ID   H16O1_CYRHA             Reviewed;         113 AA.
AC   D2Y285;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=U11-theraphotoxin-Hhn1o;
DE            Short=U11-TRTX-Hhn1o;
DE   AltName: Full=Hainantoxin-XVI-15;
DE            Short=HNTX-XVI-15;
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: Probable 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 14 (magi-1) family. 01 (HNTX-16)
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: While it is structurally defined as a knottin it lacks the
CC       conserved Cys residue in position 110. {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; GU292962; ADB56778.1; -; mRNA.
DR   AlphaFoldDB; D2Y285; -.
DR   SMR; D2Y285; -.
DR   ArachnoServer; AS001936; U11-theraphotoxin-Hhn1o.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012627; Toxin_22.
DR   Pfam; PF08092; Toxin_22; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..74
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000400945"
FT   PEPTIDE         75..113
FT                   /note="U11-theraphotoxin-Hhn1o"
FT                   /id="PRO_0000400946"
FT   REGION          61..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        75..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   113 AA;  13149 MW;  9E302772A19337E6 CRC64;
     MNTVRVTFLL VFVLAVSLGQ ADKDENRMEM QEKTEQGKSY LDFAENLLLQ KLEELEAKLL
     EEDSEESRNS RQKRCIGEGV PCDENDPRCC SGLVCLKPTL HGIWYKSYYY YKK