TXC11_CUPSA
ID TXC11_CUPSA Reviewed; 69 AA.
AC B3EWT1;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Toxin CSTX-11 {ECO:0000303|PubMed:22672445};
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, AND SUBCELLULAR 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 -!- FUNCTION: Spider venom toxin that shows calcium channel blocking
CC activity and exhibits cytolytic activity by affecting the outer leaflet
CC curvature and/or pore formation across the membrane. It blocks L-type
CC calcium channels (Cav1/CACNA1) in mammalian neurons at nanomolar
CC concentrations. Furthermore, it produces a slow voltage-independent
CC block of mid/low and high voltage-activated calcium channels in
CC cockroach neurons. Potassium ions, histamine, M-ctenitoxin-Cs1a (AC
CC P83619), CSTX-9 (AC P58604), and CSTX-13 (AC P83919) synergistically
CC increase the insecticidal activity of this toxin. In vivo, it causes
CC paralysis in blow flies and provokes death in drosophila.
CC {ECO:0000250|UniProtKB:P81694}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22672445}. Target
CC cell membrane {ECO:0000250|UniProtKB:P81694}.
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 -!- MASS SPECTROMETRY: Mass=8068.747; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22672445};
CC -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. {ECO:0000255}.
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DR AlphaFoldDB; B3EWT1; -.
DR SMR; B3EWT1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR InterPro; IPR019553; Spider_toxin_CSTX_knottin.
DR InterPro; IPR011142; Spider_toxin_CSTX_Knottin_CS.
DR Pfam; PF10530; Toxin_35; 1.
DR PROSITE; PS60029; SPIDER_CSTX; 1.
PE 1: Evidence at protein level;
KW Amidation; Calcium channel impairing toxin; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Knottin; Membrane; Neurotoxin; Secreted; Target cell membrane;
KW Target membrane; Toxin; Voltage-gated calcium channel impairing toxin.
FT PEPTIDE 1..69
FT /note="Toxin CSTX-11"
FT /evidence="ECO:0000269|PubMed:22672445"
FT /id="PRO_0000421180"
FT DISULFID 6..21
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 13..30
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 20..47
FT /evidence="ECO:0000250|UniProtKB:P58604"
FT DISULFID 32..45
FT /evidence="ECO:0000250|UniProtKB:P58604"
SQ SEQUENCE 69 AA; 8083 MW; 7077C73565571748 CRC64;
KDKENCIGKH HECTDDRDSC CKGKLFRYQC QCFKVIDGKK ETKRCACVTP LHYKMAEMAV
SVFKKMFKN
