ID   H4C01_CYRHA             Reviewed;          86 AA.
AC   D2Y235;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Mu-theraphotoxin-Hhn1d;
DE            Short=Mu-TRTX-Hhn1d;
DE   AltName: Full=Hainantoxin-IV-3;
DE            Short=HNTX-IV-3;
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: Neurotoxin. Selectively blocks neuronal tetrodotoxin-
CC       sensitive voltage-gated sodium channels (Nav). Does not affect
CC       tetrodotoxin-resistant voltage-gated sodium channels or calcium
CC       channels. {ECO:0000250|UniProtKB:D2Y232}.
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. 22 (Htx-4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GU292912; ADB56728.1; -; mRNA.
DR   AlphaFoldDB; D2Y235; -.
DR   BMRB; D2Y235; -.
DR   SMR; D2Y235; -.
DR   ArachnoServer; AS001927; mu-theraphotoxin-Hhn1d.
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..49
FT                   /evidence="ECO:0000250|UniProtKB:D2Y232"
FT                   /id="PRO_0000400574"
FT   PEPTIDE         50..84
FT                   /note="Mu-theraphotoxin-Hhn1d"
FT                   /id="PRO_0000400575"
FT   MOD_RES         84
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..66
FT                   /evidence="ECO:0000250|UniProtKB:D2Y232"
FT   DISULFID        58..73
FT                   /evidence="ECO:0000250|UniProtKB:D2Y232"
FT   DISULFID        65..80
FT                   /evidence="ECO:0000250|UniProtKB:D2Y232"
SQ   SEQUENCE   86 AA;  9478 MW;  9498BA67C83CB6DD CRC64;
     MKASMFLALA GLALLFVVCY ASESEEKEFS NELLSSVLAV DDNSKGEERE CLGFGKGCNP
     SSDQCCKSSN LVCSRKHRWC KYEIGK