KKX28_HETPE
ID KKX28_HETPE Reviewed; 61 AA.
AC P0DJ35;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Potassium channel toxin kappa-KTx 2.8 {ECO:0000303|PubMed:22305749};
DE AltName: Full=HSP053C.2 {ECO:0000303|PubMed:20443192};
DE AltName: Full=Toxin HeTx204 {ECO:0000303|PubMed:22511981};
DE AltName: Full=Toxin kappa-KTx 2.7 {ECO:0000303|PubMed:22511981};
DE Flags: Precursor; Fragment;
OS Heterometrus petersii (Asian forest scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae;
OC Heterometrus.
OX NCBI_TaxID=754296;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=20443192; DOI=10.1002/pmic.200900763;
RA Ma Y., Zhao Y., Zhao R., Zhang W., He Y., Wu Y., Cao Z., Guo L., Li W.;
RT "Molecular diversity of toxic components from the scorpion Heterometrus
RT petersii venom revealed by proteomic and transcriptome analysis.";
RL Proteomics 10:2471-2485(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=22511981; DOI=10.1371/journal.pone.0035154;
RA Chen Z.Y., Zeng D.Y., Hu Y.T., He Y.W., Pan N., Ding J.P., Cao Z.J.,
RA Liu M.L., Li W.X., Yi H., Jiang L., Wu Y.L.;
RT "Structural and functional diversity of acidic scorpion potassium channel
RT toxins.";
RL PLoS ONE 7:E35154-E35154(2012).
RN [3]
RP NOMENCLATURE.
RX PubMed=22305749; DOI=10.1016/j.bcp.2012.01.021;
RA Vandendriessche T., Kopljar I., Jenkins D.P., Diego-Garcia E.,
RA Abdel-Mottaleb Y., Vermassen E., Clynen E., Schoofs L., Wulff H.,
RA Snyders D., Tytgat J.;
RT "Purification, molecular cloning and functional characterization of HelaTx1
RT (Heterometrus laoticus): the first member of a new kappa-KTX subfamily.";
RL Biochem. Pharmacol. 83:1307-1317(2012).
CC -!- FUNCTION: Voltage-gated potassium channel inhibitor (Kv) that acts on
CC Kv1.3/KCNA3 and Kv7.1/KCNQ1. 1 uM of the toxin inhibits Kv1.3/KCNA3
CC currents by 35.1%, whereas 10 uM of the toxin inhibits Kv7.1/KCNQ1
CC currents by 44.9%. {ECO:0000269|PubMed:22511981}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized
CC by disulfide bonds (CSalpha/alpha 2(S-S)).
CC {ECO:0000250|UniProtKB:P0C1Z3}.
CC -!- MISCELLANEOUS: Does not show activity on ion channels KCa2.3/KCNN3,
CC TRPV1, and KCa1.1/KCNMA1. {ECO:0000305|PubMed:22511981}.
CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC channel inhibitor kappa-KTx family. Kappa-KTx 2 subfamily.
CC {ECO:0000305}.
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DR EMBL; FD664204; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DJ35; -.
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 Cleavage on pair of basic residues; 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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..35
FT /evidence="ECO:0000250"
FT /id="PRO_0000416800"
FT PEPTIDE 38..61
FT /note="Potassium channel toxin kappa-KTx 2.8"
FT /id="PRO_0000416801"
FT DISULFID 41..59
FT /evidence="ECO:0000250|UniProtKB:P0C1Z3"
FT DISULFID 45..55
FT /evidence="ECO:0000250|UniProtKB:P0C1Z3"
FT NON_TER 1
SQ SEQUENCE 61 AA; 6748 MW; E31C93C933D42CBE CRC64;
GTVYVFLLLL AFGIFTDISN ACSEQMDDED SYEVEKRGNA CIEVCLQHTG NPAECDKPCD
K