SCX1_CENTE
ID SCX1_CENTE Reviewed; 87 AA.
AC P18926; C0HLT9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Beta-toxin Ct1a {ECO:0000303|PubMed:23840487};
DE AltName: Full=Beta-toxin Clt1 {ECO:0000303|PubMed:2849217};
DE AltName: Full=Neurotoxin 1 {ECO:0000303|PubMed:2849217};
DE AltName: Full=Toxin II.20.3.4 {ECO:0000303|PubMed:2849217};
DE Flags: Precursor;
OS Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=1028682;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-45, PROBABLE AMIDATION
RP AT ASN-85, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=23840487; DOI=10.1371/journal.pone.0066486;
RA Valdez-Velazquez L.L., Quintero-Hernandez V., Romero-Gutierrez M.T.,
RA Coronas F.I., Possani L.D.;
RT "Mass fingerprinting of the venom and transcriptome of venom gland of
RT scorpion Centruroides tecomanus.";
RL PLoS ONE 8:e66486-e66486(2013).
RN [2]
RP PROTEIN SEQUENCE OF 20-85, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=2849217; DOI=10.1016/0041-0101(88)90319-4;
RA Martin B.M., Carbone E., Yatani A., Brown A.M., Ramirez A.N., Gurrola G.B.,
RA Possani L.D.;
RT "Amino acid sequence and physiological characterization of toxins from the
RT venom of the scorpion Centruroides limpidus tecomanus Hoffmann.";
RL Toxicon 26:785-794(1988).
RN [3]
RP FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=27130039; DOI=10.1016/j.toxicon.2016.04.046;
RA Valdez-Velazquez L.L., Romero-Gutierrez M.T., Delgado-Enciso I.,
RA Dobrovinskaya O., Melnikov V., Quintero-Hernandez V., Ceballos-Magana S.G.,
RA Gaitan-Hinojosa M.A., Coronas F.I., Puebla-Perez A.M., Zamudio F.,
RA De la Cruz-Garcia I., Vazquez-Vuelvas O.F., Soriano-Hernandez A.D.,
RA Possani L.D.;
RT "Comprehensive analysis of venom from the scorpion Centruroides tecomanus
RT reveals compounds with antimicrobial, cytotoxic, and insecticidal
RT activities.";
RL Toxicon 118:95-103(2016).
RN [4]
RP NEUTRALIZATION BY ANTIBODY.
RX PubMed=30634620; DOI=10.3390/toxins11010032;
RA Riano-Umbarila L., Gomez-Ramirez I.V., Ledezma-Candanoza L.M.,
RA Olamendi-Portugal T., Rodriguez-Rodriguez E.R., Fernandez-Taboada G.,
RA Possani L.D., Becerril B.;
RT "Generation of a broadly cross-neutralizing antibody fragment against
RT several mexican scorpion venoms.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium
CC channels (Nav) and shift the voltage of activation toward more negative
CC potentials thereby affecting sodium channel activation and promoting
CC spontaneous and repetitive firing (By similarity). Is lethal to mice
CC but does not show toxicity to freshwater shrimp and crickets
CC (PubMed:27130039). {ECO:0000250|UniProtKB:P60266,
CC ECO:0000269|PubMed:27130039}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2849217}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:2849217}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=7591; Method=Electrospray; Note=Average mass.;
CC Evidence={ECO:0000269|PubMed:23840487, ECO:0000269|PubMed:27130039};
CC -!- MISCELLANEOUS: Is neutralized by the single-chain antibody fragment
CC 10FG2. {ECO:0000269|PubMed:30634620}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {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; JZ122265; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A31188; A31188.
DR AlphaFoldDB; P18926; -.
DR SMR; P18926; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR018218; Scorpion_toxinL.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR PRINTS; PR00285; SCORPNTOXIN.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:23840487"
FT CHAIN 20..85
FT /note="Beta-toxin Ct1a"
FT /evidence="ECO:0000269|PubMed:23840487"
FT /id="PRO_0000066761"
FT DOMAIN 20..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 85
FT /note="Asparagine amide"
FT /evidence="ECO:0000305|PubMed:23840487"
FT DISULFID 31..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 44..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 81
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 87 AA; 9787 MW; 491ACFCF58607B41 CRC64;
MNSLLMITAC LALIGTVWAK EGYLVNHSTG CKYECFKLGD NDYCLRECRQ QYGKGAGGYC
YAFGCWCTHL YEQAVVWPLP KKTCNGK
