ID   KA15S_CHATC             Reviewed;          62 AA.
AC   P0DJO5;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Potassium channel toxin alpha-KTx Ctri9577;
DE   Flags: Precursor;
OS   Chaerilus tricostatus (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Chaerilida; Chaeriloidea; Chaerilidae; Chaerilus.
OX   NCBI_TaxID=1055734;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=22580271; DOI=10.1016/j.peptides.2012.04.023;
RA   Xie S., Feng J., Yu C., Li Z., Wu Y., Cao Z., Li W., He X., Xiang M.,
RA   Han S.;
RT   "Identification of a new specific Kv1.3 channel blocker, Ctri9577, from the
RT   scorpion Chaerilus tricostatus.";
RL   Peptides 36:94-99(2012).
CC   -!- FUNCTION: Blocker of A-type voltage-gated potassium channels of
CC       cerebellar granular cells. May also inhibit Kv4/KCND when coexpressed
CC       with DPP6 or DPP10. The occlusion of the outer entry of the K(+)
CC       conducting pore is partially reversible and affects both open and
CC       closed channels. It shares the same target in rat brain than BmTX3 (AC
CC       Q8I0L5) and AmmTX3 (AC P60208). Recombinant toxin inhibits mKv1.3/KCNA3
CC       channel (IC(50)=0.49 nM) (PubMed:22580271).
CC       {ECO:0000250|UniProtKB:P60208, ECO:0000250|UniProtKB:Q867F4,
CC       ECO:0000269|PubMed:22580271}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22580271}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22580271}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta).
CC       {ECO:0000250|UniProtKB:P84777}.
CC   -!- MISCELLANEOUS: Exhibits little blockage on mKv1.1/KCNA1, hKv1.2/KCNA2,
CC       hERG/Kv11.1/KCNH2, and hKCa2.3/KCNN3. {ECO:0000269|PubMed:22580271}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 15 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJO5; -.
DR   SMR; P0DJO5; -.
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   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         24..62
FT                   /note="Potassium channel toxin alpha-KTx Ctri9577"
FT                   /id="PRO_0000418799"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        38..58
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
FT   DISULFID        42..60
FT                   /evidence="ECO:0000250|UniProtKB:Q86BX0"
SQ   SEQUENCE   62 AA;  7039 MW;  D7BDB854019CB849 CRC64;
     MKLVMRILLT CFLLTTLVIK AEGQIHTNQP CTSNNTRCRT YCIKVHKINS GKCMNSKCVC
     HP