TPDB

3D PDB MODEL

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TPDB ID TPDB35915

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 27-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

NLLQFGFMIRCANKRRRPVWPYEESGC

FASTA

>TPDB35915|Neurotoxin;Toxicity|length=27
NLLQFGFMIRCANKRRRPVWPYEESGC

Formula C145H224N44O37S3

Absent Amino Acids DHT

Common Amino Acids R

Mass 3271.83

PI 9.79

Basic Residues 5

Acidic Residues 2

Hydrophobic Residues 10

Net Charge +3

Boman Index 3.45

Hydrophobicity -0.585

Aliphatic Index 57.78

Half Life

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

Extinction Coefficient Cystines 7115

Absorbance 280nm 217.46

Polar Residues 7

number

1

A

4

R

2

N

0

D

2

C

2

E

1

Q

2

G

0

H

1

I

2

L

1

K

1

M

2

F

2

P

1

S

0

T

1

W

1

Y

1

V

Amino Acid Distribution

A: 1 R: 4 N: 2 D: 0 C: 2 E: 2 Q: 1 G: 2 H: 0 I: 1 L: 2 K: 1 M: 1 F: 2 P: 2 S: 1 T: 0 W: 1 Y: 1 V: 1

Length

27

Formula

C145H224N44O37S3

Mass

3271.83

PI

9.79

Net Charge

+3

Boman Index

3.45

Hydrophobicity

-0.585

Evidence 1 Activity

Activity

Detail Source Activity Neurotoxin

Function Text

FUNCTION: Heterotrimer: presynaptic neurotoxin. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl. Causes a fade in tetanic contractions. Displays a triphasic mode of action with depression, enhancement and blockade of neurotransmission. Does not display myotoxic activity such as changes in baseline muscle tension or inhibition of directly stimulated muscle twitches. All subunits are necessary for maximum toxicity. {ECO:0000269|PubMed:20361942}. FUNCTION: Monomer: Snake venom phospholipase A2 (PLA2) alpha chain that has enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20361942}.

Target

Target or Channel proton-gated sodium channel / ASIC

Source & Reference

Database Source NA

Source UniProtKB/Swiss-Prot Tox-Prot

Other

Organism Source Acanthophis antarcticus (Common death adder)

Neurotoxin Type Neurotoxin Presynaptic neurotoxin

Mechanism

Heterotrimer: presynaptic neurotoxin. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl.

Protein Name

Phospholipase A2 P-elapitoxin-Aa1a alpha chain (P-EPTX-Aa1a alpha chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)

Venom Taxon Group snake

Protein Family Phospholipase A2 family, Group I 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. {ECO:0000269|PubMed:20361942}.

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

Protein_Name

Phospholipase A2 P-elapitoxin-Aa1a alpha chain (P-EPTX-Aa1a alpha chain) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)

Tissue_Specificity

TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:20361942}.

Venom_Taxon_Group

snake