JZT1C_CHIGU
ID JZT1C_CHIGU Reviewed; 62 AA.
AC B1P1B8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Delta-theraphotoxin-Cg1a 3 {ECO:0000305};
DE Short=Delta-TRTX-Cg1a {ECO:0000305};
DE AltName: Full=Jingzhaotoxin-1.3 {ECO:0000305};
DE Short=JZTX-1.3 {ECO:0000305};
DE AltName: Full=Jingzhaotoxin-I.3 {ECO:0000305};
DE Short=JZTX-I.3 {ECO:0000312|EMBL:ABY71668.1};
DE AltName: Full=Peptide F5-24.92 {ECO:0000303|PubMed:17476710};
DE Flags: Precursor;
OS Chilobrachys guangxiensis (Chinese earth tiger tarantula) (Chilobrachys
OS jingzhao).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Chilobrachys.
OX NCBI_TaxID=278060;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Venom gland;
RX PubMed=18581053; DOI=10.1007/s00018-008-8135-x;
RA Chen J., Deng M., He Q., Meng E., Jiang L., Liao Z., Rong M., Liang S.;
RT "Molecular diversity and evolution of cystine knot toxins of the tarantula
RT Chilobrachys jingzhao.";
RL Cell. Mol. Life Sci. 65:2431-2444(2008).
RN [2]
RP PROTEIN SEQUENCE OF 30-62, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=17476710; DOI=10.1002/pmic.200600785;
RA Liao Z., Cao J., Li S., Yan X., Hu W., He Q., Chen J., Tang J., Xie J.,
RA Liang S.;
RT "Proteomic and peptidomic analysis of the venom from Chinese tarantula
RT Chilobrachys jingzhao.";
RL Proteomics 7:1892-1907(2007).
RN [3]
RP FUNCTION, AND BIOASSAY.
RC TISSUE=Venom;
RX PubMed=17150181; DOI=10.1016/j.bbrc.2006.11.086;
RA Yuan C., Yang S., Liao Z., Liang S.;
RT "Effects and mechanism of Chinese tarantula toxins on the Kv2.1 potassium
RT channels.";
RL Biochem. Biophys. Res. Commun. 352:799-804(2007).
RN [4]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=17618665; DOI=10.1016/j.toxicon.2007.04.018;
RA Xiao Y.-C., Li J., Deng M., Dai C.-L., Liang S.-P.;
RT "Characterization of the excitatory mechanism induced by Jingzhaotoxin-I
RT inhibiting sodium channel inactivation.";
RL Toxicon 50:507-517(2007).
RN [5]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=23246579; DOI=10.1016/j.toxicon.2012.12.001;
RA Tao H., Wu Y., Deng M., He J., Wang M., Xiao Y., Liang S.;
RT "Molecular determinants for the tarantula toxin jingzhaotoxin-I interacting
RT with potassium channel Kv2.1.";
RL Toxicon 63:129-136(2013).
RN [6]
RP FUNCTION.
RX PubMed=26721415; DOI=10.1016/j.toxicon.2015.12.009;
RA Tao H., Chen X., Lu M., Wu Y., Deng M., Zeng X., Liu Z., Liang S.;
RT "Molecular determinant for the tarantula toxin Jingzhaotoxin-I slowing the
RT fast inactivation of voltage-gated sodium channels.";
RL Toxicon 111:13-21(2016).
RN [7]
RP STRUCTURE BY NMR OF 30-62, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=16077905; DOI=10.1111/j.1745-7270.2005.00078.x;
RA Zeng X.-Z., Zhu Q., Liang S.-P.;
RT "Sequence-specific assignment of 1H-NMR resonance and determination of the
RT secondary structure of Jingzhaotoxin-I.";
RL Acta Biochim. Biophys. Sin. 37:567-572(2005).
CC -!- FUNCTION: Moderately inhibits voltage-gated sodium channels and weakly
CC inhibits voltage-gated potassium channel (PubMed:17150181,
CC PubMed:17618665, PubMed:23246579, PubMed:26721415). Inhibits the
CC inactivation of rat Nav1.2/SCN2A (IC(50)=870 nM), rat Nav1.3/SCN3A
CC (IC(50)=845 nM), rat Nav1.4/SCN4A (IC(50)=339 nM), human Nav1.5/SCN5A
CC (IC(50)=335 nM) and human Nav1.7/SCN9A sodium channels (IC(50)=348 nM)
CC (PubMed:26721415). The toxin delays the inactivation of sodium channels
CC without affecting the activation and steady-state inactivation kinetics
CC in the physiological range of voltages (PubMed:26721415). Site-directed
CC mutagenesis of the sodium channel indicates that the toxin interacts
CC with site 3 located at the extracellular S3-S4 linker of domain IV
CC (PubMed:26721415). On potassium channels, it inhibits activation of
CC channels with an IC(50) of 8.05 uM through a voltage sensor-trapping
CC mechanism (PubMed:23246579). It increases muscle contraction in several
CC assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens)
CC and is suggested to act both presynaptically and postsynaptically
CC (PubMed:17618665). {ECO:0000269|PubMed:17150181,
CC ECO:0000269|PubMed:17618665, ECO:0000269|PubMed:23246579,
CC ECO:0000269|PubMed:26721415}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17476710}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17476710}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000269|PubMed:16077905}.
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 33 (Jztx-1)
CC subfamily. {ECO:0000305}.
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DR EMBL; EU233849; ABY71668.1; -; mRNA.
DR AlphaFoldDB; B1P1B8; -.
DR SMR; B1P1B8; -.
DR ArachnoServer; AS000045; delta-theraphotoxin-Cg1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR Pfam; PF07740; Toxin_12; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Knottin; Neurotoxin; Postsynaptic neurotoxin;
KW Potassium channel impairing toxin; Presynaptic neurotoxin; Secreted;
KW Signal; Toxin; Voltage-gated potassium channel impairing toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..29
FT /evidence="ECO:0000269|PubMed:17476710"
FT /id="PRO_0000398390"
FT PEPTIDE 30..62
FT /note="Delta-theraphotoxin-Cg1a 3"
FT /evidence="ECO:0000269|PubMed:17476710"
FT /id="PRO_0000398391"
FT DISULFID 31..46
FT /evidence="ECO:0000269|PubMed:16077905"
FT DISULFID 38..51
FT /evidence="ECO:0000269|PubMed:16077905"
FT DISULFID 45..58
FT /evidence="ECO:0000269|PubMed:16077905"
SQ SEQUENCE 62 AA; 6906 MW; 4DF86F039E17816B CRC64;
MKTSILFVIF SLALVFALSP ATEIEETDRA CGQFWWKCGE GKPPCCANFA CKIGLYLCIW
SP
