JZTX2_CHIGU
ID JZTX2_CHIGU Reviewed; 63 AA.
AC B1P1B9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=U7-theraphotoxin-Cg1a;
DE Short=U7-TRTX-Cg1a;
DE AltName: Full=Jingzhaotoxin-2;
DE Short=JZTX-2;
DE AltName: Full=Peptide F2-32.19;
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 [MRNA], PROTEIN SEQUENCE OF 32-63, FUNCTION, MASS
RP SPECTROMETRY, AND TOXIN TARGET.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18840410; DOI=10.1016/j.bcp.2008.09.008;
RA Wang M., Liu Q., Luo H., Li J., Tang J., Xiao Y., Liang S.;
RT "Jingzhaotoxin-II, a novel tarantula toxin preferentially targets rat
RT cardiac sodium channel.";
RL Biochem. Pharmacol. 76:1716-1727(2008).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 32-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
CC -!- FUNCTION: Inhibits preferentially tetrodotoxin-insensitive sodium
CC currents (Nav) on rat cardiac myocytes (IC(50) is 0.26 uM) and has
CC weaker inhibition activity toward tetrodotoxin-sensitive sodium
CC currents on rat dorsal root ganglion (DRG) sensory neurons (IC(50) is
CC 0.83 uM) and on cockroach dorsal unpaired median (DUM) neurons (IC(50)
CC is 1.19 uM). Has no significant effect on potassium currents on DRG
CC neurons. {ECO:0000269|PubMed:18840410}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=3561.13; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18840410};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 36 (Jztx-2)
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; EU233850; ABY71669.1; -; mRNA.
DR AlphaFoldDB; B1P1B9; -.
DR SMR; B1P1B9; -.
DR ArachnoServer; AS000799; delta-theraphotoxin-Cg3a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..31
FT /evidence="ECO:0000269|PubMed:17476710,
FT ECO:0000269|PubMed:18840410"
FT /id="PRO_0000398392"
FT PEPTIDE 32..63
FT /note="U7-theraphotoxin-Cg1a"
FT /id="PRO_0000398393"
FT DISULFID 33..47
FT /evidence="ECO:0000250"
FT DISULFID 40..52
FT /evidence="ECO:0000250"
FT DISULFID 46..59
FT /evidence="ECO:0000250"
SQ SEQUENCE 63 AA; 7066 MW; B50089A75FF15054 CRC64;
MKTSILFVIF GLALLFALSV AIEMEEEETD RGCGTMWSPC STEKPCCDNF SCQPAIKWCI
WSP