ID   VKT11_CYRSC             Reviewed;          88 AA.
AC   B2ZBB6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Kunitz-type kappaPI-theraphotoxin-Hs1b;
DE            Short=KappaPI-TRTX-Hs1b;
DE   AltName: Full=Kunitz-type serine protease inhibitor huwentoxin-11g11;
DE            Short=HW11g11;
DE   Flags: Precursor;
OS   Cyriopagopus schmidti (Chinese bird spider) (Haplopelma schmidti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Cyriopagopus.
OX   NCBI_TaxID=29017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18590782; DOI=10.1016/j.peptides.2008.06.001;
RA   Jiang L., Chen J., Peng L., Zhang Y., Xiong X., Liang S.;
RT   "Genomic organization and cloning of novel genes encoding toxin-like
RT   peptides of three superfamilies from the spider Orinithoctonus huwena.";
RL   Peptides 29:1679-1684(2008).
CC   -!- FUNCTION: Serine protease inhibitor that inhibits trypsin and blocks
CC       voltage-gated potassium channels (Kv). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. 02 (native)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; EU635744; ACD01236.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2ZBB6; -.
DR   SMR; B2ZBB6; -.
DR   MEROPS; I02.968; -.
DR   ArachnoServer; AS000458; kappa-theraphotoxin-Hs1b.
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   3: Inferred from homology;
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..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..33
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380160"
FT   CHAIN           34..88
FT                   /note="Kunitz-type kappaPI-theraphotoxin-Hs1b"
FT                   /id="PRO_0000380161"
FT   DOMAIN          37..85
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   SITE            47..48
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        46..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DISULFID        60..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ   SEQUENCE   88 AA;  9707 MW;  1A99CB06DDD4F652 CRC64;
     MGIARILSAV LFLSVLFVVT FPALLSADHH DGRIDTCRLP SDRGRCKASF ERWYFNGRTC
     AKFIYGGCGG NGNKFPTQEA CMKRCGKA