JZ38D_CHIGU
ID JZ38D_CHIGU Reviewed; 105 AA.
AC B1P1G1;
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=U21-theraphotoxin-Cg1a 4;
DE Short=U21-TRTX-Cg1a;
DE AltName: Full=Jingzhaotoxin-38.4;
DE Short=JZTX-38.4;
DE AltName: Full=Peptide F4-25.19;
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 48-82, MASS SPECTROMETRY, AMIDATION AT VAL-82, 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: 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=4075.1; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:17476710};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 05 (F4a)
CC subfamily. {ECO:0000305}.
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DR EMBL; EU233892; ABY71711.1; -; mRNA.
DR AlphaFoldDB; B1P1G1; -.
DR SMR; B1P1G1; -.
DR ArachnoServer; AS000839; U21-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 Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..48
FT /evidence="ECO:0000250"
FT /id="PRO_0000398485"
FT PEPTIDE 48..82
FT /note="U21-theraphotoxin-Cg1a 4"
FT /evidence="ECO:0000269|PubMed:17476710"
FT /id="PRO_0000398486"
FT PROPEP 83..105
FT /id="PRO_0000398487"
FT MOD_RES 82
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:17476710"
FT DISULFID 49..63
FT /evidence="ECO:0000250|UniProtKB:P0C247"
FT DISULFID 56..68
FT /evidence="ECO:0000250|UniProtKB:P0C247"
FT DISULFID 62..76
FT /evidence="ECO:0000250|UniProtKB:P0C247"
SQ SEQUENCE 105 AA; 12117 MW; 60ECE6F12D7D8A03 CRC64;
MKVSVLITLA VLGVMFLLTS AEERGSDQMD SPAWLKSMEI IFQSEERECR WLFGGCEKDS
DCCEHLGCRR AKPSWCGWDF TVGKWEMLIN MNIFRIVFSY SMCTV