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Peptide record

TPDB40112

Leucomyosuppressin Neuropeptide Neurotoxin Toxicity standard
10 amino acids
Basic Information
3D PDB MODEL
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TPDB40112
Leucomyosuppressin
Neuropeptide Neurotoxin Toxicity
Toxicity and safety peptides Neuroactive peptides
Peptipedia NTxPred2 ToxinPred 3.0
standard
No
A 10-aa standard natural multi-activity (Neuropeptide, Neurotoxin, and Toxicity) peptide sequence curated from Peptipedia, NTxPred2, and ToxinPred 3.0, with an available 3D structural model.
Sequence
EDVDHVFLRF
Physicochemical Analysis
C59H85N15O17
ANCQGIKMPSTWY
DFV
1276.41
4.30
2
3
5
-2
3.57
-0.040
97.00
Mammalian: 1 hour Yeast: 30 min E.coli: >10 hour
0
0.00
0
Residue Composition
number
0
A
1
R
0
N
2
D
0
C
1
E
0
Q
0
G
1
H
0
I
1
L
0
K
0
M
2
F
0
P
0
S
0
T
0
W
0
Y
2
V
Amino Acid Distribution
A: 0 R: 1 N: 0 D: 2 C: 0 E: 1 Q: 0 G: 0 H: 1 I: 0 L: 1 K: 0 M: 0 F: 2 P: 0 S: 0 T: 0 W: 0 Y: 0 V: 2
Chemical Descriptors
10
C59H85N15O17
1276.41
4.30
-2
3.57
-0.040
Evidence Records 6 records
Evidence 1 Activity

Activity

Neuropeptide

Source & Reference

NA
NeuroPepV2

Other

Haematobia irritans
Myosuppressin
Evidence 2 Activity

Activity

Neuropeptide

Source & Reference

NA
NeuroPepV2

Other

Stomoxys calcitrans
Myosuppressin
Evidence 3 Activity

Activity

Neuropeptide

Source & Reference

NA
NeuroPepV2

Other

Tenebrio molitor
Myosuppressin
Evidence 4 Activity

Activity

Neuropeptide

Source & Reference

NA
NeuroPepV2

Other

Zophobas atratus
Myosuppressin
Evidence 5 Activity

Activity

Neurotoxin
FUNCTION: May be directly involved in a paralyzing effect, by inhibiting muscle contraction, or may also act centrally to modulate prey behaviors (Probable). The non-amidated form (Sa12b) potently inhibits ASIC current in rat DRG neurons (IC(50)=81 nM) when preincubated before activation by acidic pH (PubMed:31658776). Has no consistent action on the time course of desensitization or the sustained component of the current (PubMed:31658776). Has no activity when coapplied with acidic pH, suggesting that the peptide needs to interact with the channel during its closed state (PubMed:31658776). This effect is concentration-dependent and reversed after washout of the peptide (PubMed:31658776). Since the inhibition is almost complete at 1 uM and all ASIC subunits are expressed in dorsal root ganglion (DRG) neurons, it suggests that it inhibits different ASIC subunits without an apparent selectivity (PubMed:31658776). It is noteworthy that it does not show activity on the locust oviduct contraction (tested at 50 nM), in contrast to the amidated form (PubMed:34023397, Ref.2). {ECO:0000269|PubMed:31658776, ECO:0000269|PubMed:34023397, ECO:0000269|Ref.2, ECO:0000305|PubMed:34023397}. FUNCTION: The amidated form (Sa112) inhibits both the frequency and amplitude of spontaneous contractions of the locust oviducts (tested at 50 nM). {ECO:0000269|PubMed:34023397, ECO:0000269|Ref.2}.

Target

voltage-gated sodium channel (Nav) proton-gated sodium channel / ASIC

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Sphex argentatus argentatus (Black digger wasp)
Neurotoxin Ion channel impairing toxin Proton-gated sodium channel impairing toxin
May be directly involved in a paralyzing effect, by inhibiting muscle contraction, or may also act centrally to modulate prey behaviors (Probable). The non-amidated form (Sa12b) potently inhibits ASIC current in rat DRG neurons (IC(50)=81 nM) when preincubated before activation by acidic pH (PubMed:31658776).
FMRFamide-like peptide Sa12b (Sa-12) (Sa12b) (Sa-112) (Sa112)
insect
FARP (FMRFamide related peptide) family
Evidence at protein level
Amidation Direct protein sequencing Ion channel impairing toxin Neurotoxin Proton-gated sodium channel impairing toxin Secreted Toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:31658776, ECO:0000305|PubMed:34023397, ECO:0000305|Ref.2}.
Evidence 6 Activity

Activity

Neurotoxin
FUNCTION: [FMRFamide-like peptide Sh5a]: May be directly involved in a paralyzing effect, by inhibiting muscle contraction, or may also act centrally to modulate prey behaviors (Probable). Inhibits both the frequency and amplitude of spontaneous contractions of the locust oviducts (tested at 50 nM) (Ref.2). {ECO:0000269|Ref.2, ECO:0000305|PubMed:34023397}. FUNCTION: [FMRFamide-like peptide Sh5b]: Does not produce consistent and reproducible effects on ASIC currents (PubMed:31658776). Inhibits spontaneous oviduct contractions to the same extent as that of SchistoFLRFamide (Probable). {ECO:0000269|PubMed:31658776, ECO:0000305|PubMed:34023397}.

Target

proton-gated sodium channel / ASIC

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Isodontia harmandi (Grass-carrying wasp)
Neurotoxin
[FMRFamide-like peptide Sh5a]: May be directly involved in a paralyzing effect, by inhibiting muscle contraction, or may also act centrally to modulate prey behaviors (Probable). Inhibits both the frequency and amplitude of spontaneous contractions of the locust oviducts (tested at 50 nM) (Ref.2).. FUNCTION: [FMRFamide-like peptide Sh5b]: Does not produce consistent and reproducible effects on ASIC currents (PubMed:31658776).
FMRFamide-like peptide Sh5a (FMRFamide-like peptide Sa-112) (Sa112) [Cleaved into: FMRFamide-like peptide Sh5b]
insect
FARP (FMRFamide related peptide) family
Evidence at protein level
Amidation Direct protein sequencing Neurotoxin Secreted Toxin
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:31658776, ECO:0000305|PubMed:34023397, ECO:0000305|Ref.2}.
Additional Detail Fields 8 fields
Myosuppressin
Amidation Direct protein sequencing Ion channel impairing toxin Neurotoxin Proton-gated sodium channel impairing toxin Secreted Toxin
Neurotoxin Ion channel impairing toxin Proton-gated sodium channel impairing toxin
Evidence at protein level
FARP (FMRFamide related peptide) family
FMRFamide-like peptide Sa12b (Sa-12) (Sa12b) (Sa-112) (Sa112) FMRFamide-like peptide Sh5a (FMRFamide-like peptide Sa-112) (Sa112) [Cleaved into: FMRFamide-like peptide Sh5b]
TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|PubMed:31658776, ECO:0000305|PubMed:34023397, ECO:0000305|Ref.2}.
insect