位置:首页 > 蛋白库 > VKT4_CYRSC
VKT4_CYRSC
ID   VKT4_CYRSC              Reviewed;          88 AA.
AC   P0DJ76; A0A023WBH6;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Kunitz-type kappaPI-theraphotoxin-Hs1e;
DE            Short=KappaPI-TRTX-Hs1e;
DE   AltName: Full=Huwentoxin HW11c4 {ECO:0000303|PubMed:24418069};
DE   AltName: Full=Kunitz-type serine protease inhibitor HWTX-XI-IS4 {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:AHY30306.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND RECOMBINANT EXPRESSION.
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: Toxin that shows weak activity against voltage-gated
CC       potassium channels (Kv), and no activity against serine proteases
CC       (PubMed:24418069). The recombinant toxin shows a weak inhibition on
CC       Kv1.1/KCNA1 (59.2% inhibition at 10 uM) (PubMed:24418069).
CC       {ECO:0000269|PubMed:24418069}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18923708}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18923708}.
CC   -!- MISCELLANEOUS: The recombinant toxin does not show activity on
CC       Kv1.2/KCNA2, Kv1.3/KCNA3, Kv2.1/KCNB1 and Kv4.3/KCND3 channels, as well
CC       as on calcium (Cav) and sodium channels (Nav). It also does not show
CC       detectable activity against trypsin, kallikrein, chymotrypsin, and
CC       thrombin. {ECO:0000269|PubMed:24418069}.
CC   -!- SIMILARITY: Belongs to the venom Kunitz-type family. 02 (native)
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KF160295; AHY30306.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0DJ76; -.
DR   SMR; P0DJ76; -.
DR   ArachnoServer; AS001843; kappa-theraphotoxin-Hs1e.
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_0000413826"
FT   CHAIN           34..88
FT                   /note="Kunitz-type kappaPI-theraphotoxin-Hs1e"
FT                   /id="PRO_0000413827"
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;  9747 MW;  1A86EB72DDD4E94D CRC64;
     MGIARILSAV LFLSVLFVVT FPALLLADHH DGRIDTCRLP SDRGRCKASF ERWYFNGRTC
     AKFIYGGCGG NGNKFPTEKA CMKRCAKA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024