ID   K1HH_ANESU              Reviewed;          29 AA.
AC   P0DPF1;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Ask132958 {ECO:0000303|PubMed:28993277};
DE   AltName: Full=U-ASTX-Asu1 {ECO:0000303|PubMed:28993277};
OS   Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=6108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS, STRUCTURE BY NMR, AND MUTAGENESIS OF
RP   THR-16; GLN-20 AND LEU-28.
RX   PubMed=28993277; DOI=10.1016/j.peptides.2017.10.001;
RA   Krishnarjuna B., MacRaild C.A., Sunanda P., Morales R.A.V., Peigneur S.,
RA   Macrander J., Yu H.H., Daly M., Raghothama S., Dhawan V., Chauhan S.,
RA   Tytgat J., Pennington M.W., Norton R.S.;
RT   "Structure, folding and stability of a minimal homologue from Anemonia
RT   sulcata of the sea anemone potassium channel blocker ShK.";
RL   Peptides 99:169-178(2018).
CC   -!- FUNCTION: This peptide is similar to the potassium channel toxin ShK,
CC       but does not show activity on potassium channels. It appears that Lys-
CC       19, which is expected to occupy the pore of the channel, is not
CC       sufficiently accessible for binding, and therefore that this peptide
CC       must have a distinct functional role that does not involve potassium
CC       channels. It is noteworthy that this peptide is much more stable in the
CC       presence of trypsin, chymotrypsin and pepsin than the toxin ShK.
CC       {ECO:0000269|PubMed:28993277}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28993277}.
CC       Nematocyst {ECO:0000305}.
CC   -!- MISCELLANEOUS: Does not show activity against grass shrimp
CC       (Palaemonetes sp.) and brine shrimp (A.nauplii). Does not show activity
CC       on the voltage-gated potassium channels tested (rKv1.1/KCNA1,
CC       rKv1.2/KCNA2, hKv1.3/KCNA3, rKv1.4/KCNA4, rKv1.5/KCNA5, rKv1.6/KCNA6,
CC       Shaker IR/Sh, rKv4.2/KCND2, Kv11.1/KCNH2/ERG1, hKv10.1/KCNH1/EAG1).
CC       {ECO:0000269|PubMed:28993277}.
CC   -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC       family. Type 1a subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC       URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=30315";
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DR   PDB; 5WCV; NMR; -; A=1-29.
DR   PDBsum; 5WCV; -.
DR   AlphaFoldDB; P0DPF1; -.
DR   SMR; P0DPF1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Nematocyst; Secreted.
FT   PEPTIDE         1..29
FT                   /note="Ask132958"
FT                   /evidence="ECO:0000305|PubMed:28993277"
FT                   /id="PRO_0000443530"
FT   DOMAIN          1..29
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        1..29
FT                   /evidence="ECO:0000269|PubMed:28993277,
FT                   ECO:0000312|PDB:5WCV"
FT   DISULFID        8..22
FT                   /evidence="ECO:0000269|PubMed:28993277,
FT                   ECO:0000312|PDB:5WCV"
FT   DISULFID        13..26
FT                   /evidence="ECO:0000269|PubMed:28993277,
FT                   ECO:0000312|PDB:5WCV"
FT   MUTAGEN         16
FT                   /note="T->Y: No gain of activity on Kv channels."
FT                   /evidence="ECO:0000269|PubMed:28993277"
FT   MUTAGEN         20
FT                   /note="Q->Y: No gain of activity on Kv channels."
FT                   /evidence="ECO:0000269|PubMed:28993277"
FT   MUTAGEN         28
FT                   /note="L->Y: No gain of activity on Kv channels."
FT                   /evidence="ECO:0000269|PubMed:28993277"
SQ   SEQUENCE   29 AA;  3130 MW;  974EA58019385DD9 CRC64;
     CENTISGCSR ADCLLTHRKQ GCQKTCGLC