ID   KA301_SCOR              Reviewed;          66 AA.
AC   P0DL33;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Potassium channel toxin alpha-KTx 30.1;
DE   AltName: Full=Toxin SjKTx23;
DE   AltName: Full=Toxin StKTx23;
DE   Flags: Precursor;
OS   Scorpiops margerisonae (Scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Iurida; Chactoidea; Euscorpiidae; Scorpiopinae; Scorpiopini;
OC   Scorpiops.
OX   NCBI_TaxID=856992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22155128; DOI=10.1016/j.jprot.2011.11.029;
RA   Ma Y., He Y., Zhao R., Wu Y., Li W., Cao Z.;
RT   "Extreme diversity of scorpion venom peptides and proteins revealed by
RT   transcriptomic analysis: implication for proteome evolution of scorpion
RT   venom arsenal.";
RL   J. Proteomics 75:1563-1576(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Venom gland;
RX   PubMed=22511981; DOI=10.1371/journal.pone.0035154;
RA   Chen Z.Y., Zeng D.Y., Hu Y.T., He Y.W., Pan N., Ding J.P., Cao Z.J.,
RA   Liu M.L., Li W.X., Yi H., Jiang L., Wu Y.L.;
RT   "Structural and functional diversity of acidic scorpion potassium channel
RT   toxins.";
RL   PLoS ONE 7:E35154-E35154(2012).
CC   -!- FUNCTION: inhibits Kv1.3/KCNA3 channel (1 uM of the toxin inhibits
CC       currents by 64.1%). {ECO:0000269|PubMed:22511981}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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: Does not block Kv7.1/KCNQ1 channels.
CC       {ECO:0000305|PubMed:22511981}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 30 subfamily. {ECO:0000305}.
CC   -!- CAUTION: PubMed:22511981 refers the nucleotide sequence FD664509 as
CC       coming from Scorpiops tibetanus. {ECO:0000305}.
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DR   EMBL; FD664509; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DL33; -.
DR   SMR; P0DL33; -.
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; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   2: Evidence at transcript level;
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..66
FT                   /note="Potassium channel toxin alpha-KTx 30.1"
FT                   /id="PRO_0000424389"
FT   DISULFID        30..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..55
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..57
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   66 AA;  7338 MW;  0D04CFB672083E18 CRC64;
     MNTGFFFFVI MATGLVLTFD TIHAEDKLKC TKTDDCAKYC SQFTDVHPAC LGGYCECLRW
     EGGISS