ID KKX32_HETPE Reviewed; 62 AA. AC P0DJ37; DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2012, sequence version 1. DT 11-DEC-2019, entry version 14. DE RecName: Full=Potassium channel toxin kappa-KTx 3.2 {ECO:0000303|PubMed:22305749}; DE AltName: Full=HSP040C.3 {ECO:0000303|PubMed:20443192}; DE Flags: Precursor; OS Heterometrus petersii (Asian forest scorpion). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Scorpioninae; 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 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: Potassium channel inhibitor (Kv). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}. CC -!- DOMAIN: Has the structural arrangement of two alpha-helices stabilized CC by two disulfide bonds (CSalpha/alpha 2(S-S)). CC {ECO:0000250|UniProtKB:P82850}. CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium CC channel inhibitor kappa-KTx family. Kappa-KTx 3 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR SMR; P0DJ37; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:GOC. PE 1: Evidence at protein level; KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; KW Potassium channel impairing toxin; Secreted; Signal; Toxin; KW Voltage-gated potassium channel impairing toxin. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT PROPEP 27..36 FT /evidence="ECO:0000250" FT /id="PRO_0000416804" FT PEPTIDE 38..62 FT /note="Potassium channel toxin kappa-KTx 3.2" FT /id="PRO_0000416805" FT DISULFID 43..61 FT /evidence="ECO:0000250|UniProtKB:P82850" FT DISULFID 47..57 FT /evidence="ECO:0000250|UniProtKB:P82850" SQ SEQUENCE 62 AA; 7029 MW; EEC3DBCD004A5519 CRC64; MKSTLMTASL LILVLLSIVD YASVYAELID SEISMERHWI NACFNICMKI SSDQKYCKSF CG //