ID   KAX3B_ODODO             Reviewed;          38 AA.
AC   P0C909;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Potassium channel toxin alpha-KTx 3.11;
DE   AltName: Full=OdK2 {ECO:0000303|PubMed:18471844};
OS   Odontobuthus doriae (Yellow Iranian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Odontobuthus.
OX   NCBI_TaxID=342590;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=18471844; DOI=10.1016/j.toxicon.2008.03.027;
RA   Abdel-Mottaleb Y., Vandendriessche T., Clynen E., Landuyt B., Jalali A.,
RA   Vatanpour H., Schoofs L., Tytgat J.;
RT   "OdK2, a Kv1.3 channel-selective toxin from the venom of the Iranian
RT   scorpion Odonthobuthus doriae.";
RL   Toxicon 51:1424-1430(2008).
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
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: Blocks the voltage-gated potassium channel Kv1.3/KCNA3
CC       (IC(50)=7.2 nM) (PubMed:18471844, PubMed:29483648). Correnti and
CC       colleagues have also shown that this toxin inhibits Kv1.1/KCNA1, which
CC       is different from Abdel-Mottaleb and colleagues conclusions
CC       (PubMed:29483648). {ECO:0000269|PubMed:18471844,
CC       ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18471844}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18471844}.
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=4072; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18471844};
CC   -!- MISCELLANEOUS: Has no activity on Kv1.1/KCNA1, Kv1.2/KCNA2,
CC       Kv1.4/KCNA4, Kv1.5/ KCNA5, Kv1.6/KCNA6, Shaker/Sh and human
CC       Kv11.1/KCNH2. {ECO:0000269|PubMed:18471844}.
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   AlphaFoldDB; P0C909; -.
DR   SMR; P0C909; -.
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   PRINTS; PR00286; CHARYBDTOXIN.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS01138; SCORP_SHORT_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   PEPTIDE         1..38
FT                   /note="Potassium channel toxin alpha-KTx 3.11"
FT                   /evidence="ECO:0000269|PubMed:18471844"
FT                   /id="PRO_0000368017"
FT   DISULFID        8..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..35
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   38 AA;  4083 MW;  0ACB1B1D168D2174 CRC64;
     GVPTDVKCRG SPQCIQPCKD AGMRFGKCMN GKCHCTPK