ID   H17A3_CYRHA             Reviewed;          98 AA.
AC   D2Y2C8;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Hainantoxin-XVII.3;
DE            Short=HNTX-XVII.3;
DE   AltName: Full=Peptide F2-20.97;
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], PROTEIN SEQUENCE OF 65-98,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and 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 65-98.
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: Inhibits with low potency Kv1.2/KCNA2 and Kv1.3/KCNA3
CC       voltage-gated potassium channels(PubMed:29483648).
CC       {ECO:0000269|PubMed:29483648}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|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 hainantoxin family. 17 subfamily.
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DR   EMBL; GU293005; ADB56821.1; -; mRNA.
DR   AlphaFoldDB; D2Y2C8; -.
DR   ArachnoServer; AS001987; U12-theraphotoxin-Hhn1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   PROPEP          41..64
FT                   /evidence="ECO:0000305|PubMed:20192277"
FT                   /id="PRO_0000401031"
FT   PEPTIDE         65..98
FT                   /note="Hainantoxin-XVII.3"
FT                   /evidence="ECO:0000269|PubMed:20192277"
FT                   /id="PRO_0000401032"
FT   DISULFID        66..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..95
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   98 AA;  11153 MW;  FCCA83031942A79B CRC64;
     MTTVGVSLFR RSPEKITMKI ATFLGLSFLL IASYFLICEA QHPGFQELLI LEENMRDPEN
     SKERSCAKPR ENCNRMNILC CRGECVCPTF GDCFCYGD