SCX1_CENNO
ID SCX1_CENNO Reviewed; 86 AA.
AC P15223; Q26460; Q6V4Z2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Toxin Cn1;
DE AltName: Full=Toxin II.14 {ECO:0000303|PubMed:4052021};
DE Short=Toxin 1;
DE Flags: Precursor;
OS Centruroides noxius (Mexican scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=6878;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT SER-84.
RC TISSUE=Venom gland;
RX PubMed=8585086; DOI=10.1016/0041-0101(95)00058-t;
RA Vazquez A., Tapia J.V., Eliason W.K., Martin B.M., Lebreton F.,
RA Delepierre M., Possani L.D., Becerril B.;
RT "Cloning and characterization of the cDNAs encoding Na+ channel-specific
RT toxins 1 and 2 of the scorpion Centruroides noxius Hoffmann.";
RL Toxicon 33:1161-1170(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-83.
RA Zhu S.;
RT "Alignment of beta-toxin nucleotide sequences.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 20-84, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4052021; DOI=10.1042/bj2290739;
RA Possani L.D., Martin B.M., Svendsen I., Rode G.S., Erickson B.W.;
RT "Scorpion toxins from Centruroides noxius and Tityus serrulatus. Primary
RT structures and sequence comparison by metric analysis.";
RL Biochem. J. 229:739-750(1985).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4052021}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:4052021}.
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 -!- 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; S81093; AAB36085.2; -; mRNA.
DR EMBL; AY351298; AAR08033.1; -; Genomic_DNA.
DR PIR; S32789; S32789.
DR AlphaFoldDB; P15223; -.
DR SMR; P15223; -.
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 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:4052021"
FT CHAIN 20..84
FT /note="Toxin Cn1"
FT /evidence="ECO:0000269|PubMed:4052021"
FT /id="PRO_0000035279"
FT DOMAIN 20..84
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 84
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:8585086"
FT DISULFID 30..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 34..59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 43..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 47..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 79
FT /note="P -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 9586 MW; AB8C1EA742F17222 CRC64;
MNSLLMITAC FVLIGTVWAK DGYLVDAKGC KKNCYKLGKN DYCNRECRMK HRGGSYGYCY
GFGCYCEGLS DSTPTWPLPN KTCSGK
