ID   KAX2K_CENTE             Reviewed;          62 AA.
AC   P0DUI4;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Toxin Ct28 {ECO:0000303|PubMed:23840487};
DE   AltName: Full=Potassium channel toxin alpha-KTx 2 {ECO:0000305};
DE   Flags: Precursor;
OS   Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=1028682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-46, PROBABLE AMIDATION
RP   AT ASN-61, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23840487; DOI=10.1371/journal.pone.0066486;
RA   Valdez-Velazquez L.L., Quintero-Hernandez V., Romero-Gutierrez M.T.,
RA   Coronas F.I., Possani L.D.;
RT   "Mass fingerprinting of the venom and transcriptome of venom gland of
RT   scorpion Centruroides tecomanus.";
RL   PLoS ONE 8:e66486-e66486(2013).
CC   -!- FUNCTION: Blocks voltage-gated potassium channels.
CC       {ECO:0000250|UniProtKB:P0C161}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23840487}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23840487}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC       beta-sheet by disulfide bonds (CSalpha/beta). {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4255; Method=Electrospray; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:23840487};
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 02 subfamily. {ECO:0000305}.
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DR   EMBL; JZ122292; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DUI4; -.
DR   SMR; P0DUI4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   CHAIN           23..61
FT                   /note="Toxin Ct28"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT                   /id="PRO_0000452431"
FT   SITE            50
FT                   /note="Basic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   SITE            59
FT                   /note="Aromatic residue of the functional dyad"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         61
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000305|PubMed:23840487"
FT   DISULFID        29..51
FT                   /evidence="ECO:0000250|UniProtKB:P08815"
FT   DISULFID        35..56
FT                   /evidence="ECO:0000250|UniProtKB:P08815"
FT   DISULFID        39..58
FT                   /evidence="ECO:0000250|UniProtKB:P08815"
SQ   SEQUENCE   62 AA;  6883 MW;  4278E22B00BA5106 CRC64;
     MKAFYGILII LLFCSMFKLN ESTTINVKCT SPKQCLKPCK DLYGPHAGAK CMNGKCKCYN
     NG