ID   TXC10_CUPSA             Reviewed;         116 AA.
AC   B3EWT0; A0A4Y5UGJ5;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 2.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Toxin CSTX-10 {ECO:0000303|PubMed:22672445};
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=30893800; DOI=10.3390/toxins11030167;
RA   Kuhn-Nentwig L., Langenegger N., Heller M., Koua D., Nentwig W.;
RT   "The dual prey-inactivation strategy of spiders-in-depth venomic analysis
RT   of Cupiennius salei.";
RL   Toxins 11:0-0(2019).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-116, 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=8095.806; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22672445};
CC   -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. {ECO:0000255}.
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DR   EMBL; MH754560; QDC23095.1; -; mRNA.
DR   EMBL; MH754561; QDC23096.1; -; mRNA.
DR   AlphaFoldDB; B3EWT0; -.
DR   SMR; B3EWT0; -.
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; Signal; Target cell membrane;
KW   Target membrane; Toxin; Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000305|PubMed:22672445"
FT                   /id="PRO_0000452336"
FT   PEPTIDE         48..116
FT                   /note="Toxin CSTX-10"
FT                   /evidence="ECO:0000269|PubMed:22672445"
FT                   /id="PRO_0000421179"
FT   DISULFID        53..68
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        60..77
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        67..94
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
FT   DISULFID        79..92
FT                   /evidence="ECO:0000250|UniProtKB:P58604"
SQ   SEQUENCE   116 AA;  13406 MW;  FFB6D2A30F961B73 CRC64;
     MKVLVIFAVL SLVIFSNCSA ETDEDFFGEE SFEADDIIPF IAKEQVRKDK ENCIGKHHEC
     TDDRDNCCKG KLFRYQCQCF KVIDGKKETK RCACVTPLHY KMAEMAVSVF KKMFKN