ID   KTX23_TITSE             Reviewed;          59 AA.
AC   A0A218QXG2;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Putative potassium channel toxin Ts23 {ECO:0000305};
DE   AltName: Full=Putative KTx {ECO:0000305};
DE   AltName: Full=Tityustoxin-23 {ECO:0000305};
DE   Flags: Precursor;
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1] {ECO:0000312|EMBL:JAW06994.1, ECO:0000312|EMBL:JAW07037.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Telson;
RX   PubMed=29561852; DOI=10.1371/journal.pone.0193739;
RA   de Oliveira U.C., Nishiyama M.Y. Jr., Dos Santos M.B.V.,
RA   Santos-da-Silva A.P., Chalkidis H.M., Souza-Imberg A., Candido D.M.,
RA   Yamanouye N., Dorce V.A.C., Junqueira-de-Azevedo I.L.M.;
RT   "Proteomic endorsed transcriptomic profiles of venom glands from Tityus
RT   obscurus and T. serrulatus scorpions.";
RL   PLoS ONE 13:e0193739-e0193739(2018).
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:0000305|PubMed:29561852}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:29561852}.
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   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 04 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GEUW01000051; JAW06994.1; -; mRNA.
DR   EMBL; GEUW01000008; JAW07037.1; -; mRNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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   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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..59
FT                   /note="Putative potassium channel toxin Ts23"
FT                   /id="PRO_5011910071"
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;  6487 MW;  DE30B2FE90917B8A CRC64;
     MKAFYGILII FILISMLDLS QQVFINAKCR GSPQCLPKCK EAIGKAAGKC MNGKCKCYP