ID   KAX3A_BUTOS             Reviewed;          59 AA.
AC   P0C908; B8XH28;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.10 {ECO:0000303|PubMed:17490656};
DE   AltName: Full=BoiTx1 {ECO:0000303|PubMed:17490656};
DE   Flags: Precursor;
OS   Buthus occitanus israelis (Common yellow scorpion) (Buthus israelis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=539894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-59, FUNCTION, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17490656; DOI=10.1016/j.febslet.2007.04.065;
RA   Kozminsky-Atias A., Somech E., Zilberberg N.;
RT   "Isolation of the first toxin from the scorpion Buthus occitanus israelis
RT   showing preference for Shaker potassium channels.";
RL   FEBS Lett. 581:2478-2484(2007).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 23-59.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Inhibits insect potassium channel. Is at least a 100-fold
CC       more potent against the Drosophila Shaker channel than towards its
CC       mammalian homologs Kv1.1/KCNA1 and Kv1.3/KCNA3.
CC       {ECO:0000269|PubMed:17490656, ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17490656}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17490656}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4015.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17490656};
CC   -!- MISCELLANEOUS: Mammalian potassium channels (Kv2.1/KCNB1, Kir1.1/KCNJ1,
CC       Kv3.4/KCNC4, Kv4.2/KCND2, Kv7.1/KCNQ1, Kv7.2/KCNQ2, Kv7.3/KCNQ3 and
CC       Kv11.1/KCNH2) are even less affected by this toxin (PubMed:17490656).
CC       Also weakly inhibits Kv11.1/KCNH2/ERG1, Kv1.2/KCNA2 and Nav1.7/SCN9A
CC       channels (PubMed:29483648). {ECO:0000269|PubMed:17490656,
CC       ECO:0000269|PubMed:29483648}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 03 subfamily. {ECO:0000305}.
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DR   EMBL; FJ360817; ACJ23137.1; -; mRNA.
DR   PDB; 6ATM; X-ray; 2.09 A; C=23-59.
DR   PDBsum; 6ATM; -.
DR   AlphaFoldDB; P0C908; -.
DR   SMR; P0C908; -.
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; Knottin, scorpion toxin-like; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR001947; Scorpion_toxinS_K_inh.
DR   Pfam; PF00451; Toxin_2; 1.
DR   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; Scorpion toxin-like; 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..22
FT                   /evidence="ECO:0000269|PubMed:17490656"
FT   PEPTIDE         23..59
FT                   /note="Potassium channel toxin alpha-KTx 3.10"
FT                   /evidence="ECO:0000269|PubMed:17490656"
FT                   /id="PRO_0000368016"
FT   DISULFID        30..50
FT                   /evidence="ECO:0007744|PDB:6ATM"
FT   DISULFID        36..55
FT                   /evidence="ECO:0007744|PDB:6ATM"
FT   DISULFID        40..57
FT                   /evidence="ECO:0007744|PDB:6ATM"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:6ATM"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:6ATM"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:6ATM"
FT   STRAND          45..51
FT                   /evidence="ECO:0007829|PDB:6ATM"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:6ATM"
SQ   SEQUENCE   59 AA;  6402 MW;  FEE2327C83D2C862 CRC64;
     MKVFFAVLIA LFVCSMVIGI HGGVPINVKC RGSRDCLDPC KKAGMRFGKC INSKCHCTP
//