TXC9A_CUPSA
ID TXC9A_CUPSA Reviewed; 115 AA.
AC P58604; A0A4Y5UGK1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Toxin CSTX-9;
DE AltName: Full=Toxin CsTx-9a {ECO:0000303|PubMed:32290562};
DE AltName: Full=U1-ctenitoxin-Cs1a;
DE Short=U1-CNTX-Cs1a;
DE Contains:
DE RecName: Full=Toxin CSTX-7;
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 48-115, DISULFIDE BONDS, FUNCTION, TOXIC DOSE, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=11693532; DOI=10.1007/pl00000794;
RA Schaller J., Kaempfer U., Schuerch S., Kuhn-Nentwig L., Haeberli S.,
RA Nentwig W.;
RT "CSTX-9, a toxic peptide from the spider Cupiennius salei: amino acid
RT sequence, disulphide bridge pattern and comparison with other spider toxins
RT containing the cystine knot structure.";
RL Cell. Mol. Life Sci. 58:1538-1545(2001).
RN [3]
RP PROTEIN SEQUENCE OF 48-114, AND REVIEW.
RX PubMed=15066412; DOI=10.1016/j.toxicon.2004.02.009;
RA Kuhn-Nentwig L., Schaller J., Nentwig W.;
RT "Biochemistry, toxicology and ecology of the venom of the spider Cupiennius
RT salei (Ctenidae).";
RL Toxicon 43:543-553(2004).
RN [4]
RP FUNCTION IN SYNERGY WITH OTHER TOXINS, AND TOXIC DOSE.
RX PubMed=15914655; DOI=10.1242/jeb.01594;
RA Wullschleger B., Nentwig W., Kuhn-Nentwig L.;
RT "Spider venom: enhancement of venom efficacy mediated by different
RT synergistic strategies in Cupiennius salei.";
RL J. Exp. Biol. 208:2115-2121(2005).
RN [5]
RP FUNCTION, TOXIC DOSE, SUBUNIT, AND 3D-STRUCTURE MODELING.
RC TISSUE=Venom;
RX PubMed=32290562; DOI=10.3390/toxins12040250;
RA Clemencon B., Kuhn-Nentwig L., Langenegger N., Kopp L., Peigneur S.,
RA Tytgat J., Nentwig W., Luescher B.P.;
RT "Neurotoxin merging: a strategy deployed by the venom of the spider
RT cupiennius salei to potentiate toxicity on insects.";
RL Toxins 12:0-0(2020).
CC -!- FUNCTION: [Toxin CSTX-9]: Synergistic toxin that induces or increases a
CC cytolytic effect when combined with CSTX-1 (AC P81694) or CSTX-13 (AC
CC P83919). Potassium ions and M-ctenitoxin-Cs1a (AC P83619) have also an
CC effect on its activity. When alone, has no insecticidal activity.
CC {ECO:0000250, ECO:0000269|PubMed:11693532, ECO:0000269|PubMed:15914655,
CC ECO:0000269|PubMed:32290562}.
CC -!- SUBUNIT: Monomer (Probable). Interacts with CSTX-13 (AC P83919) (Kd=370
CC nM), but does not interact with CSTX-1 (AC P81694) (PubMed:32290562).
CC {ECO:0000269|PubMed:32290562, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11693532}. Target
CC cell membrane {ECO:0000305|PubMed:32290562}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:11693532}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: [Toxin CSTX-9]: Mass=7529.75; Mass_error=0.32;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:11693532};
CC -!- MASS SPECTROMETRY: [Toxin CSTX-7]: Mass=7383.04; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15066412};
CC -!- TOXIC DOSE: LD(50) is 10.6 pmol on Drosophila.
CC -!- TOXIC DOSE: LD(50) is 3.12 pmol/mg on Drosophila.
CC -!- TOXIC DOSE: [Toxin CSTX-9]: LD(50) is 45.54 pmol/mg when
CC intrathoracically injected into drosophila.
CC {ECO:0000269|PubMed:32290562}.
CC -!- TOXIC DOSE: [Toxin CSTX-9]: LD(50) is 0.432 pmol/mg when
CC intrathoracically co-injected with CSTX-1 (AC P81694) into drosophila.
CC {ECO:0000269|PubMed:32290562}.
CC -!- TOXIC DOSE: [Toxin CSTX-9]: LD(50) is 0.082 pmol/mg when
CC intrathoracically co-injected with CSTX-13 (AC P83919) into drosophila.
CC {ECO:0000269|PubMed:32290562}.
CC -!- SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MH754564; QDC23099.1; -; mRNA.
DR AlphaFoldDB; P58604; -.
DR SMR; P58604; -.
DR TCDB; 8.B.19.2.1; the sea anemone k+ channel blocker toxin, bcstx3 (bcstx3) family.
DR ArachnoServer; AS000299; U1-ctenitoxin-Cs1a.
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 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 Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Membrane; Neurotoxin; Secreted;
KW Signal; Target cell membrane; Target membrane; Toxin;
KW Voltage-gated calcium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..47
FT /evidence="ECO:0000305|PubMed:11693532,
FT ECO:0000305|PubMed:15066412"
FT /id="PRO_0000452333"
FT CHAIN 48..115
FT /note="Toxin CSTX-9"
FT /evidence="ECO:0000269|PubMed:11693532"
FT /id="PRO_0000087672"
FT CHAIN 48..114
FT /note="Toxin CSTX-7"
FT /evidence="ECO:0000269|PubMed:15066412"
FT /id="PRO_0000391351"
FT DISULFID 53..68
FT /evidence="ECO:0000269|PubMed:11693532"
FT DISULFID 60..77
FT /evidence="ECO:0000269|PubMed:11693532"
FT DISULFID 67..95
FT /evidence="ECO:0000269|PubMed:11693532"
FT DISULFID 79..93
FT /evidence="ECO:0000269|PubMed:11693532"
SQ SEQUENCE 115 AA; 12845 MW; 84811EF6A5E4657E CRC64;
MKVLVICAVL FLAIFSNSSA ETEDDFLEDE SFEADDVIPF LAREQVRKDD KNCIPKHHEC
TNDKKNCCKK GLTKMKCKCF TVADAKGATS ERCACDSSLL QKFGFTGLHI IKGLF