ID   KAX6B_OPIMA             Reviewed;          63 AA.
AC   P0C194;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Potassium channel toxin alpha-KTx 6.11;
DE   AltName: Full=Male-specific potassium channel inhibitor IsTX {ECO:0000303|PubMed:15373831};
DE   Flags: Precursor;
OS   Opisthacanthus madagascariensis (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Scorpionoidea; Hemiscorpiidae; Opisthacanthus.
OX   NCBI_TaxID=167108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-62, DISULFIDE BONDS,
RP   SYNTHESIS OF 22-62, MASS SPECTROMETRY, AND STRUCTURE BY NMR OF 22-62.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15373831; DOI=10.1111/j.1432-1033.2004.04322.x;
RA   Yamaji N., Dai L., Sugase K., Andriantsiferana M., Nakajima T.,
RA   Iwashita T.;
RT   "Solution structure of IsTX. A male scorpion toxin from Opisthacanthus
RT   madagascariensis (Ischnuridae).";
RL   Eur. J. Biochem. 271:3855-3864(2004).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels Kv1.1/KCNA1 and
CC       Kv1.3/KCNA3. Causes paralysis to crickets.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. Only expressed by
CC       males.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC   -!- MASS SPECTROMETRY: Mass=4818.23; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15373831};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 06 subfamily. {ECO:0000305}.
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DR   PDB; 1WMT; NMR; -; A=22-62.
DR   PDBsum; 1WMT; -.
DR   AlphaFoldDB; P0C194; -.
DR   SMR; P0C194; -.
DR   TCDB; 8.B.8.1.8; the Alpha-ktx15 scorpion toxin (Alpha-ktx15) family.
DR   EvolutionaryTrace; P0C194; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 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; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15373831"
FT   CHAIN           22..62
FT                   /note="Potassium channel toxin alpha-KTx 6.11"
FT                   /id="PRO_0000232654"
FT   SITE            48
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   SITE            50
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   SITE            51
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   SITE            57
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:Q10726"
FT   DISULFID        28..49
FT                   /evidence="ECO:0000269|PubMed:15373831,
FT                   ECO:0007744|PDB:1WMT"
FT   DISULFID        34..54
FT                   /evidence="ECO:0000269|PubMed:15373831,
FT                   ECO:0007744|PDB:1WMT"
FT   DISULFID        38..56
FT                   /evidence="ECO:0000269|PubMed:15373831,
FT                   ECO:0007744|PDB:1WMT"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000269|PubMed:15373831,
FT                   ECO:0007744|PDB:1WMT"
FT   HELIX           31..40
FT                   /evidence="ECO:0007829|PDB:1WMT"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1WMT"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:1WMT"
SQ   SEQUENCE   63 AA;  7324 MW;  C9BDC4E26532BB26 CRC64;
     MKVAYLLVLF TIMMLANDAS LVHTNIPCRG TSDCYEPCEK KYNCARAKCM NRHCNCYNNC
     PWR