ID   H8F01_CYRHA             Reviewed;          87 AA.
AC   D2Y2G7;
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=U3-theraphotoxin-Hhn1n;
DE            Short=U3-TRTX-Hhn1n;
DE   AltName: Full=Hainantoxin-VIII-6;
DE            Short=HNTX-VIII-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 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).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 53-87.
RX   PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA   Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA   Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA   Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA   Olson J.M., Strong R.K.;
RT   "Screening, large-scale production and structure-based classification of
RT   cystine-dense peptides.";
RL   Nat. Struct. Mol. Biol. 25:270-278(2018).
CC   -!- FUNCTION: Weakly inhibits Kv11.1/KCNH2/ERG1, Kv1.2/KCNA2, Kv1.3/KCNA3,
CC       and Kv2.1/KCNB1 (PubMed:29483648). {ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20192277}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:20192277}.
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. 51 (Hntx-8)
CC       subfamily. Hntx-8 sub-subfamily. {ECO:0000305}.
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DR   EMBL; GU293044; ADB56860.1; -; mRNA.
DR   AlphaFoldDB; D2Y2G7; -.
DR   SMR; D2Y2G7; -.
DR   ArachnoServer; AS001611; U3-theraphotoxin-Hhn1n.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0015459; F:potassium 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   3: Inferred from homology;
KW   Disulfide bond; Ion channel impairing toxin; Knottin;
KW   Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..52
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000400625"
FT   PEPTIDE         53..87
FT                   /note="U3-theraphotoxin-Hhn1n"
FT                   /id="PRO_0000400626"
FT   DISULFID        54..67
FT                   /evidence="ECO:0000250|UniProtKB:B3FIS6"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000250|UniProtKB:B3FIS6"
FT   DISULFID        66..79
FT                   /evidence="ECO:0000250|UniProtKB:B3FIS6"
SQ   SEQUENCE   87 AA;  10154 MW;  E9ABB657397BB8FE CRC64;
     MVNMKASMFL TFAGLVLLFV VCYASESEEK EFPKEMLSSI FAVDNDFKQE ERNCAGYMRE
     CKEKLCCSGY VCSSRWKWCV LPAPWRR