ID   KBX2_TITCO              Reviewed;          47 AA.
AC   Q0GY42;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Potassium channel toxin TcoKIK;
OS   Tityus costatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=309814;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-29.
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   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15683865; DOI=10.1016/j.toxicon.2004.10.014;
RA   Diego-Garcia E., Batista C.V.F., Garcia-Gomez B.I., Lucas S., Candido D.M.,
RA   Gomez-Lagunas F., Possani L.D.;
RT   "The Brazilian scorpion Tityus costatus Karsch: genes, peptides and
RT   function.";
RL   Toxicon 45:273-283(2005).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=5278.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15683865};
CC   -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DQ465349; ABE98265.1; -; mRNA.
DR   PDB; 7LGL; NMR; -; A=1-47.
DR   PDBsum; 7LGL; -.
DR   AlphaFoldDB; Q0GY42; -.
DR   SMR; Q0GY42; -.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..47
FT                   /note="Potassium channel toxin TcoKIK"
FT                   /id="PRO_0000274683"
FT   DOMAIN          14..47
FT                   /note="BetaSPN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        17..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        24..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01209"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:7LGL"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:7LGL"
FT   HELIX           22..29
FT                   /evidence="ECO:0007829|PDB:7LGL"
FT   TURN            30..32
FT                   /evidence="ECO:0007829|PDB:7LGL"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:7LGL"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:7LGL"
SQ   SEQUENCE   47 AA;  5284 MW;  98E2D018CD9E87B0 CRC64;
     KIKSGWERLT SESEYACPAI DKFCEDHCAA KKAVGKCDDF KCNCIKL