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Peptide record

TPDB34624

Neurotoxin Toxicity standard
85 amino acids
Basic Information
3D PDB MODEL
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TPDB34624
Neurotoxin Toxicity
Toxicity and safety peptides
Peptipedia
standard
No
A 85-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from Peptipedia, with an available 3D structural model.
Sequence
MKTSVFAAILGLALFAVLCSGSELQEKDLKETLLSAIMETALEAQPEERECRYLFGGCKTTSDCCKHLGCKFRDKYCAWDFTFSK
Physicochemical Analysis
C421H663N107O126S9
N
L
9528.08
5.69
12
12
34
-1
15.02
-0.015
75.88
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
8855
92.94
23
Residue Composition
number
8
A
3
R
0
N
4
D
7
C
8
E
2
Q
5
G
1
H
2
I
11
L
8
K
2
M
6
F
1
P
6
S
6
T
1
W
2
Y
2
V
Amino Acid Distribution
A: 8 R: 3 N: 0 D: 4 C: 7 E: 8 Q: 2 G: 5 H: 1 I: 2 L: 11 K: 8 M: 2 F: 6 P: 1 S: 6 T: 6 W: 1 Y: 2 V: 2
Chemical Descriptors
85
C421H663N107O126S9
9528.08
5.69
-1
15.02
-0.015
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Inhibits Kv2.1/KCNB1 and Kv4.2/KCND2 voltage-gated potassium channels. Acts as a gating modifier by shifting channel openings to more depolarized voltages and acts via the occupancy of multiple binding sites on the channel. The toxin binding sites are situated on the S3-S4 extracellular linker of the channel. At least two hanatoxin molecules can occupy the Kv2.1/KCNB1 channel, and maybe more (three or four). Can also inhibit calcium channels (Cav2.1/CACNA1A). Needs to partition into the membrane in order to bind to the channel. {ECO:0000269|PubMed:17101164, ECO:0000269|PubMed:9136774, ECO:0000269|PubMed:9136775, ECO:0000269|PubMed:9671721}.

Target

voltage-gated potassium channel (Kv) voltage-gated calcium channel (Cav)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata)
Neurotoxin Calcium channel impairing toxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated calcium channel impairing toxin Voltage-gated potassium channel impairing toxin
Inhibits Kv2.1/KCNB1 and Kv4.2/KCND2 voltage-gated potassium channels. Acts as a gating modifier by shifting channel openings to more depolarized voltages and acts via the occupancy of multiple binding sites on the channel.
Kappa-theraphotoxin-Gr1a (Kappa-TRTX-Gr1a) (Hanatoxin-1) (HaTx1)
spider
Neurotoxin 10 (Hwtx-1) family, 09 (HaTx) subfamily
Evidence at protein level
3D-structure Calcium channel impairing toxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated calcium channel impairing toxin Voltage-gated potassium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:7576642}.
Additional Detail Fields 7 fields
3D-structure Calcium channel impairing toxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Signal Toxin Voltage-gated calcium channel impairing toxin Voltage-gated potassium channel impairing toxin
Neurotoxin Calcium channel impairing toxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated calcium channel impairing toxin Voltage-gated potassium channel impairing toxin
Evidence at protein level
Neurotoxin 10 (Hwtx-1) family, 09 (HaTx) subfamily
Kappa-theraphotoxin-Gr1a (Kappa-TRTX-Gr1a) (Hanatoxin-1) (HaTx1)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:7576642}.
spider