Back to search

Peptide record

TPDB34683

Neurotoxin Toxicity standard
86 amino acids
Basic Information
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber.
TPDB34683
Neurotoxin Toxicity
Toxicity and safety peptides
Peptipedia
standard
No
A 86-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
MKVSVLITLAVLGVMFVWASAAELEERGSDQRDSPAWLKSMERIFQSGERECRKMFGGCSVDSDCCAHLGCKPTLKYCAWDGTFGK
Physicochemical Analysis
C415H652N114O123S10
N
GS
9527.03
6.78
12
11
34
-0
14.14
-0.073
69.19
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
18365
192.77
20
Residue Composition
number
7
A
5
R
0
N
5
D
6
C
6
E
2
Q
8
G
1
H
2
I
7
L
6
K
4
M
4
F
2
P
8
S
3
T
3
W
1
Y
6
V
Amino Acid Distribution
A: 7 R: 5 N: 0 D: 5 C: 6 E: 6 Q: 2 G: 8 H: 1 I: 2 L: 7 K: 6 M: 4 F: 4 P: 2 S: 8 T: 3 W: 3 Y: 1 V: 6
Chemical Descriptors
86
C415H652N114O123S10
9527.03
6.78
-0
14.14
-0.073
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed-state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}.

Target

voltage-gated sodium channel (Nav) voltage-gated potassium channel (Kv)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys jingzhao)
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294).
Kappa-theraphotoxin-Cg1a 1 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11) (JZTX-11) (Jingzhaotoxin-XI) (JZTX-XI) (Peptide F4-13.64)
spider
Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily
Evidence at protein level
3D-structure Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:17176080, ECO:0000305|PubMed:17476710}.
Additional Detail Fields 7 fields
3D-structure Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin Voltage-gated sodium channel impairing toxin
Evidence at protein level
Neurotoxin 10 (Hwtx-1) family, 28 (Jztx-11) subfamily
Kappa-theraphotoxin-Cg1a 1 (Kappa-TRTX-Cg1a) (Jingzhaotoxin-11) (JZTX-11) (Jingzhaotoxin-XI) (JZTX-XI) (Peptide F4-13.64)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:17176080, ECO:0000305|PubMed:17476710}.
spider