SCX2_BUTOC
ID SCX2_BUTOC Reviewed; 65 AA.
AC P01483;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Neurotoxin Bot2;
DE AltName: Full=Bot II;
DE Short=BotII;
DE AltName: Full=Neurotoxin II {ECO:0000303|PubMed:6845379};
OS Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX NCBI_TaxID=6871;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RA Vargas O., Gregoire J., Martin M.-F., Bechis G., Rochat H.;
RT "Neurotoxins from the venoms of two scorpions: Buthus occitanus tunetanus
RT and Buthus occitanus mardochei.";
RL Toxicon 20:79-79(1982).
RN [2]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AMIDATION AT PHE-65, AND DISULFIDE
RP BOND.
RC TISSUE=Venom;
RX PubMed=6845379; DOI=10.1016/0041-0101(83)90058-2;
RA Gregoire J., Rochat H.;
RT "Covalent structure of toxins I and II from the scorpion Buthus occitanus
RT tunetanus.";
RL Toxicon 21:153-162(1983).
CC -!- FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation
CC of the activated channels, thereby blocking neuronal transmission.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
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. Alpha subfamily. {ECO:0000305}.
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DR PIR; A01743; NTSR2B.
DR AlphaFoldDB; P01483; -.
DR SMR; P01483; -.
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 CDD; cd00107; Knot1; 1.
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; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..65
FT /note="Neurotoxin Bot2"
FT /evidence="ECO:0000269|PubMed:6845379, ECO:0000269|Ref.1"
FT /id="PRO_0000066733"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 65
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:6845379, ECO:0000269|Ref.1"
FT DISULFID 12..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:6845379"
FT DISULFID 16..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:6845379"
FT DISULFID 22..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:6845379"
FT DISULFID 26..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:6845379"
SQ SEQUENCE 65 AA; 7354 MW; 52CC2836B2763B9A CRC64;
GRDAYIAQPE NCVYECAKNS YCNDLCTKNG AKSGYCQWLG RWGNACYCID LPDKVPIRIE
GKCHF
