ID   SCX1_ORTSC              Reviewed;          66 AA.
AC   P15224;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Toxin Os1;
DE            Short=Os-1;
OS   Orthochirus scrobiculosus (Central Asian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Orthochirus.
OX   NCBI_TaxID=6892;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=3730007;
RA   Potapenko N.A., Volkova T.M., Garsia A.F., Galkina T.G., Dulubova I.E.,
RA   Grishin E.V.;
RT   "Complete amino acid sequence of neurotoxin Os-1 from the venom of the
RT   Central Asian black scorpion Orthochirus scrobiculosus.";
RL   Bioorg. Khim. 12:581-590(1986).
CC   -!- FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium
CC       channels (Nav) and inhibit the inactivation of the activated channels,
CC       thereby blocking neuronal transmission (By similarity). This toxin
CC       possesses a high paralytic activity against mice. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
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; JN0408; JN0408.
DR   AlphaFoldDB; P15224; -.
DR   SMR; P15224; -.
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   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..66
FT                   /note="Toxin Os1"
FT                   /id="PRO_0000066789"
FT   DOMAIN          2..66
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        22..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   66 AA;  7559 MW;  7CEA53544D57C5BC CRC64;
     ERDGYIVQLH NCVYHCGLNP YCNGLCTKNG ATSGSYCQWM TKWGNACYCY ALPDKVPIKW
     LDPKCY