ID   KA20_TITSE              Reviewed;          58 AA.
AC   P86271; A0A218QX02;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Potassium channel toxin Ts16 {ECO:0000303|PubMed:22238341, ECO:0000303|Ref.2};
DE   AltName: Full=Tityustoxin-16;
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:JAW06970.1, ECO:0000312|EMBL:JAW07001.1}
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 28-56, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Bordon K.C.F., Varanda W.A., Arantes E.C.;
RT   "Isolation and primary structure of a new scorpion toxin from Tityus
RT   serrulatus venom.";
RL   Submitted (MAR-2009) to UniProtKB.
RN   [3]
RP   MASS SPECTROMETRY, DOMAIN, DISULFIDE BONDS, AND STRUCTURE BY NMR OF 28-56.
RX   PubMed=22238341; DOI=10.1074/jbc.m111.329607;
RA   Saucedo A.L., Flores-Solis D., Rodriguez de la Vega R.C.,
RA   Ramirez-Cordero B., Hernandez-Lopez R., Cano-Sanchez P.,
RA   Noriega-Navarro R., Garcia-Valdes J., Coronas-Valderrama F., de Roodt A.,
RA   Brieba L.G., Possani L.D., Del Rio-Portilla F.;
RT   "New tricks of an old pattern: structural versatility of scorpion toxins
RT   with common cysteine spacing.";
RL   J. Biol. Chem. 287:12321-12330(2012).
CC   -!- FUNCTION: Blocks potassium channels. {ECO:0000250|UniProtKB:P0C183}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized
CC       by disulfide bonds (CSalpha/alpha 3(S-S)).
CC       {ECO:0000269|PubMed:22238341}.
CC   -!- MASS SPECTROMETRY: Mass=3325.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:22238341};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 20 subfamily. {ECO:0000255}.
CC   -!- CAUTION: The sequence aligns with alpha-KTx but has the CSalpha/alpha
CC       scaffold of a kappa-KTx due to the unusual pattern of disulfide bonds.
CC       As is the method of choice in UniProtKB, the assignment to the alpha-
CC       KTx 20 subfamily is based purely on the primary structure.
CC       {ECO:0000305}.
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DR   EMBL; GEUW01000075; JAW06970.1; -; mRNA.
DR   EMBL; GEUW01000044; JAW07001.1; -; mRNA.
DR   PDB; 2LO7; NMR; -; A=28-56.
DR   PDBsum; 2LO7; -.
DR   AlphaFoldDB; P86271; -.
DR   BMRB; P86271; -.
DR   SMR; P86271; -.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         17..58
FT                   /note="Potassium channel toxin Ts16"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000376049"
FT   DISULFID        29..51
FT                   /evidence="ECO:0000269|PubMed:22238341,
FT                   ECO:0007744|PDB:2LO7"
FT   DISULFID        34..47
FT                   /evidence="ECO:0000269|PubMed:22238341,
FT                   ECO:0007744|PDB:2LO7"
FT   DISULFID        38..53
FT                   /evidence="ECO:0000269|PubMed:22238341,
FT                   ECO:0007744|PDB:2LO7"
FT   HELIX           31..37
FT                   /evidence="ECO:0007829|PDB:2LO7"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:2LO7"
SQ   SEQUENCE   58 AA;  6634 MW;  B3D84680F2B5BCD8 CRC64;
     MHSSVFILIL FSLAVINPIF FDMKVEAGCM KEYCAGQCRG KVSQDYCLKH CKCIPRFI