ID   H9F01_CYRHA             Reviewed;          86 AA.
AC   D2Y2L8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Omega-theraphotoxin-Hhn1e;
DE            Short=Omega-TRTX-Hhn1e;
DE   AltName: Full=Hainantoxin-IX-6;
DE            Short=HNTX-IX-6;
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 GENOMIC DNA].
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: Ion channel inhibitor. {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. 17 (Hntx-9)
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: While it is structurally defined as a knottin it lacks the
CC       conserved Cys residue in position 71. {ECO:0000305}.
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DR   EMBL; GU293095; ADB56911.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2Y2L8; -.
DR   SMR; D2Y2L8; -.
DR   ArachnoServer; AS001517; omega-theraphotoxin-Hhn1e.
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   InterPro; IPR011696; Huwentoxin-1.
DR   Pfam; PF07740; Toxin_12; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..50
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000400669"
FT   PEPTIDE         51..86
FT                   /note="Omega-theraphotoxin-Hhn1e"
FT                   /id="PRO_0000400670"
FT   DISULFID        52..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..78
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   86 AA;  9668 MW;  058C0B6E7D66F9F0 CRC64;
     MKSIVFVALF GLALLAVVCS ASEGAHKELL KEVVRAMVVD KTDAVQAEER ECRWYLGGCS
     QDGDCCKHLQ RHSNYEWCIW DGTFSK