ID   TXC14_CUPSA             Reviewed;          48 AA.
AC   B3EWS7;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Toxin CSTX-14 {ECO:0000303|PubMed:22672445};
DE   Contains:
DE     RecName: Full=CSTX-14 A chain {ECO:0000303|PubMed:22672445};
DE   Contains:
DE     RecName: Full=CSTX-14 B chain {ECO:0000303|PubMed:22672445};
DE   Flags: Precursor; Fragments;
OS   Cupiennius salei (American wandering spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Cupiennius.
OX   NCBI_TaxID=6928;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom;
RX   PubMed=22672445; DOI=10.1111/j.1742-4658.2012.08650.x;
RA   Trachsel C., Siegemund D., Kampfer U., Kopp L.S., Buhr C., Grossmann J.,
RA   Luthi C., Cunningham M., Nentwig W., Kuhn-Nentwig L., Schurch S.,
RA   Schaller J.;
RT   "Multicomponent venom of the spider Cupiennius salei: a bioanalytical
RT   investigation applying different strategies.";
RL   FEBS J. 279:2683-2694(2012).
CC   -!- SUBUNIT: Heterodimer of A and B chains; disulfide-linked.
CC       {ECO:0000250|UniProtKB:P83919}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22672445}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:22672445}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P58604}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:22672445}.
CC   -!- MASS SPECTROMETRY: [CSTX-14 A chain]: Mass=4369.812;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:22672445};
CC   -!- MASS SPECTROMETRY: [CSTX-14 B chain]: Mass=1757.848;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:22672445};
CC   -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 12 subfamily.
CC       {ECO:0000255}.
CC   -!- CAUTION: It is probable that CSTX-14 A and B chains originate from the
CC       same gene. Both chains may be separated by some amino acids.
CC       {ECO:0000305}.
CC   -!- CAUTION: May be a cleavage product of CSTX-12. {ECO:0000305}.
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DR   AlphaFoldDB; B3EWS7; -.
DR   SMR; B3EWS7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011142; Spider_toxin_CSTX_Knottin_CS.
DR   PROSITE; PS60029; SPIDER_CSTX; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Secreted; Toxin.
FT   PEPTIDE         1..34
FT                   /note="CSTX-14 A chain"
FT                   /evidence="ECO:0000269|PubMed:22672445"
FT                   /id="PRO_0000421183"
FT   PEPTIDE         35..48
FT                   /note="CSTX-14 B chain"
FT                   /evidence="ECO:0000269|PubMed:22672445"
FT                   /id="PRO_0000421184"
FT   DISULFID        3..18
FT                   /evidence="ECO:0000250|UniProtKB:P83919"
FT   DISULFID        10..27
FT                   /evidence="ECO:0000250|UniProtKB:P83919"
FT   DISULFID        17..42
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P83919"
FT   DISULFID        29..40
FT                   /note="Interchain (between A and B chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P83919"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000303|PubMed:22672445"
SQ   SEQUENCE   48 AA;  5657 MW;  71B2B99EBB88AA80 CRC64;
     SDCTLRNHDC TDDRHSCCRS KMFKDVCKCF YPSQAKKELC TCQQDKHL