ID   H3B01_CYRHA             Reviewed;          83 AA.
AC   D2Y1Y4;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Mu-theraphotoxin-Hhn2j 1;
DE            Short=Mu-TRTX-Hhn2j;
DE   AltName: Full=Hainantoxin-III-2;
DE            Short=HNTX-III-2;
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].
RC   TISSUE=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).
CC   -!- FUNCTION: Lethal neurotoxin. Selectively blocks tetrodotoxin-sensitive
CC       voltage-gated sodium channels (Nav). Does not affect tetrodotoxin-
CC       resistant voltage-gated sodium channels or calcium channels (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 15 (Hntx-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   EMBL; GU292861; ADB56677.1; -; mRNA.
DR   AlphaFoldDB; D2Y1Y4; -.
DR   SMR; D2Y1Y4; -.
DR   ArachnoServer; AS001740; mu-theraphotoxin-Hhn2j.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011696; Huwentoxin-1.
DR   InterPro; IPR013140; Huwentoxin_CS1.
DR   Pfam; PF07740; Toxin_12; 1.
DR   PROSITE; PS60021; HWTX_1; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Neurotoxin; Presynaptic 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:0000250"
FT                   /id="PRO_0000400528"
FT   PEPTIDE         49..81
FT                   /note="Mu-theraphotoxin-Hhn2j 1"
FT                   /id="PRO_0000400529"
FT   MOD_RES         81
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..77
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  9137 MW;  A9866D3CB839B627 CRC64;
     MKASMFLALA GLVLLFVVGY ASESEEKEFP IELLSKIFAV DVFKGEERGC KGFGDSCTPG
     KNECCPNHAC SNKHKWCKVY LGK