ID   JZ31A_CHIGU             Reviewed;          86 AA.
AC   B1P1F4;
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=Mu-theraphotoxin-Cg2a 1 {ECO:0000305};
DE            Short=Mu-TRTX-Cg2a {ECO:0000305};
DE   AltName: Full=Jingzhaotoxin-31 {ECO:0000305};
DE            Short=JZTX-31 {ECO:0000312|EMBL:ABY71704.1};
DE   AltName: Full=Jingzhaotoxin-IV {ECO:0000303|PubMed:18848955};
DE            Short=JZTX-IV {ECO:0000303|PubMed:18848955};
DE   AltName: Full=Peptide F1-23.73 {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 [MRNA], PROTEIN SEQUENCE OF 51-84, AMIDATION AT PHE-84,
RP   FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18848955; DOI=10.1016/j.toxicon.2008.08.018;
RA   Wang M., Diao J., Li J., Tang J., Lin Y., Hu W., Zhang Y., Xiao Y.,
RA   Liang S.;
RT   "JZTX-IV, a unique acidic sodium channel toxin isolated from the spider
RT   Chilobrachys jingzhao.";
RL   Toxicon 52:871-880(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 51-84, MASS SPECTROMETRY, AMIDATION AT PHE-84, 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).
CC   -!- FUNCTION: Inhibits both peak current and fast inactivation of voltage-
CC       gated sodium channels (Nav) channels. Inhibits the inactivation of Nav
CC       on DRG neurons (EC(50)=1.77 uM) and peak current of cardiac myocytes
CC       (IC(50)=0.90 uM). {ECO:0000269|PubMed:18848955}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17476710,
CC       ECO:0000269|PubMed:18848955}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17476710, ECO:0000305|PubMed:18848955}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:B1P1E1}.
CC   -!- MASS SPECTROMETRY: Mass=3774.88; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:18848955};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 37 (Jztx-31)
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; EU233885; ABY71704.1; -; mRNA.
DR   AlphaFoldDB; B1P1F4; -.
DR   SMR; B1P1F4; -.
DR   ArachnoServer; AS000832; delta-theraphotoxin-Cg2a.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..50
FT                   /evidence="ECO:0000269|PubMed:17476710,
FT                   ECO:0000269|PubMed:18848955"
FT                   /id="PRO_0000398461"
FT   PEPTIDE         51..84
FT                   /note="Mu-theraphotoxin-Cg2a 1"
FT                   /evidence="ECO:0000269|PubMed:17476710,
FT                   ECO:0000269|PubMed:18848955"
FT                   /id="PRO_0000398462"
FT   MOD_RES         84
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:17476710,
FT                   ECO:0000269|PubMed:18848955"
FT   DISULFID        52..66
FT                   /evidence="ECO:0000250|UniProtKB:B1P1E1"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000250|UniProtKB:B1P1E1"
FT   DISULFID        65..78
FT                   /evidence="ECO:0000250|UniProtKB:B1P1E1"
SQ   SEQUENCE   86 AA;  9647 MW;  8B45E95D6F99B6FF CRC64;
     MKVSVVITLA VLGIMFVWAS AAELEERGSD QRDSPAWLKS MERIFQSEER ECTKFLGGCS
     EDSECCPHLG CKDVLYYCAW DGTFGK