VKT39_CYRSC
ID VKT39_CYRSC Reviewed; 88 AA.
AC P0DMJ1; A0A023WB37;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Kunitz-type U15-theraphotoxin-Hs1g;
DE Short=U15-TRTX-Hs1g;
DE AltName: Full=Huwentoxin HW11c39 {ECO:0000303|PubMed:24418069};
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], AND RECOMBINANT EXPRESSION.
RC TISSUE=Venom gland;
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: Protein with unknown function. {ECO:0000305|PubMed:24418069}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24418069}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24418069}.
CC -!- MISCELLANEOUS: The recombinant protein does not show activity on
CC Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3, Kv2.1/KCNB1 and Kv4.3/KCND3
CC channels, as well as calcium (Cav) and sodium channels (Nav). It also
CC does not show detectable activity against chymotrypsin, trypsin
CC kallikrein, and thrombin. {ECO:0000269|PubMed:24418069}.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. 03 (sub-Kunitz)
CC subfamily. {ECO:0000305}.
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DR EMBL; KF160307; AHY30318.1; -; Genomic_DNA.
DR AlphaFoldDB; P0DMJ1; -.
DR SMR; P0DMJ1; -.
DR ArachnoServer; AS001773; U15-theraphotoxin-Hs1g.
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.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..33
FT /evidence="ECO:0000250"
FT /id="PRO_0000429347"
FT CHAIN 34..88
FT /note="Kunitz-type U15-theraphotoxin-Hs1g"
FT /id="PRO_0000429348"
FT DOMAIN 37..85
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
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; 9719 MW; 52E704677968AF06 CRC64;
MGTARFLSAV LLLSVLLMVT FPALLSAEYH DGRVDICSLP SDSGDCLRFF EMWYFDGTTC
TKFVYGGCGG NDNRFPTEKA CMKRCAKA
