ID   KAX94_HOTTA             Reviewed;          32 AA.
AC   P60209;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Potassium channel toxin alpha-KTx 9.4 {ECO:0000305};
DE   AltName: Full=BTK-2 {ECO:0000303|PubMed:12650917};
OS   Hottentotta tamulus (Eastern Indian scorpion) (Mesobuthus tamulus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX   NCBI_TaxID=34647;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   3D-STRUCTURE MODELING.
RC   TISSUE=Venom;
RX   PubMed=12650917; DOI=10.1016/s0014-5793(03)00125-x;
RA   Dhawan R., Varshney A., Mathew M.K., Lala A.K.;
RT   "BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian
RT   scorpion Buthus tamulus.";
RL   FEBS Lett. 539:7-13(2003).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=21256986; DOI=10.1016/j.bbapap.2011.01.006;
RA   Kumar G.S., Upadhyay S., Mathew M.K., Sarma S.P.;
RT   "Solution structure of BTK-2, a novel hK(v)1.1 inhibiting scorpion toxin,
RT   from the eastern Indian scorpion Mesobuthus tamulus.";
RL   Biochim. Biophys. Acta 1814:459-469(2011).
CC   -!- FUNCTION: Blocker of human voltage-gated potassium channel Kv1.1/KCNA1
CC       (PubMed:12650917). {ECO:0000269|PubMed:12650917}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12650917}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:12650917}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000269|PubMed:21256986}.
CC   -!- MASS SPECTROMETRY: Mass=3452; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12650917};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 09 subfamily. {ECO:0000305}.
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DR   PDB; 2KTC; NMR; -; A=1-32.
DR   PDBsum; 2KTC; -.
DR   AlphaFoldDB; P60209; -.
DR   BMRB; P60209; -.
DR   SMR; P60209; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR008911; Toxin_alpha-KTx_8/9.
DR   Pfam; PF05453; Toxin_6; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin; Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..32
FT                   /note="Potassium channel toxin alpha-KTx 9.4"
FT                   /evidence="ECO:0000269|PubMed:12650917"
FT                   /id="PRO_0000044948"
FT   DISULFID        3..19
FT                   /evidence="ECO:0000269|PubMed:21256986,
FT                   ECO:0000312|PDB:2KTC"
FT   DISULFID        6..24
FT                   /evidence="ECO:0000269|PubMed:21256986,
FT                   ECO:0000312|PDB:2KTC"
FT   DISULFID        10..26
FT                   /evidence="ECO:0000269|PubMed:21256986,
FT                   ECO:0000312|PDB:2KTC"
FT   HELIX           2..8
FT                   /evidence="ECO:0007829|PDB:2KTC"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:2KTC"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:2KTC"
SQ   SEQUENCE   32 AA;  3456 MW;  D472FEEB98E7E97F CRC64;
     VGCAECPMHC KGKMAKPTCE NEVCKCNIGK KD