TXC15_CUPSA
ID TXC15_CUPSA Reviewed; 48 AA.
AC B3EWS8;
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-15 {ECO:0000303|PubMed:22672445};
DE Contains:
DE RecName: Full=CSTX-15 A chain {ECO:0000303|PubMed:22672445};
DE Contains:
DE RecName: Full=CSTX-15 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-15 A chain]: Mass=4342.764;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:22672445};
CC -!- MASS SPECTROMETRY: [CSTX-15 B chain]: Mass=1739.879;
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-15 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-13. {ECO:0000305}.
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DR AlphaFoldDB; B3EWS8; -.
DR SMR; B3EWS8; -.
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-15 A chain"
FT /evidence="ECO:0000269|PubMed:22672445"
FT /id="PRO_0000421185"
FT PEPTIDE 35..48
FT /note="CSTX-15 B chain"
FT /evidence="ECO:0000269|PubMed:22672445"
FT /id="PRO_0000421186"
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; 5612 MW; 71B2B9836DE47A80 CRC64;
SDCTLRNHDC TDDRHSCCRS KMFKDVCTCF YPSQAKKELC TCQQPKHL
