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Peptide record

TPDB27876

Neurotoxin Toxicity standard
49 amino acids
Basic Information
3D PDB MODEL
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TPDB27876
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
GVPCLCDSDGPRPRGNTLSGILWFYPSGCPSGWHNCKAHGPNIGWCCKK
Physicochemical Analysis
C231H344N68O63S6
EQM
G
5274.05
8.31
7
2
12
+3
2.21
-0.431
47.76
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
18365
348.21
15
Residue Composition
number
1
A
2
R
3
N
2
D
6
C
0
E
0
Q
8
G
2
H
2
I
3
L
3
K
0
M
1
F
6
P
4
S
1
T
3
W
1
Y
1
V
Amino Acid Distribution
A: 1 R: 2 N: 3 D: 2 C: 6 E: 0 Q: 0 G: 8 H: 2 I: 2 L: 3 K: 3 M: 0 F: 1 P: 6 S: 4 T: 1 W: 3 Y: 1 V: 1
Chemical Descriptors
49
C231H344N68O63S6
5274.05
8.31
+3
2.21
-0.431
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 has the highest affinity of all anemone toxins for the mammalian sodium channel, whereas its paralog Anthopleurin-A retains the greatest capacity to discriminate between cardiac (Nav1.5/SCN5A) and neuronal sodium channels (PubMed:8916901). When tested electrophysiologically, this toxin exhibits a high affinity for multiple sodium channels with a 50-fold preference for rat cardiac (Nav1.5/SCN5A) over neuronal channels (0.1 nM versus 5 nM). When tested by ion flux, the affinities are similar and appear to have higher affinity (9 nM versus 22 nM) (PubMed:7612595, PubMed:8276803). The residue Lys-37 of this toxin has been shown to interact with channel Nav1.5 (residue Asp-1612 in rat and Asp-1610 in human), which is located in the DIV S3-S4 linker (corresponding to channel site 3) (PubMed:24898004, PubMed:9417050). Selectively modifies sodium channel inactivation from the open state with little effect on channel activation or on inactivation from closed states (By similarity). 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 (PubMed:15632158). {ECO:0000250|UniProtKB:P01530, ECO:0000269|PubMed:15632158, ECO:0000269|PubMed:24898004, ECO:0000269|PubMed:7612595, ECO:0000269|PubMed:8276803, ECO:0000269|PubMed:8916901, ECO:0000269|PubMed:9306007, ECO:0000269|PubMed:9417050}.

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 has the highest affinity of all anemone toxins for the mammalian sodium channel, whereas its paralog Anthopleurin-A retains the greatest capacity to discriminate between cardiac (Nav1.5/SCN5A) and neuronal sodium channels (PubMed:8916901).
Delta-actitoxin-Axm1b (Delta-AITX-Axm1b) (Anthopleurin-B) (AP-B) (ApB)
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-Axm1b (Delta-AITX-Axm1b) (Anthopleurin-B) (AP-B) (ApB)
sea anemone