JZ31C_CHIGU
ID JZ31C_CHIGU Reviewed; 86 AA.
AC P0CH56;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Mu-theraphotoxin-Cg2a 3 {ECO:0000305};
DE Short=Mu-TRTX-Cg2a {ECO:0000305};
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, FUNCTION, AMIDATION
RP AT PHE-84, 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 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 AlphaFoldDB; P0CH56; -.
DR SMR; P0CH56; -.
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_0000398465"
FT PEPTIDE 51..84
FT /note="Mu-theraphotoxin-Cg2a 3"
FT /evidence="ECO:0000269|PubMed:17476710,
FT ECO:0000269|PubMed:18848955"
FT /id="PRO_0000398466"
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; 9632 MW; 9D0BDC986434B8FF CRC64;
MKVSVVITLA VLGVMFVWAS AAELKERGSD QRDSPAWIKS MERIFQSEER ECTKFLGGCS
EDSECCPHLG CKDVLYYCAW DGTFGK