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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
 
 
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