SCX1_CENII
ID SCX1_CENII Reviewed; 66 AA.
AC P59897;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Beta-toxin Cii1 {ECO:0000305};
DE Short=Cii 1 {ECO:0000303|PubMed:8653586};
DE AltName: Full=Toxin 1 {ECO:0000303|PubMed:7725317};
OS Centruroides infamatus (Kock scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX NCBI_TaxID=42199;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8653586; DOI=10.1016/0305-0491(95)02031-4;
RA Dehesa-Davila M., Ramirez A.N., Zamudio F.Z., Gurrola-Briones G.,
RA Lievano A., Darszon A., Possani L.D.;
RT "Structural and functional comparison of toxins from the venom of the
RT scorpions Centruroides infamatus infamatus, Centruroides limpidus limpidus
RT and Centruroides noxius.";
RL Comp. Biochem. Physiol. 113B:331-339(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-48, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7725317; DOI=10.1016/0041-0101(94)90307-7;
RA Dehesa-Davila M., Martin B.M., Nobile M., Prestipino G., Possani L.D.;
RT "Isolation of a toxin from Centruroides infamatus infamatus Koch scorpion
RT venom that modifies Na+ permeability on chick dorsal root ganglion cells.";
RL Toxicon 32:1487-1493(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. {ECO:0000269|PubMed:7725317,
CC ECO:0000269|PubMed:8653586}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7725317,
CC ECO:0000269|PubMed:8653586}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:7725317, ECO:0000305|PubMed:8653586}.
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 AlphaFoldDB; P59897; -.
DR SMR; P59897; -.
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 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; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..66
FT /note="Beta-toxin Cii1"
FT /evidence="ECO:0000269|PubMed:8653586"
FT /id="PRO_0000066760"
FT DOMAIN 1..66
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 66
FT /note="Asparagine amide"
FT /evidence="ECO:0000250"
FT DISULFID 12..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 25..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 29..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 66 AA; 7587 MW; DF124D41D0A5B0C2 CRC64;
KEGYLVNHST GCKYECYKLG DNDYCLRECK QQYGKGAGGY CYAFGCWCTH LYEQAVVWPL
PKKTCN
