Back to search

Peptide record

TPDB29256

Neurotoxin Toxicity standard
32 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.
TPDB29256
Neurotoxin Toxicity
Toxicity and safety peptides
NTxPred2 Peptipedia ToxinPred 3.0
standard
No
A 32-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
CRTEGMSCEENQQCCWRSCCRGECEAPCRFGP
Physicochemical Analysis
C141H220N48O49S9
DHILKYV
C
3660.13
4.85
4
5
4
-1
10.95
-0.847
3.12
Mammalian: 1.2 hour Yeast: >20 hour E.coli: >10 hour
6000
163.93
14
Residue Composition
number
1
A
4
R
1
N
0
D
8
C
5
E
2
Q
3
G
0
H
0
I
0
L
0
K
1
M
1
F
2
P
2
S
1
T
1
W
0
Y
0
V
Amino Acid Distribution
A: 1 R: 4 N: 1 D: 0 C: 8 E: 5 Q: 2 G: 3 H: 0 I: 0 L: 0 K: 0 M: 1 F: 1 P: 2 S: 2 T: 1 W: 1 Y: 0 V: 0
Chemical Descriptors
32
C141H220N48O49S9
3660.13
4.85
-1
10.95
-0.847
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). Irreversibly inhibits Kv1 channels with a pore-blocking mechanism (PubMed:40324600). Causes slow but complete inhibition of Kv1.2/KCNA2 and Kv1.6/KCNA6 (PubMed:20403399, PubMed:40324600). Tested at 5 uM, the recombinant peptide (without gamma-carboxyglutamic acid (Gla) and C-terminal amidated Pro) also inhibits Kv1.1/KCNA1 (19%) and Kv1.4/KCNA4 (53%) (PubMed:40324600). In vivo, produces stiffening of body, limbs and tail when injected intracranially into mice (PubMed:17166627). {ECO:0000269|PubMed:17166627, ECO:0000269|PubMed:20403399, ECO:0000269|PubMed:40324600}.

Target

voltage-gated potassium channel (Kv)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Conus spurius (Alphabet cone)
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin
Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). Irreversibly inhibits Kv1 channels with a pore-blocking mechanism (PubMed:40324600).
Kappa-conotoxin SrXIA (Kappa-SrXIA) (I2-superfamily conotoxin sr11a)
cone snail
Conotoxin I2 superfamily
Evidence at protein level
3D-structure Amidation Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Toxin Voltage-gated potassium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|PubMed:17166627}.
Additional Detail Fields 7 fields
3D-structure Amidation Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Toxin Voltage-gated potassium channel impairing toxin
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin
Evidence at protein level
Conotoxin I2 superfamily
Kappa-conotoxin SrXIA (Kappa-SrXIA) (I2-superfamily conotoxin sr11a)
TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|PubMed:17166627}.
cone snail