JZT8B_CHIGU
ID JZT8B_CHIGU Reviewed; 83 AA.
AC B1P1A5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=U3-theraphotoxin-Cg1a {ECO:0000305};
DE Short=U3-TRTX-Cg1a {ECO:0000305};
DE AltName: Full=Jingzhaotoxin-8.2 {ECO:0000305};
DE Short=JZTX-8.2 {ECO:0000305};
DE AltName: Full=Jingzhaotoxin-VIII.2 {ECO:0000305};
DE Short=JZTX-VIII.2 {ECO:0000312|EMBL:ABY71655.1};
DE AltName: Full=Peptide F7-12.17 {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 45-83, 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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17476710}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:17476710}.
CC -!- MASS SPECTROMETRY: Mass=4330.3; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:17476710};
CC -!- SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 03 (juruin)
CC subfamily. {ECO:0000305}.
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DR EMBL; EU233836; ABY71655.1; -; mRNA.
DR AlphaFoldDB; B1P1A5; -.
DR SMR; B1P1A5; -.
DR ArachnoServer; AS000785; U3-theraphotoxin-Cg1a.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR012625; Toxin_20.
DR Pfam; PF08089; Toxin_20; 1.
DR PROSITE; PS60022; HWTX_2; 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..23
FT /evidence="ECO:0000255"
FT PROPEP 24..44
FT /evidence="ECO:0000269|PubMed:17476710"
FT /id="PRO_0000398402"
FT PEPTIDE 45..83
FT /note="U3-theraphotoxin-Cg1a"
FT /evidence="ECO:0000269|PubMed:17476710"
FT /id="PRO_0000398403"
FT DISULFID 48..61
FT /evidence="ECO:0000250|UniProtKB:P85504"
FT DISULFID 52..75
FT /evidence="ECO:0000250|UniProtKB:P85504"
FT DISULFID 69..80
FT /evidence="ECO:0000250|UniProtKB:P85504"
SQ SEQUENCE 83 AA; 9155 MW; 42A9DE57A6DA34C1 CRC64;
MKTFTLIAIL TCAVFVIFHA AAAEELEAQD VIETEALATL DEERLFECSF SCDIKKNGKP
CKGSGEKKCS GGWRCKMNFC VKV