Record in detail
General Info
- lamp_id:L07APD0132
- Name:SCAS_MESMA
- FullName:Beta-toxin BmKAS
- Source:Mesobuthus martensii
- Mass:7701.7 Da
- Sequence Length:66 aa
- Isoelectric Point:8.38
- Activity:Antimicrobial
- Sequence
DNGYLLDKYTGCKVWCVINNESCNSECKIRGGYYGYCYFWKLACFCQGARKSELWNYNTNKCNGKL - Function:Beta toxins bind voltage-independently at site-4 of sodium channels and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. It binds to distinct receptor sites of mammal and insect voltage-gated sodium channels. It displays antinociceptive effect in rat models, which is due to its specific modulation of sodium channels of sensory neurons. It also significantly stimulates the binding of [3H]-ryanodine to ryanodine receptors on the sarcoplasmic reticulum of the skeletal muscle through an indirect mechanism. And it promotes noradrenaline release from the rat hippocampus slice.
Cross-Linking
- Cross-linking
- 1 Database:dbAMP dbAMP_01147
- 2 Database:DRAMP DRAMP03744
- 3 Database:Uniprot Q9UAC9
- 4 Database:RAP RAPD0132
Top similar AMPs
- Top similar AMPs on LAMP
- 1. L07APD0132 From 1 To 66 E-value: 1e-33 Score: 133
DNGYLLDKYTGCKVWCVINNESCNSECKIRGGYYGYCYFWKLACFCQGARKSELWNYNTNKCNGKL - 2. L11A011327 From 1 To 66 E-value: 2e-30 Score: 122
EHGYLLDKYTGCKVWCVINNESCNGECKRRGGYYGYCYFWKLACFCQGARKSELWHYETNKCNGRM - 3. L12A01148| From 1 To 66 E-value: 3e-29 Score: 119
DNGYLLDKYTGCKVWCVINNESCNSECKIRRGNYGYCYFWKLACYCEGAPKSELWHYETNKCNGRM - 4. L13A017036 From 1 To 49 E-value: 1e-21 Score: 93.2
DNGYLLDKYTGCKVWCVINNESCNSECKIRRGNYGYCYFWKLACYCEGA - 5. L11A011326 From 1 To 64 E-value: 2e-20 Score: 89.7
DNGYLLDKYTGCKIWCVINNDSCNSHCIGSGGYYGYCYFWKLACYCQGAPRSELWHYETNRCRA
Activity
- Antibacterial Activities
No MICs found on LAMP database
Toxicity
- Toxicity
No toxicity records found on LAMP database
Reference
- Reference
- [1] Hoshino M.,Liu Y.,Zhou C.-W.,Huang H.-Y.,Ji Y.-H.,
- Title:BmK AS, an active scorpion polypeptide, enhance [3H]-noradrenaline release from rat hippocampal slices.
- Journal:Biomed. Res., 1997, 18, 257-260 [:]
- [2] Xu K.,Ji Y.-H.,Hirayama Y.,Kawano S.,Kuniyasu A.,
- Title:A new scorpion toxin (BmK-PL) stimulates Ca2+-release channel activity of the skeletal-muscle ryanodine receptor by an indirect mechanism.
- Journal:Biochem. J., 1999, 339, 343-350 [PubMed:10191265]
- [3] Yamaki T.,Song B.-L.,Zhang J.-W.,Li Y.-J.,Ji Y.-H.,
- Title:Covalent structures of BmK AS and BmK AS-1, two novel bioactive polypeptides purified from Chinese scorpion Buthus martensi Karsch.
- Journal:Toxicon, 1999, 37, 519-536 [MEDLINE:99178440]
- [4] Xu K.,Feng J.-C.,Zhuo X.-L.,Dai L.,Lan Z.-D.,
- Title:Gene cloning and sequencing of BmK AS and BmK AS-1, two novel neurotoxins from the scorpion Buthus martensi Karsch.
- Journal:Toxicon, 1999, 37, 815-823 [MEDLINE:99235397]
- [5] Ji Y.-H.,Liu Y.,Li Y.-J.,
- Title:BmK AS: new scorpion neurotoxin binds to distinct receptor sites of mammal and insect voltage-gated sodium channels.
- Journal:J. Neurosci. Res., 2000, 61, 541-548 [PubMed:10956424]
- [6] Ji Y.-H.,Chen B.,
- Title:Antihyperalgesia effect of BmK AS, a scorpion toxin, in rat by intraplantar injection.
- Journal:Brain Res., 2002, 952, 322-326 [PubMed:12376194]
- [7] Ji Y.-H.,Feng X.-H.,Shun H.-Y.,Chen J.,Tan Z.-Y.,
- Title:Modulation of BmK AS, a scorpion neurotoxic polypeptide, on voltage-gated Na+ channels in B104 neuronal cell line.
- Journal:Neurosci. Lett., 2003, 340, 123-126 [PubMed:12668252]
- [8] Ji Y.-H.,Susumu T.,Feng X.-H.,Chen J.,Tan Z.-Y.,
- Title:Modulation of intracellular Na+ concentration by BmK AS, a scorpion toxin, in B104 cell line.
- Journal:NeuroReport, 2004, 15, 13-16 [PubMed:15106823]
- [9] Bai Z.-T.,Tan Z.-Y.,Shi J.,Feng X.-H.,Chen J.,
- Title:The anti-nociceptive effect of BmK AS, a scorpion active polypeptide, and the possible mechanism on specifically modulating voltage-gated Na+ currents in primary afferent neurons.
- Journal:Peptides, 2006, 27, 2182-2192 [PubMed:16716457]
Comments
- Comments
No comments found on LAMP database