Summary
Sea anemone toxin k like
Members of this clan include the Crisp domain which is involved in ryanodine receptor Ca2+ signalling, and the ShK domain which is named after the ShK channel inhibitor toxin. Both domains are cysteine rich and contain multiple disulphide bonds [1][2][3].
This clan contains 2 families and the total number of domains in the clan is 11001. The clan was built by J Mistry.
Literature references
- Tudor JE, Pallaghy PK, Pennington MW, Norton RS; , Nat Struct Biol. 1996;3:317-320.: Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. PUBMED:8599755 EPMC:8599755
- Gibbs GM, Scanlon MJ, Swarbrick J, Curtis S, Gallant E, Dulhunty A, O'bryan MK; , J Biol Chem. 2005; [Epub ahead of print]: The crisp domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signalling. PUBMED:16339766 EPMC:16339766
- Castaneda O, Sotolongo V, Amor AM, Stocklin R, Anderson AJ, Harvey AL, Engstrom A, Wernstedt C, Karlsson E; , Toxicon. 1995;33:603-613.: Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. PUBMED:7660365 EPMC:7660365
Members
This clan contains the following 2 member families:
Crisp ShKExternal database links
SCOP: | 57546 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
Pfam family | Num. domains | Alignment |
---|---|---|
ShK (PF01549) | 10282 (93.5%) | View |
Crisp (PF08562) | 719 (6.5%) | View |
Total: 2 | Total: 11001 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
Tree controls
HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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