ID H1A02_CYRHA Reviewed; 83 AA. AC D2Y1X7; P83591; DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot. DT 02-MAR-2010, sequence version 1. DT 11-DEC-2019, entry version 27. DE RecName: Full=Mu-theraphotoxin-Hhn2b 2; DE Short=Mu-TRTX-Hhn2b; DE AltName: Full=Hainantoxin-1.2; DE AltName: Full=Hainantoxin-I.2; DE Short=HnTx-I.2; DE AltName: Full=Peptide F5-19.03; DE Flags: Precursor; OS Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae; OC Mygalomorphae; Theraphosidae; Haplopelma. OX NCBI_TaxID=209901; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], PROTEIN SEQUENCE OF 49-81, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Venom, and Venom gland; RX PubMed=20192277; DOI=10.1021/pr1000016; RA Tang X., Zhang Y., Hu W., Xu D., Tao H., Yang X., Li Y., Jiang L., RA Liang S.; RT "Molecular diversification of peptide toxins from the tarantula Haplopelma RT hainanum (Ornithoctonus hainana) venom based on transcriptomic, peptidomic, RT and genomic analyses."; RL J. Proteome Res. 9:2550-2564(2010). RN [2] RP PROTEIN SEQUENCE OF 49-81. RC TISSUE=Venom; RX PubMed=12727268; DOI=10.1016/s0041-0101(02)00280-5; RA Xiao Y.-C., Liang S.-P.; RT "Purification and characterization of Hainantoxin-V, a tetrodotoxin- RT sensitive sodium channel inhibitor from the venom of the spider RT Selenocosmia hainana."; RL Toxicon 41:643-650(2003). RN [3] RP SEQUENCE REVISION TO 78-81, FUNCTION, TOXIN TARGET, SUBUNIT, SUBCELLULAR RP LOCATION, MASS SPECTROMETRY, DISULFIDE BONDS, AMIDATION AT LEU-81, AND RP STRUCTURE BY NMR. RC TISSUE=Venom; RX PubMed=14675784; DOI=10.1016/s0014-5793(03)01303-6; RA Li D.-L., Xiao Y.-C., Hu W.-J., Xie J.-Y., Bosmans F., Tytgat J., RA Liang S.-P.; RT "Function and solution structure of hainantoxin-I, a novel insect sodium RT channel inhibitor from the Chinese bird spider Selenocosmia hainana."; RL FEBS Lett. 555:616-622(2003). CC -!- FUNCTION: Is a depressant toxin. Blocks the SCN2A/SCN1B (Nav1.2/Beta1) CC sodium channel receptor (IC(50) is 68 +-6 uM) and the insect sodium CC channel para/tipE (IC(50) is 4.3 +-0.3 uM), without altering the CC activation or inactivation kinetics. {ECO:0000269|PubMed:14675784}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14675784}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC {ECO:0000269|PubMed:14675784}. CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin. CC {ECO:0000269|PubMed:14675784}. CC -!- MASS SPECTROMETRY: Mass=3608.02; Method=MALDI; CC Evidence={ECO:0000269|PubMed:14675784}; CC -!- MISCELLANEOUS: Several genes are coding for Mu-theraphotoxin-Hhn2b for CC which the structure by NMR has been determined. The cross-references to CC PDB can be found in entry AC D2Y1X6. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 14 (Hntx-1) 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 EMBL; GU292854; ADB56670.1; -; mRNA. DR SMR; D2Y1X7; -. DR ArachnoServer; AS000338; mu-theraphotoxin-Hhn2b. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0009405; P:pathogenesis; IEA:InterPro. DR InterPro; IPR011696; Huwentoxin-1. DR InterPro; IPR013140; Huwentoxin_CS1. DR Pfam; PF07740; Toxin_12; 1. DR PROSITE; PS60021; HWTX_1; 1. PE 1: Evidence at protein level; KW Amidation; Direct protein sequencing; Disulfide bond; KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin; KW Voltage-gated sodium channel impairing toxin. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT PROPEP 22..48 FT /evidence="ECO:0000269|PubMed:12727268, FT ECO:0000269|PubMed:20192277" FT /id="PRO_0000400496" FT PEPTIDE 49..81 FT /note="Mu-theraphotoxin-Hhn2b 2" FT /id="PRO_0000400497" FT MOD_RES 81 FT /note="Leucine amide" FT /evidence="ECO:0000269|PubMed:14675784" FT DISULFID 50..65 FT /evidence="ECO:0000269|PubMed:14675784" FT DISULFID 57..70 FT /evidence="ECO:0000269|PubMed:14675784" FT DISULFID 64..77 FT /evidence="ECO:0000269|PubMed:14675784" SQ SEQUENCE 83 AA; 9270 MW; A72E5B88A1E04933 CRC64; MKASMFLALA GLVLLFVVCY ASESEEKEFP RELISKIFTV DDFKGEEREC KGFGKSCVPG KNECCSGYAC NSRDKWCKVL LGK //