Peptide record

TPDB27787

Neurotoxin Toxicity standard
34 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.
TPDB27787
Neurotoxin Toxicity
Toxicity and safety peptides
NTxPred2 Peptipedia pep-lab ToxinPred 3.0
standard
No
A 34-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from NTxPred2, Peptipedia, pep-lab, and other sources, with an available 3D structural model.
Sequence
TCRYLFGGCKTTADCCKHLACRSDGKYCAWDGTF
Physicochemical Analysis
C161H242N46O48S6
NEQIMPV
C
3782.33
8.02
6
3
10
+2
0.91
-0.279
31.76
Mammalian: 7.2 hour Yeast: >20 hour E.coli: >10 hour
8855
234.11
13
Residue Composition
number
3
A
2
R
0
N
3
D
6
C
0
E
0
Q
4
G
1
H
0
I
2
L
3
K
0
M
2
F
0
P
1
S
4
T
1
W
2
Y
0
V
Amino Acid Distribution
A: 3 R: 2 N: 0 D: 3 C: 6 E: 0 Q: 0 G: 4 H: 1 I: 0 L: 2 K: 3 M: 0 F: 2 P: 0 S: 1 T: 4 W: 1 Y: 2 V: 0
Chemical Descriptors
34
C161H242N46O48S6
3782.33
8.02
+2
0.91
-0.279
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Reversibly inhibits potassium currents in oocytes expressing Kv2.1/KCNB1 channels (Kd=2.7 uM) (PubMed:15051809). Acts by shifting activation of the channel to more depolarized voltages. The toxin may bind to the S3b-S4 helices of the voltage sensor paddle. One, two, three or four toxin molecules may bind the Kv2.1/KCNB1 channel. It shows low to moderate affinity for lipid bilayers (PubMed:29703751). It partitions into the bilayer membrane, where it stabilizes at the water/membrane interface (PubMed:17071657, PubMed:20643084). {ECO:0000269|PubMed:10504388, ECO:0000269|PubMed:14744131, ECO:0000269|PubMed:15051809, ECO:0000269|PubMed:17071657, ECO:0000269|PubMed:20643084, ECO:0000269|PubMed:29703751}.

Target

voltage-gated potassium channel (Kv)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Stromatopelma calceatum griseipes (Feather leg baboon tarantula) (Scodra griseipes)
Neurotoxin Ion channel impairing toxin Potassium channel impairing toxin Voltage-gated potassium channel impairing toxin
Reversibly inhibits potassium currents in oocytes expressing Kv2.1/KCNB1 channels (Kd=2.7 uM) (PubMed:15051809). Acts by shifting activation of the channel to more depolarized voltages.
Kappa-theraphotoxin-Scg1a (Kappa-TRTX-Scg1a) (SGTx1) (SGTx) (SgTx-I)
spider
Neurotoxin 10 (Hwtx-1) family, 09 (HaTx) subfamily
Evidence at protein level
3D-structure Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Potassium channel impairing toxin Secreted Toxin Voltage-gated potassium channel impairing toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:10504388}.
Additional Detail Fields 7 fields
3D-structure Direct protein sequencing Disulfide bond 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
Neurotoxin 10 (Hwtx-1) family, 09 (HaTx) subfamily
Kappa-theraphotoxin-Scg1a (Kappa-TRTX-Scg1a) (SGTx1) (SGTx) (SgTx-I)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:10504388}.
spider