ID   KAX47_TITST             Reviewed;          59 AA.
AC   P0DPT4;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Potassium channel toxin alpha-KTx 4.7 {ECO:0000305};
DE   AltName: Full=T.sigmurus alpha-KTx {ECO:0000303|PubMed:30553160};
DE   Flags: Precursor;
OS   Tityus stigmurus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=50344;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND 3D-STRUCTURE MODELING OF THE TOXIN IN COMPLEX
RP   WITH POTASSIUM CHANNEL KV1.2.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=30553160; DOI=10.1016/j.jmgm.2018.11.012;
RA   Freire M.C.L.C., Silva de Menezes Y.A., Ferreira Ferraz M.V.,
RA   Bezerra da Cruz C.H., De Santis Ferreira L.,
RA   de Freitas Fernandes-Pedrosa M., Barbosa E.G.;
RT   "Molecular basis of Tityus stigmurus alpha toxin and potassium channel
RT   kV1.2 interactions.";
RL   J. Mol. Graph. Model. 87:197-203(2019).
CC   -!- FUNCTION: Potently blocks Kv1.1/KCNA1 (85%), Kv1.2/KCNA2 (91%),
CC       Kv1.3/KCNA3 (89%), Kv1.6/KCNA6 (94%), and Shaker (97%).
CC       {ECO:0000250|UniProtKB:P46114}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30553160}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:30553160}.
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:P46114}.
CC   -!- MASS SPECTROMETRY: Mass=1311.29; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:30553160};
CC   -!- MISCELLANEOUS: Inhibits with low efficiency Kv1.5/KCNA5, Kv2.1/KCNB1,
CC       Kv7.1/KCNQ1 and ERG/KCNH2. Does not inhibit Kv1.4/KCNA4, Kv3.1/KCNC1,
CC       Kv7.2/KCNQ2 and ERG1/Kv11.1/KCNH2. {ECO:0000250|UniProtKB:P46114}.
CC   -!- MISCELLANEOUS: Unexpectandly, the 3D-structure model presents a toxin
CC       with only two disulfide bonds instead of the three normally found in
CC       this toxin family. {ECO:0000305|PubMed:30553160}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 04 subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DPT4; -.
DR   SMR; P0DPT4; -.
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   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..22
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         23..59
FT                   /note="Potassium channel toxin alpha-KTx 4.7"
FT                   /evidence="ECO:0000250|UniProtKB:P46114"
FT                   /id="PRO_0000446448"
FT   REGION          48..55
FT                   /note="Interaction with Ca(2+)-activated K(+) channels"
FT                   /evidence="ECO:0000255"
FT   SITE            49
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   SITE            58
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250|UniProtKB:O46028"
FT   DISULFID        29..50
FT                   /evidence="ECO:0000250|UniProtKB:P46114"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000250|UniProtKB:P46114"
FT   DISULFID        39..57
FT                   /evidence="ECO:0000250|UniProtKB:P46114"
SQ   SEQUENCE   59 AA;  6488 MW;  DE25F3AA90917B8A CRC64;
     MKAFYGILII FILISMLDLS QQVFINAKCR GSPECLPKCK EAIGKAAGKC MNGKCKCYP