Back to search

Peptide record

TPDB27877

Neurotoxin Toxicity standard
49 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.
TPDB27877
Neurotoxin Toxicity
Toxicity and safety peptides
NTxPred2 pep-lab Peptipedia
standard
No
A 49-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from NTxPred2, pep-lab, and Peptipedia, with an available 3D structural model.
Sequence
GVSCLCDSDGPSVRGNTLSGTLWLYPSGCPSGWHNCKAHGPTIGWCCKQ
Physicochemical Analysis
C220H332N64O67S6
EMF
G
5137.80
7.65
5
2
12
+1
1.16
-0.241
53.67
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
18365
357.45
19
Residue Composition
number
1
A
1
R
2
N
2
D
6
C
0
E
1
Q
8
G
2
H
1
I
4
L
2
K
0
M
0
F
4
P
6
S
3
T
3
W
1
Y
2
V
Amino Acid Distribution
A: 1 R: 1 N: 2 D: 2 C: 6 E: 0 Q: 1 G: 8 H: 2 I: 1 L: 4 K: 2 M: 0 F: 0 P: 4 S: 6 T: 3 W: 3 Y: 1 V: 2
Chemical Descriptors
49
C220H332N64O67S6
5137.80
7.65
+1
1.16
-0.241
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. This toxin retains the greatest capacity to discriminate between the cardiac (Nav1.5/SCN5A) and neuronal sodium channels (2.5 nM versus 120 nM, when electrophysiologically tested and 14 nM versus 400 nM, when tested by ion flux), whereas its paralog Anthopleurin-B has the highest affinity of all anemone toxins for the mammalian sodium channel (PubMed:13806, PubMed:17092528, PubMed:7612595). Its ability to differentiate between cardiac and skeletal channels appears to be associated with domain 4 of the channel (PubMed:9306007). This toxin does not slow or inhibit closed-state inactivation of cardiac sodium channels, but selectively modifies inactivation from the open-state (PubMed:8576699). It does not display phospholipid-binding activities, suggesting that the domain IV S3-S4 linker is located at the extracellular surface and not buried in the phospholipid bilayer (By similarity). {ECO:0000250|UniProtKB:P01531, ECO:0000269|PubMed:13806, ECO:0000269|PubMed:17092528, ECO:0000269|PubMed:21099342, ECO:0000269|PubMed:8576699, ECO:0000269|PubMed:9306007}.

Target

voltage-gated sodium channel (Nav)

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Anthopleura xanthogrammica (Giant green sea anemone) (Actinia xanthogrammica)
Neurotoxin Ion channel impairing toxin Voltage-gated sodium channel impairing toxin
Binds specifically to voltage-gated sodium channels (Nav) (site 3), thereby delaying their inactivation. This toxin retains the greatest capacity to discriminate between the cardiac (Nav1.5/SCN5A) and neuronal sodium channels (2.5 nM versus 120 nM, when electrophysiologically tested and 14 nM versus 400 nM, when tested by ion flux), whereas its paralog Anthopleurin-B has the highest affinity of all anemone toxins for the mammalian sodium channel (PubMed:13806, PubMed:17092528, PubMed:7612595).
Delta-actitoxin-Axm1a (Delta-AITX-Axm1a) (Anthopleurin-A) (AP-A) (ApA) (PCR3-3,4) (Toxin PCR7)
sea anemone
Sea anemone sodium channel inhibitory toxin family, Type I subfamily
Evidence at protein level
3D-structure Cardiotoxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Nematocyst Neurotoxin Secreted Toxin Voltage-gated sodium channel impairing toxin
Additional Detail Fields 6 fields
3D-structure Cardiotoxin Direct protein sequencing Disulfide bond Ion channel impairing toxin Nematocyst Neurotoxin Secreted Toxin Voltage-gated sodium channel impairing toxin
Neurotoxin Ion channel impairing toxin Voltage-gated sodium channel impairing toxin
Evidence at protein level
Sea anemone sodium channel inhibitory toxin family, Type I subfamily
Delta-actitoxin-Axm1a (Delta-AITX-Axm1a) (Anthopleurin-A) (AP-A) (ApA) (PCR3-3,4) (Toxin PCR7)
sea anemone