ID   KBX1_TITDI              Reviewed;          87 AA.
AC   Q0GY44;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Potassium channel toxin Tdi-beta-KTx;
DE            Short=TdibetaKTx;
DE   Flags: Precursor;
OS   Tityus discrepans (Venezuelan scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=57059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-74.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17141373; DOI=10.1016/j.peptides.2006.06.012;
RA   Diego-Garcia E., Schwartz E.F., D'Suze G., Gonzalez S.A., Batista C.V.,
RA   Garcia B.I., Rodriguez de la Vega R.C., Possani L.D.;
RT   "Wide phylogenetic distribution of scorpine and long-chain beta-KTx-like
RT   peptides in scorpion venoms: identification of 'orphan' components.";
RL   Peptides 28:31-37(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=19470401; DOI=10.1016/j.biochi.2009.05.005;
RA   D'Suze G., Schwartz E.F., Garcia-Gomez B.I., Sevcik C., Possani L.D.;
RT   "Molecular cloning and nucleotide sequence analysis of genes from a cDNA
RT   library of the scorpion Tityus discrepans.";
RL   Biochimie 91:1010-1019(2009).
RN   [3]
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=16705749; DOI=10.1002/pmic.200500525;
RA   Batista C.V.F., D'Suze G., Gomez-Lagunas F., Zamudio F.Z., Encarnacion S.,
RA   Sevcik C., Possani L.D.;
RT   "Proteomic analysis of Tityus discrepans scorpion venom and amino acid
RT   sequence of novel toxins.";
RL   Proteomics 6:3718-3727(2006).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=6822.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16705749};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ465347; ABE98263.1; -; mRNA.
DR   AlphaFoldDB; Q0GY44; -.
DR   SMR; Q0GY44; -.
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   Pfam; PF14866; Toxin_38; 1.
DR   PROSITE; PS51862; BSPN_CSAB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000269|PubMed:17141373"
FT                   /id="PRO_0000274676"
FT   CHAIN           28..87
FT                   /note="Potassium channel toxin Tdi-beta-KTx"
FT                   /id="PRO_0000274677"
FT   DOMAIN          53..87
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        56..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        63..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        67..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   87 AA;  9833 MW;  C0A6323AF4BF0372 CRC64;
     MERKLALLLL LGMITLASSG LREKHVQKLV TLIPNDTLRS IMKTIVHKLA KTQFGCPAYE
     GYCMNHCQDI ERHDGSCHGF KCKCEKS