SCX1_CENSC
ID SCX1_CENSC Reviewed; 87 AA.
AC P01492; Q95WB7; Q95WB8; Q95WC6; Q95WC7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Toxin CsEv1;
DE Short=CsE v1;
DE AltName: Full=Neurotoxin 1;
DE Flags: Precursor;
OS Centruroides sculpturatus (Arizona bark scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=218467;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11600153; DOI=10.1016/s0041-0101(01)00174-x;
RA Corona M., Valdez-Cruz N.A., Merino E., Zurita M., Possani L.D.;
RT "Genes and peptides from the scorpion Centruroides sculpturatus Ewing, that
RT recognize Na(+)-channels.";
RL Toxicon 39:1893-1898(2001).
RN [2]
RP PROTEIN SEQUENCE OF 20-84, AMIDATION AT CYS-84, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=4460885; DOI=10.1016/0003-9861(74)90082-4;
RA Babin D.R., Watt D.D., Goos S.M., Mlejnek R.V.;
RT "Amino acid sequences of neurotoxic protein variants from the venom of
RT Centruroides sculpturatus Ewing.";
RL Arch. Biochem. Biophys. 164:694-706(1974).
RN [3]
RP SEQUENCE REVISION TO 44-46 AND 83-84, STRUCTURE BY NMR, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom;
RX PubMed=8117707; DOI=10.1021/bi00175a015;
RA Lee W., Jablonsky M.J., Watt D.D., Krishna N.R.;
RT "Proton nuclear magnetic resonance and distance geometry/simulated
RT annealing studies on the variant-1 neurotoxin from the New World scorpion
RT Centruroides sculpturatus Ewing.";
RL Biochemistry 33:2468-2475(1994).
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). Induces immediate
CC paralysis in crickets after injection, with a total paralysis occurring
CC within 15-30 minutes and lasting for 1-2 hours. Is also lethal to
CC vertebrate (chicks) when injected in very high dosages (more than 100
CC mg/kg). {ECO:0000250, ECO:0000269|PubMed:4460885}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4460885}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:4460885}.
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 -!- TOXIC DOSE: PD(50) is 11.0 mg/kg of insects (crickets).
CC {ECO:0000269|PubMed:4460885}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR EMBL; AF338454; AAL23422.1; -; mRNA.
DR EMBL; AF338455; AAL23423.1; -; mRNA.
DR EMBL; AF338463; AAL23431.1; -; mRNA.
DR EMBL; AF338464; AAL23432.1; -; mRNA.
DR PIR; A01752; NTSR1C.
DR PDB; 1VNA; NMR; -; A=20-84.
DR PDB; 1VNB; NMR; -; A=20-84.
DR PDBsum; 1VNA; -.
DR PDBsum; 1VNB; -.
DR AlphaFoldDB; P01492; -.
DR SMR; P01492; -.
DR EvolutionaryTrace; P01492; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3D-structure; 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:4460885"
FT PEPTIDE 20..84
FT /note="Toxin CsEv1"
FT /id="PRO_0000035288"
FT DOMAIN 20..85
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 84
FT /note="Cysteine amide"
FT /evidence="ECO:0000269|PubMed:4460885"
FT DISULFID 31..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:8117707"
FT DISULFID 35..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:8117707"
FT DISULFID 44..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:8117707"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:8117707"
FT VARIANT 6
FT /note="I -> M (in CsEv1C and CsEv1E)"
FT VARIANT 9..14
FT /note="ACFALV -> VCLFLI (in CsEv1D)"
FT VARIANT 26
FT /note="K -> N (in CsEv1D)"
FT VARIANT 29
FT /note="D -> T (in CsEv1D)"
FT VARIANT 40
FT /note="K -> E (in CsEv1E)"
FT VARIANT 43
FT /note="H -> G (in CsEv1E)"
FT VARIANT 46
FT /note="T -> K (in CsEv1E)"
FT VARIANT 46
FT /note="T -> L (in CsEv1C and CsEv1D)"
FT CONFLICT 45
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1VNA"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1VNA"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1VNA"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1VNA"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1VNA"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1VNA"
FT STRAND 56..68
FT /evidence="ECO:0007829|PDB:1VNA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1VNB"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1VNB"
SQ SEQUENCE 87 AA; 9636 MW; 9237B1FCBBF0E658 CRC64;
MNSLLIITAC FALVGTVWAK EGYLVKKSDG CKYDCFWLGK NEHCDTECKA KNQGGSYGYC
YAFACWCEGL PESTPTYPLP NKSCGKK