VKT5_CYRSC
ID VKT5_CYRSC Reviewed; 88 AA.
AC P0DJ77; A0A023WBS8;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Kunitz-type kappaPI-theraphotoxin-Hs1a;
DE Short=KappaPI-TRTX-Hs1a;
DE AltName: Full=Huwentoxin HW11c5 {ECO:0000303|PubMed:24418069};
DE AltName: Full=Kunitz-type serine protease inhibitor HWTX-XI-IS5 {ECO:0000303|PubMed:18923708};
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 [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).
RN [2] {ECO:0000312|EMBL:AHY30307.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=24418069; DOI=10.1016/j.peptides.2014.01.001;
RA Jiang L., Deng M., Duan Z., Tang X., Liang S.;
RT "Molecular cloning, bioinformatics analysis and functional characterization
RT of HWTX-XI toxin superfamily from the spider Ornithoctonus huwena.";
RL Peptides 54:9-18(2014).
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 EMBL; KF160296; AHY30307.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DJ77; -.
DR BMRB; P0DJ77; -.
DR SMR; P0DJ77; -.
DR ArachnoServer; AS000326; kappa-theraphotoxin-Hs1a.
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_0000413828"
FT CHAIN 34..88
FT /note="Kunitz-type kappaPI-theraphotoxin-Hs1a"
FT /id="PRO_0000413829"
FT DOMAIN 37..85
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 39
FT /note="May bind Kv1.x/KCNA"
FT /evidence="ECO:0000250"
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; 9721 MW; 1A99CEA6DDD4F652 CRC64;
MGIARILSAV LFLSVLFVVT FPALLSADHH DGRIDTCRLP SDRGRCKASF ERWYFNGRTC
AKFIYGGCGG NGNKFPTQEA CMKRCAKA
