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Peptide record

TPDB72328

Neurotoxin standard
138 amino acids
Basic Information
3D PDB MODEL
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TPDB72328
Neurotoxin
Toxicity and safety peptides
NTxPred2
standard
No
A 138-aa standard natural neurotoxin peptide sequence curated from NTxPred2, with an available 3D structural model.
Sequence
MRALWIVAVLLVGVEGHLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC
Physicochemical Analysis
C708H1071N191O194S17
C
15907.48
8.30
22
13
53
+7
11.59
-0.260
60.80
Mammalian: 30 hour Yeast: >20 hour E.coli: >10 hour
39265
246.83
43
Residue Composition
number
8
A
10
R
3
N
6
D
14
C
7
E
2
Q
13
G
2
H
6
I
9
L
10
K
3
M
6
F
5
P
6
S
7
T
4
W
11
Y
6
V
Amino Acid Distribution
A: 8 R: 10 N: 3 D: 6 C: 14 E: 7 Q: 2 G: 13 H: 2 I: 6 L: 9 K: 10 M: 3 F: 6 P: 5 S: 6 T: 7 W: 4 Y: 11 V: 6
Chemical Descriptors
138
C708H1071N191O194S17
15907.48
8.30
+7
11.59
-0.260
Evidence Records 3 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (By similarity). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (By similarity). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (By similarity). {ECO:0000250|UniProtKB:C0HM14}. FUNCTION: Monomer CBc: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:35737043). {ECO:0000250|UniProtKB:P62022, ECO:0000269|PubMed:35737043}.

Target

proton-gated sodium channel / ASIC

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Crotalus tzabcan (Yucatan neotropical rattlesnake) (Crotalus simus tzabcan)
Neurotoxin Presynaptic neurotoxin Ion channel impairing toxin
Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (By similarity).
Phospholipase A2 crotoxin basic subunit CBc (CB1) (CTX subunit CBc) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
snake
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
Evidence at protein level
Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Ion channel impairing toxin Lipid degradation Lipid metabolism Metal-binding Neurotoxin Presynaptic neurotoxin Secreted Signal Toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:35737043, ECO:0000305|PubMed:27280639}.
Evidence 2 Activity

Activity

Neurotoxin
FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (By similarity). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (By similarity). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (By similarity). In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (PubMed:20109480). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (PubMed:20109480). {ECO:0000250|UniProtKB:C0HM14, ECO:0000269|PubMed:20109480}. FUNCTION: Monomer CBc: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC(50) is 0.7 nM) (PubMed:18062812). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (PubMed:27241308). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:18062812, ECO:0000269|PubMed:27241308}.

Target

proton-gated sodium channel / ASIC

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Crotalus durissus terrificus (South American rattlesnake)
Neurotoxin Presynaptic neurotoxin Ion channel impairing toxin
Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (By similarity). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (By similarity).
Phospholipase A2 crotoxin basic subunit CBc (CB1) (CTX subunit CBc) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
snake
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
Evidence at protein level
3D-structure Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Ion channel impairing toxin Lipid degradation Lipid metabolism Metal-binding Neurotoxin Pharmaceutical Presynaptic neurotoxin Secreted Signal Toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:3174444}.
Evidence 3 Activity

Activity

Neurotoxin
FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:15032748}.

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Crotalus scutulatus scutulatus (Mojave rattlesnake)
Neurotoxin Presynaptic neurotoxin
Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides..
Basic phospholipase A2 Mtx-b (svPLA2) (EC 3.1.1.4) (Mojave toxin basic chain) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 CB1)
snake
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
Evidence at protein level
Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Neurotoxin Presynaptic neurotoxin Secreted Signal Toxin
TISSUE SPECIFICITY: Expressed by the venom gland.
Additional Detail Fields 7 fields
Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Ion channel impairing toxin Lipid degradation Lipid metabolism Metal-binding Neurotoxin Presynaptic neurotoxin Secreted Signal Toxin 3D-structure Pharmaceutical
Neurotoxin Presynaptic neurotoxin Ion channel impairing toxin
Evidence at protein level
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
Phospholipase A2 crotoxin basic subunit CBc (CB1) (CTX subunit CBc) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) Basic phospholipase A2 Mtx-b (svPLA2) (EC 3.1.1.4) (Mojave toxin basic chain) (Phosphatidylcholine 2-acylhydrolase) (Phospholipase A2 CB1)
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:35737043, ECO:0000305|PubMed:27280639}. TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|PubMed:3174444}. TISSUE SPECIFICITY: Expressed by the venom gland.
snake