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Peptide record

TPDB34164

Neurotoxin Toxicity standard
83 amino acids
Basic Information
3D PDB MODEL
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TPDB34164
Neurotoxin Toxicity
Toxicity and safety peptides
Peptipedia
standard
No
A 83-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
MKASMFLALAGLVLLFVVGYASGSEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK
Physicochemical Analysis
C408H632N104O117S8
Q
K
9122.61
8.01
13
10
32
+2
14.83
-0.125
66.99
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
10345
113.40
19
Residue Composition
number
6
A
2
R
2
N
3
D
6
C
7
E
0
Q
9
G
1
H
1
I
8
L
10
K
2
M
6
F
3
P
7
S
1
T
1
W
3
Y
5
V
Amino Acid Distribution
A: 6 R: 2 N: 2 D: 3 C: 6 E: 7 Q: 0 G: 9 H: 1 I: 1 L: 8 K: 10 M: 2 F: 6 P: 3 S: 7 T: 1 W: 1 Y: 3 V: 5
Chemical Descriptors
83
C408H632N104O117S8
9122.61
8.01
+2
14.83
-0.125
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}.

Target

voltage-gated sodium channel (Nav)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum)
Neurotoxin Presynaptic neurotoxin Ion channel impairing toxin Voltage-gated sodium channel impairing toxin
Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics.
Hainantoxin-III 12 (HnTx-III.12) (Hainantoxin-3.12) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
spider
Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily
Evidence at protein level
Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Presynaptic neurotoxin Secreted Signal Toxin Voltage-gated sodium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:14512091, ECO:0000305|PubMed:23703613}.
Additional Detail Fields 7 fields
Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Presynaptic neurotoxin Secreted Signal Toxin Voltage-gated sodium channel impairing toxin
Neurotoxin Presynaptic neurotoxin Ion channel impairing toxin Voltage-gated sodium channel impairing toxin
Evidence at protein level
Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily
Hainantoxin-III 12 (HnTx-III.12) (Hainantoxin-3.12) (Mu-theraphotoxin-Hhn2a) (Mu-TRTX-Hhn2a) (Peptide F7-18.76)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:14512091, ECO:0000305|PubMed:23703613}.
spider