ID KAX33_LEIHE Reviewed; 38 AA. AC P46112; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 22-FEB-2023, entry version 86. DE RecName: Full=Potassium channel toxin alpha-KTx 3.3; DE AltName: Full=Agitoxin-3; DE Short=AgTx-3; DE Short=AgTx3; OS Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus OS hebraeus). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus. OX NCBI_TaxID=6884; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Venom; RX PubMed=8204618; DOI=10.1021/bi00188a012; RA Garcia M.L., Garcia-Calvo M., Hidalgo P., Lee A., Mackinnon R.; RT "Purification and characterization of three inhibitors of voltage-dependent RT K+ channels from Leiurus quinquestriatus var. hebraeus venom."; RL Biochemistry 33:6834-6839(1994). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16551474; DOI=10.1016/j.toxicon.2006.01.015; RA Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A., RA Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E., RA Pimenta A.M.C.; RT "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering RT analyses to infer phylogenetic relationships in some scorpions from the RT Buthidae family (Scorpiones)."; RL Toxicon 47:628-639(2006). CC -!- FUNCTION: Potent inhibitor of shaker potassium channels as well as the CC mammalian homologs of shaker. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta). CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium CC channel inhibitor family. Alpha-KTx 03 subfamily. {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 PIR; C54471; C54471. DR AlphaFoldDB; P46112; -. DR BMRB; P46112; -. DR SMR; P46112; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. 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; Knottin, scorpion toxin-like; 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; Scorpion toxin-like; 1. DR PROSITE; PS01138; SCORP_SHORT_TOXIN; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin; KW Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin. FT PEPTIDE 1..38 FT /note="Potassium channel toxin alpha-KTx 3.3" FT /id="PRO_0000044927" FT REGION 26..33 FT /note="Interaction with Ca(2+)-activated K(+) channels" FT /evidence="ECO:0000255" FT DISULFID 8..28 FT /evidence="ECO:0000250" FT DISULFID 14..33 FT /evidence="ECO:0000250" FT DISULFID 18..35 FT /evidence="ECO:0000250" SQ SEQUENCE 38 AA; 4107 MW; E5945513F87B51CE CRC64; GVPINVPCTG SPQCIKPCKD AGMRFGKCMN RKCHCTPK //