ID   VKT17_CYRHA             Reviewed;          76 AA.
AC   P0DJ66;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Kunitz-type serine protease inhibitor HNTX-03141017 {ECO:0000303|PubMed:18923708};
DE   Flags: Precursor; Fragment;
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 [MRNA].
RX   PubMed=18923708; DOI=10.1371/journal.pone.0003414;
RA   Yuan C.-H., He Q.-Y., Peng K., Diao J.-B., Jiang L.-P., Tang X.,
RA   Liang S.-P.;
RT   "Discovery of a distinct superfamily of Kunitz-type toxin (KTT) from
RT   tarantulas.";
RL   PLoS ONE 3:E3414-E3414(2008).
CC   -!- FUNCTION: Dual-function toxin that inhibits both serine proteases
CC       (trypsin) and voltage-gated potassium channels (Kv). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18923708}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18923708}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. 02 (native)
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DJ66; -.
DR   SMR; P0DJ66; -.
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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 4.10.410.10; -; 1.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF57362; SSF57362; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Ion channel impairing toxin;
KW   Potassium channel impairing toxin; Protease inhibitor; Secreted;
KW   Serine protease inhibitor; Signal; Toxin;
KW   Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          <1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..76
FT                   /note="Kunitz-type serine protease inhibitor HNTX-03141017"
FT                   /id="PRO_0000413809"
FT   DOMAIN          25..73
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            27
FT                   /note="May bind Kv1.x/KCNA"
FT                   /evidence="ECO:0000250"
FT   SITE            35..36
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        34..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        48..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   NON_TER         1
SQ   SEQUENCE   76 AA;  8848 MW;  1CBE519B2A8A2D53 CRC64;
     RLSVLRYYRR PDLRILPQET FEDTCRLPSD RGRCKASFER WYFNGRTCAK FIYGGCGGNG
     NKFPTQEACM KRCGKA