ID   KIK2_TITDI              Reviewed;          91 AA.
AC   Q0GY43;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Potassium channel toxin TdiKIK;
DE            Short=TdKIK;
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].
RC   TISSUE=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, AND SUBCELLULAR LOCATION.
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:0000269|PubMed:16705749}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16705749}.
CC   -!- MASS SPECTROMETRY: Mass=5221.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16705749};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ465348; ABE98264.1; -; mRNA.
DR   AlphaFoldDB; Q0GY43; -.
DR   SMR; Q0GY43; -.
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   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..44
FT                   /id="PRO_0000274684"
FT   CHAIN           45..91
FT                   /note="Potassium channel toxin TdiKIK"
FT                   /id="PRO_0000274685"
FT   DOMAIN          58..91
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        61..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        72..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
SQ   SEQUENCE   91 AA;  9960 MW;  772D439D161F0BAD CRC64;
     MVATNRCCVF ALLVALLLIH SLAEAGKGKE VLGKIKNKLV EVKEKIKAGW DKLTSKSEYA
     CPVIDKFCED HCAAKNAIGK CDDFKCQCLN S