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JZ11B_CHIGU
ID   JZ11B_CHIGU             Reviewed;          86 AA.
AC   B1P1E1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Kappa-theraphotoxin-Cg1a 2 {ECO:0000303|PubMed:25240294};
DE            Short=Kappa-TRTX-Cg1a {ECO:0000303|PubMed:25240294};
DE   AltName: Full=Jingzhaotoxin-11.2;
DE            Short=JZTX-11.2;
DE   AltName: Full=Jingzhaotoxin-XI.2 {ECO:0000303|PubMed:17176080};
DE            Short=JZTX-XI.2 {ECO:0000303|PubMed:17176080, ECO:0000303|PubMed:18581053};
DE   AltName: Full=Peptide F4-13.64 {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 51-84, AND 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   PROTEIN SEQUENCE OF 51-84, SUBCELLULAR LOCATION, FUNCTION, STRUCTURE BY NMR
RP   OF 51-84, AMIDATION AT PHE-84, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17176080; DOI=10.1021/bi061457+;
RA   Liao Z., Yuan C., Deng M., Li J., Chen J., Yang Y., Hu W., Liang S.;
RT   "Solution structure and functional characterization of Jingzhaotoxin-XI: a
RT   novel gating modifier of both potassium and sodium channels.";
RL   Biochemistry 45:15591-15600(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 51-84, FUNCTION, SUBCELLULAR LOCATION, AND DISULFIDE
RP   BOND.
RC   TISSUE=Venom;
RX   PubMed=25240294; DOI=10.1016/j.toxicon.2014.09.002;
RA   Tang C., Zhou X., Huang Y., Zhang Y., Hu Z., Wang M., Chen P., Liu Z.,
RA   Liang S.;
RT   "The tarantula toxin jingzhaotoxin-XI (kappa-theraphotoxin-Cj1a) regulates
RT   the activation and inactivation of the voltage-gated sodium channel
RT   Nav1.5.";
RL   Toxicon 92:6-13(2014).
CC   -!- FUNCTION: This toxin acts as a voltage-dependent gating-modifier
CC       (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM)
CC       and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A
CC       (PubMed:17176080, PubMed:25240294). It significantly shifts the
CC       activation to more depolarized voltages and decreases the deactivation
CC       of Nav1.5 currents upon extreme depolarization, but only slightly
CC       affects voltage-dependence of steady-state inactivation
CC       (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an
CC       approximately five-fold decrease in the rate of recovery from
CC       inactivation and an approximately 1.9-fold reduction in the closed-
CC       state inactivation rate (PubMed:25240294). This toxin integrates the
CC       functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins
CC       (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5
CC       (PubMed:25240294). Also shows inhibition of voltage-gated potassium
CC       channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately
CC       inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080).
CC       {ECO:0000269|PubMed:17176080, ECO:0000269|PubMed:25240294}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17176080,
CC       ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17176080, 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:25240294}.
CC   -!- MASS SPECTROMETRY: Mass=3727.3; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:17176080};
CC   -!- MISCELLANEOUS: This toxin does not show effect on Kv1.1/KCNA1,
CC       Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.4/KCNA4, Kv3.1/KCNC1 (all expressed in
CC       oocytes), voltage-gated sodium channels (Nav1/SCN) (from DRG neurons),
CC       and in a range of voltage-gated calcium channels (expressed in rat DRG
CC       neurons) (PubMed:17176080). Does not show significant toxic symptoms
CC       when injected into mice and into cockroaches (PubMed:17176080).
CC       {ECO:0000305|PubMed:17176080}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 28 (Jztx-11)
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: Several genes are coding for this toxin for which the
CC       structure by NMR has been determined. The cross-references to PDB and
CC       additional information can be found in entry AC P0C247. {ECO:0000305}.
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DR   EMBL; EU233872; ABY71691.1; -; mRNA.
DR   AlphaFoldDB; B1P1E1; -.
DR   SMR; B1P1E1; -.
DR   ArachnoServer; AS000043; kappa-theraphotoxin-Cg1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Potassium channel impairing toxin;
KW   Secreted; 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..50
FT                   /evidence="ECO:0000269|PubMed:17176080,
FT                   ECO:0000269|PubMed:17476710"
FT                   /id="PRO_0000398407"
FT   PEPTIDE         51..84
FT                   /note="Kappa-theraphotoxin-Cg1a 2"
FT                   /evidence="ECO:0000269|PubMed:17176080,
FT                   ECO:0000269|PubMed:17476710, ECO:0000269|PubMed:25240294"
FT                   /id="PRO_0000398408"
FT   MOD_RES         84
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:17176080"
FT   DISULFID        52..66
FT                   /evidence="ECO:0000269|PubMed:17176080"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000269|PubMed:17176080"
FT   DISULFID        65..78
FT                   /evidence="ECO:0000269|PubMed:17176080"
SQ   SEQUENCE   86 AA;  9585 MW;  C7F3C7FF1AD1F98F CRC64;
     MKVSVVITLA VLGVMFVWAS AAELEERGSD QRDSPAWLKS MERIFQSEER ECRKMFGGCS
     VDSDCCAHLG CKPTLKYCAW DGTFGK
 
 
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