ID KBX3_HETLA Reviewed; 95 AA. AC P0C2F4; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 24-JAN-2024, entry version 35. DE RecName: Full=Heteroscorpine-1 {ECO:0000303|PubMed:17056081}; DE Short=HS-1 {ECO:0000303|PubMed:17056081}; DE Flags: Precursor; OS Heterometrus laoticus (Thai giant scorpion). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; OC Scorpiones; Iurida; Scorpionoidea; Scorpionidae; Heterometrinae; OC Heterometrus. OX NCBI_TaxID=217256; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20; 58-71 AND 80-86, RP FUNCTION, MASS SPECTROMETRY, TOXIC DOSE, AND SUBCELLULAR LOCATION. RC TISSUE=Venom; RX PubMed=17056081; DOI=10.1016/j.toxicon.2006.09.003; RA Uawonggul N., Thammasirirak S., Chaveerach A., Arkaravichien T., RA Bunyatratchata W., Ruangjirachuporn W., Jearranaiprepame P., Nakamura T., RA Matsuda M., Kobayashi M., Hattori S., Daduang S.; RT "Purification and characterization of Heteroscorpine-1 (HS-1) toxin from RT Heterometrus laoticus scorpion venom."; RL Toxicon 49:19-29(2007). CC -!- FUNCTION: Has antibacterial activity against B.subtilis, K.pneumoniae CC and P.aeruginosa. {ECO:0000269|PubMed:17056081}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17056081}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000305|PubMed:17056081}. CC -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:17056081}. CC -!- MASS SPECTROMETRY: Mass=8293; Method=MALDI; CC Evidence={ECO:0000269|PubMed:17056081}; CC -!- TOXIC DOSE: PD(50) is 80 ul to crickets (Gryllus sp). CC {ECO:0000269|PubMed:17056081}. CC -!- SIMILARITY: Belongs to the long chain scorpion toxin family. Class 3 CC 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 AlphaFoldDB; P0C2F4; -. DR SMR; P0C2F4; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; 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 Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond; KW Secreted; Signal; Toxin. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:17056081" FT CHAIN 20..95 FT /note="Heteroscorpine-1" FT /evidence="ECO:0000305|PubMed:17056081" FT /id="PRO_0000274680" FT DOMAIN 55..95 FT /note="BetaSPN-type CS-alpha/beta" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209" FT DISULFID 58..82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209" FT DISULFID 68..87 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209" FT DISULFID 72..89 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01209" SQ SEQUENCE 95 AA; 10246 MW; 21CCE2CD82EFFFA6 CRC64; MNSKLTALIF LGLVAIASCG WINEEKIQKK IDEKIGNNIL GGMAKAVVHK LAKGEFQCVA NIDTMGNCET HCQKTSGEKG FCHGTKCKCG KPLSY //