ID   JZT36_CHIGU             Reviewed;          88 AA.
AC   B1P1D7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=U13-theraphotoxin-Cg1a;
DE            Short=U13-TRTX-Cg1a;
DE   AltName: Full=Jingzhaotoxin-36;
DE            Short=JZTX-36;
DE   AltName: Full=Peptide F1-27.85;
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 53-63, MASS SPECTROMETRY, 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).
CC   -!- FUNCTION: Probable ion channel inhibitor.
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:0000250|UniProtKB:P0C247}.
CC   -!- MASS SPECTROMETRY: Mass=3755.5; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:17476710};
CC   -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 41 (Jztx-36)
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The measured mass obtained by MALDI is higher than the
CC       calculated mass. {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; EU233868; ABY71687.1; -; mRNA.
DR   AlphaFoldDB; B1P1D7; -.
DR   SMR; B1P1D7; -.
DR   ArachnoServer; AS000816; U13-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: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.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..52
FT                   /evidence="ECO:0000269|PubMed:17476710"
FT                   /id="PRO_0000398475"
FT   PEPTIDE         53..88
FT                   /note="U13-theraphotoxin-Cg1a"
FT                   /id="PRO_0000398476"
FT   DISULFID        54..68
FT                   /evidence="ECO:0000250|UniProtKB:P0C247"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000250|UniProtKB:P0C247"
FT   DISULFID        67..80
FT                   /evidence="ECO:0000250|UniProtKB:P0C247"
SQ   SEQUENCE   88 AA;  9891 MW;  D46585FB481AD807 CRC64;
     MKVSVLITLA VLGVMFVWAS AAELEQSGSD QKDSDSPAWL KSMERIFQSE ERDCRKMFGG
     CSKHEDCCAH LACKRTFNYC AWDGSFSK