TPDB

3D PDB MODEL

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TPDB ID TPDB35916

Activity

Neurotoxin Toxicity

Activity_category_statistics

Toxicity and safety peptides

Database_Source

NTxPred2 Peptipedia ToxinPred 3.0

Sequence_Type

standard

Has_Modification No

Description A 20-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from NTxPred2, Peptipedia, and ToxinPred 3.0, with an available 3D structural model.

Sequence

NLLQFGYMIRCANGRSRPVW

FASTA

>TPDB35916|Neurotoxin;Toxicity|length=20
NLLQFGYMIRCANGRSRPVW

Formula C106H165N33O26S2

Absent Amino Acids DEHKT

Common Amino Acids R

Mass 2381.80

PI 11.07

Basic Residues 3

Acidic Residues 0

Hydrophobic Residues 9

Net Charge +3

Boman Index -1.47

Hydrophobicity -0.205

Aliphatic Index 78.00

Half Life

Mammalian: 1.4 hour Yeast: 3 min E.coli: >10 hour

Extinction Coefficient Cystines 6990

Absorbance 280nm 293.48

Polar Residues 6

number

1

A

3

R

2

N

0

D

1

C

0

E

1

Q

2

G

0

H

1

I

2

L

0

K

1

M

1

F

1

P

1

S

0

T

1

W

1

Y

1

V

Amino Acid Distribution

A: 1 R: 3 N: 2 D: 0 C: 1 E: 0 Q: 1 G: 2 H: 0 I: 1 L: 2 K: 0 M: 1 F: 1 P: 1 S: 1 T: 0 W: 1 Y: 1 V: 1

Length

20

Formula

C106H165N33O26S2

Mass

2381.80

PI

11.07

Net Charge

+3

Boman Index

-1.47

Hydrophobicity

-0.205

Evidence 1 Activity

Activity

Detail Source Activity Neurotoxin

Function Text

FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. Enzymatic activity is essential for the neurotoxic effects (PubMed:16135698). May act by binding in a calcium-dependent fashion to neurotonal pentraxin-1 (NPTX1) and neurotonal pentraxin-2 (NPTX2), but not to neuronal pentraxin receptor (NPTXR). Also binds to taipoxin-associated calcium binding protein 49 (RCN2), a protein localized in the lumen of endoplasmic reticulum (By similarity). {ECO:0000250, ECO:0000269|PubMed:16135698}. FUNCTION: Monomer (alpha chain): Snake venom phospholipase A2 (PLA2) that possesses a low level of presynaptic activity and the same high enzymatic activity than the heterotrimer. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:16135698}.

Source & Reference

Database Source NA

Source UniProtKB/Swiss-Prot Tox-Prot

Other

Organism Source Oxyuranus scutellatus canni (Papuan taipan)

Neurotoxin Type Neurotoxin Presynaptic neurotoxin

Mechanism

Heterotrimer: Snake venom phospholipase A2 (PLA2) heterotrimer that acts as a potent presynaptic neurotoxin by blocking synaptic transmission and synaptic vesicle recycling. Enzymatic activity is essential for the neurotoxic effects (PubMed:16135698).

Protein Name Basic phospholipase A2 cannitoxin alpha chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)

Venom Taxon Group snake

Protein Family Phospholipase A2 family, Group I subfamily, D49 sub-subfamily

Protein Existence Evidence at protein level

Keywords Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Neurotoxin Presynaptic neurotoxin Secreted Toxin

Tissue Specificity TISSUE SPECIFICITY: Expressed by the venom gland.

Keywords

Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Neurotoxin Presynaptic neurotoxin Secreted Toxin

Neurotoxin_Type

Neurotoxin Presynaptic neurotoxin

Protein_Existence

Evidence at protein level

Protein_Family

Phospholipase A2 family, Group I subfamily, D49 sub-subfamily

Protein_Name

Basic phospholipase A2 cannitoxin alpha chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)

Tissue_Specificity

TISSUE SPECIFICITY: Expressed by the venom gland.

Venom_Taxon_Group

snake