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Peptide record

TPDB71951

Neurotoxin standard
121 amino acids
Basic Information
3D PDB MODEL
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TPDB71951
Neurotoxin
Toxicity and safety peptides
NTxPred2
standard
No
A 121-aa standard natural neurotoxin peptide sequence curated from NTxPred2, with an available 3D structural model.
Sequence
MHLSHLLAWALLLTLLSLRAEAKPPSPQPQVPRSPGDEASEAVAANGGGKKGDKEPKGDRPRLLRELRLDTRSRGSRGVWTRLLHDHPNPRKYKPANKKGLSKGCFGLKLDRIGSTSGLGC
Physicochemical Analysis
C575H951N183O164S3
L
13148.18
10.89
27
11
37
+12
32.55
-0.724
79.09
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
12615
95.94
22
Residue Composition
number
9
A
12
R
3
N
6
D
2
C
5
E
2
Q
14
G
4
H
1
I
19
L
11
K
1
M
1
F
11
P
10
S
4
T
2
W
1
Y
3
V
Amino Acid Distribution
A: 9 R: 12 N: 3 D: 6 C: 2 E: 5 Q: 2 G: 14 H: 4 I: 1 L: 19 K: 11 M: 1 F: 1 P: 11 S: 10 T: 4 W: 2 Y: 1 V: 3
Chemical Descriptors
121
C575H951N183O164S3
13148.18
10.89
+12
32.55
-0.724
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Venom component with vasorelaxant activity. In vitro stimulates the production of cGMP in rat aortic smooth muscle cells and histamine release from rat peritoneal mast cells. Induces relaxation of isolated rat uterus. Induces local edema following subplantar injection into rat hind paw. Forms voltage-dependent cation channels which are weakly selective for potassium relative to sodium, and whose conductance decreases with increasing dehydration energy of the monovalent cation. The activity of the fast cation channels is calcium dependent and is characterized by short bursts of current separated by long periods of inactivation. {ECO:0000269|PubMed:10381585, ECO:0000269|PubMed:10409107, ECO:0000269|PubMed:7597719, ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}. FUNCTION: Venom peptide 1 induces slow and continuous calcium influx in IMR-32 human neuroblastoma cells. Venom peptide 4 weakly induces calcium influx in IMR-32 human neuroblastoma cells while venom peptide 2 was not observed to induce calcium influx.

Target

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

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Ornithorhynchus anatinus (Duckbill platypus)
Neurotoxin
Venom component with vasorelaxant activity. In vitro stimulates the production of cGMP in rat aortic smooth muscle cells and histamine release from rat peritoneal mast cells.
C-type natriuretic peptide (CNP) [Cleaved into: Venom peptide 1 Venom peptide 2 Venom peptide 3 Venom peptide 4 Venom peptide 5 Venom peptide 6 Venom peptide 7 Venom peptide 8 Venom peptide 9 Venom peptide 10 Venom peptide 11 C-type natriuretic peptide 39 (ovCNP-39)]
other
Natriuretic peptide family
Evidence at protein level
D-amino acid Direct protein sequencing Hypotensive agent Ion channel Ion transport Neurotoxin Potassium Potassium channel Potassium transport Reference proteome Secreted Signal Sodium Sodium channel Sodium transport Toxin Transport Vasoactive Vasodilator
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:7597719, ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}.
Additional Detail Fields 7 fields
D-amino acid Direct protein sequencing Hypotensive agent Ion channel Ion transport Neurotoxin Potassium Potassium channel Potassium transport Reference proteome Secreted Signal Sodium Sodium channel Sodium transport Toxin Transport Vasoactive Vasodilator
Neurotoxin
Evidence at protein level
Natriuretic peptide family
C-type natriuretic peptide (CNP) [Cleaved into: Venom peptide 1 Venom peptide 2 Venom peptide 3 Venom peptide 4 Venom peptide 5 Venom peptide 6 Venom peptide 7 Venom peptide 8 Venom peptide 9 Venom peptide 10 Venom peptide 11 C-type natriuretic peptide 39 (ovCNP-39)]
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:7597719, ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}.
other