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Peptide record

TPDB10949

Antibacterial Anticancer Antifungal Antiparasitic Neurotoxin Toxicity standard
27 amino acids
Basic Information
3D PDB MODEL
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TPDB10949
Antibacterial Anticancer Antifungal Antiparasitic Neurotoxin Toxicity
Anti-infective peptides Cancer-related peptides Toxicity and safety peptides
AntiBP3 dbAMP DRAMP pep-lab Peptipedia AntiCP 2.0 iACP-DRLF AFP-GFuse Antifungipept CAFPdb i2APP NTxPred2 ToxinPred 3.0
standard
No
A 27-aa standard natural multi-activity (Antibacterial, Anticancer, Antifungal, and other sources) peptide sequence curated from AntiBP3, dbAMP, DRAMP, and other sources, with an available 3D structural model.
Sequence
KIKWFKTMKSIAKFIAKEQMKKHLGGE
Physicochemical Analysis
C149H245N39O35S2
RNDCPYV
K
3206.94
10.74
9
2
11
+6
7.39
-0.659
65.19
Mammalian: 1.3 hour Yeast: 3 min E.coli: 2 min
5500
171.50
3
Residue Composition
number
2
A
0
R
0
N
0
D
0
C
2
E
1
Q
2
G
1
H
3
I
1
L
8
K
2
M
2
F
0
P
1
S
1
T
1
W
0
Y
0
V
Amino Acid Distribution
A: 2 R: 0 N: 0 D: 0 C: 0 E: 2 Q: 1 G: 2 H: 1 I: 3 L: 1 K: 8 M: 2 F: 2 P: 0 S: 1 T: 1 W: 1 Y: 0 V: 0
Chemical Descriptors
27
C149H245N39O35S2
3206.94
10.74
+6
7.39
-0.659
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane. Potently inhibits the growth of bacteria, yeast and Leishmania. May function both in the prey capture strategy as well as protection from infectious organisms arising from prey ingestion (By similarity). {ECO:0000250, ECO:0000269|PubMed:18098329, ECO:0000269|PubMed:9442044}.

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Hogna carolinensis (Carolina wolf spider) (Lycosa carolinensis)
Neurotoxin
Forms pore that permeabilize the cell membrane. Promotes efflux of calcium from synaptosomes, causes hemolysis, and dissipates voltage gradients across muscle membrane.
M-lycotoxin-Hc2a (M-LCTX-Hc2a) (Lycotoxin II) (Lycotoxin-2)
spider
Cationic peptide 04 (cupiennin) family, 05 subfamily
Evidence at protein level
Antibiotic Antimicrobial Cytolysis Direct protein sequencing Hemolysis Neurotoxin Secreted Toxin
TISSUE SPECIFICITY: Expressed by the venom gland.
Additional Detail Fields 7 fields
Antibiotic Antimicrobial Cytolysis Direct protein sequencing Hemolysis Neurotoxin Secreted Toxin
Neurotoxin
Evidence at protein level
Cationic peptide 04 (cupiennin) family, 05 subfamily
M-lycotoxin-Hc2a (M-LCTX-Hc2a) (Lycotoxin II) (Lycotoxin-2)
TISSUE SPECIFICITY: Expressed by the venom gland.
spider