ID   KA11N_SCOPC             Reviewed;          63 AA.
AC   P0DQN4;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Potassium channel toxin alpha-KTX 11 Sp4 {ECO:0000305};
DE            Short=KTX-Sp4 {ECO:0000303|PubMed:29142737};
DE   Flags: Precursor;
OS   Scorpiops pococki (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Euscorpiidae; Scorpiopinae; Scorpiopini;
OC   Scorpiops.
OX   NCBI_TaxID=2766750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND RECOMBINANT EXPRESSION.
RC   TISSUE=Venom gland;
RX   PubMed=29142737; DOI=10.1186/s13578-017-0187-x;
RA   Zou Y., Zhang F., Li Y., Wang Y., Li Y., Long Z., Shi S., Shuai L., Liu J.,
RA   Di Z., Yin S.;
RT   "Cloning, expression and identification of KTX-Sp4, a selective Kv1.3
RT   peptidic blocker from Scorpiops pococki.";
RL   Cell Biosci. 7:60-60(2017).
CC   -!- FUNCTION: This recombinant toxin selectively inhibits mouse voltage-
CC       gated potassium channel Kv1.3/KCNA3 (IC(50)=24.73 nM).
CC       {ECO:0000269|PubMed:29142737}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29142737}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29142737}.
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   -!- MISCELLANEOUS: Shows only a weak inhibition on Kv1.1/KCNA1 (20.85%
CC       inhibition when tested with 1 uM of toxin) and Kv1.2/KCNA2 (7.23%
CC       inhibition, same conditions). {ECO:0000269|PubMed:29142737}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 11 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DQN4; -.
DR   SMR; P0DQN4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR029237; Long_scorpion_toxin.
DR   PROSITE; PS51862; BSPN_CSAB; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..63
FT                   /note="Potassium channel toxin alpha-KTX 11 Sp4"
FT                   /evidence="ECO:0000305|PubMed:29142737"
FT                   /id="PRO_0000451631"
FT   DISULFID        31..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        38..58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        42..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   63 AA;  6709 MW;  D3CEF9675523E24A CRC64;
     MNKVHFALFL LVLTVLAVSG FPSENAPTGG CPLSDNVCSS YCKKNKFGNE GKCHGTICKC
     SIK