General Information of This Peptide
Peptide ID
BTDP008390
Peptide Name
Kappa-stichotoxin-Hmg1a
Symonym
Potassium channel toxin HmK
Species
Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica)
Uniprot Name
1AK_HETMG
Alphafold ID
O16846
3D Structure
Download
2D Sequence
3D Structure
Source
Alphafold db: O16846
Sequence
MKSQMIAAVLLIAFCLCVVVTARMELQDVEDMENGFQKRRTCKDLIPVSECTDIRCRTSM
KYRLNLCRKTCGSC
   Click to Show/Hide
Sequence Length
74
Mass (Da)
8469
Signal Sequence
MKSQMIAAVLLIAFCLCVVVTA
   Click to Show/Hide
Sequence Removed Signal Peptide
RMELQDVEDMENGFQKRRTCKDLIPVSECTDIRCRTSMKYRLNLCRKTCGSC
   Click to Show/Hide
Disulfide Bond
42-74;51-67;56-71
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Cnidaria
Class: Anthozoa
Order: Actiniaria
Family: Stichodactylidae
Genus: Heteractis
Species: Heteractis magnifica
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    Shaker-KcsA Inhibition constant
0.94 nM
.
Blocker
[4]
 Target Info    Shaker-KcsA Inhibition constant
1 nM
.
Blocker
[5]
 Target Info    Shaker Inhibition constant
1 nM
.
Blocker
[5]
 Target Info    Kv1.2 Inhibition constant
2.5 nM
.
Blocker
[5]
 Target Info    Kv1.3 Inhibition constant
3.1 nM
.
Blocker
[5]
 Target Info    Kv1 IC50
3.2 nM
.
Blocker
[1], [2], [3]
 Target Info    Kv1.2 IC50
10 nM
.
Blocker
[1], [2], [3]
References
Ref 1 A new potassium channel toxin from the sea anemone Heteractis magnifica: isolation, cDNA cloning, and functional expression. Biochemistry. 1997 Sep 23;36(38):11461-71. doi: 10.1021/bi970253d.
Ref 2 Genomic structure of a potassium channel toxin from Heteractis magnifica. FEBS Lett. 1997 Nov 24;418(1-2):183-8. doi: 10.1016/s0014-5793(97)01365-3.
Ref 3 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 4 Tethered peptide neurotoxins display two blocking mechanisms in the K(+) channel pore as do their untethered analogs. Sci Adv. 2020 Mar 4;6(10):eaaz3439. doi: 10.1126/sciadv.aaz3439. eCollection 2020 Mar.
Ref 5 Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage display. Proc Natl Acad Sci U S A. 2015 Dec 15;112(50):E7013-21. doi: 10.1073/pnas.1514728112. Epub 2015 Dec 1.
Data Quality & Feedback

Help us maintain data quality by reporting any errors or inaccuracies you may find.

samedaypayday.com visits since 2024

If you find any error in data or bug in web service, please kindly report it to biodb_contact@163.com et al.