ref 9 Identification of a novel binding site for calmodulin in ammodytoxin A, a neurotoxic group IIA phospholipase A2. Eur J Biochem. 2003 Jul;270(14):3018-25. doi: 10.1046/j.1432-1033.2003.03679.x.
Ref 10 Ammodytoxin, a neurotoxic secreted phospholipase A(2), can act in the cytosol of the nerve cell. Biochem Biophys Res Commun. 2004 Nov 19;324(3):981-5. doi: 10.1016/j.bbrc.2004.09.144.
Ref 11 Basic amino acid residues in the beta-structure region contribute, but not critically, to presynaptic neurotoxicity of ammodytoxin A. Biochim Biophys Acta. 2004 Nov 1;1702(2):217-25. doi: 10.1016/j.bbapap.2004.09.002.
Ref 12 Ammodytoxins, potent presynaptic neurotoxins, are also highly efficient phospholipase A2 enzymes. Biochemistry. 2005 Sep 20;44(37):12535-45. doi: 10.1021/bi051024r.
Ref 13 The C-terminal and beta-wing regions of ammodytoxin A, a neurotoxic phospholipase A2 from Vipera ammodytes ammodytes, are critical for binding to factor Xa and for anticoagulant effect. Biochimie. 2006 Jan;88(1):69-76. doi: 10.1016/j.biochi.2005.06.015. Epub 2005 Jul 7.
Ref 14 Binding to the high-affinity M-type receptor for secreted phospholipases A(2) is not obligatory for the presynaptic neurotoxicity of ammodytoxin A. Biochimie. 2006 Oct;88(10):1425-33. doi: 10.1016/j.biochi.2006.06.008. Epub 2006 Jun 21.
Ref 15 A presynaptically toxic secreted phospholipase A2 is internalized into motoneuron-like cells where it is rapidly translocated into the cytosol. Biochim Biophys Acta. 2008 Jun;1783(6):1129-39. doi: 10.1016/j.bbamcr.2008.01.011. Epub 2008 Jan 26.
Ref 16 Ammodytoxin: a window into understanding presynaptic toxicity of secreted phospholipases A(2) and more. Toxicon. 2011 Sep 1;58(3):219-29. doi: 10.1016/j.toxicon.2011.06.009. Epub 2011 Jun 26.
Ref 17 Comparative structural studies of two natural isoforms of ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which differ in neurotoxicity and anticoagulant activity. J Struct Biol. 2010 Mar;169(3):360-9. doi: 10.1016/j.jsb.2009.10.010. Epub 2009 Oct 24.
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