ID   DORT_PARTR              Reviewed;          58 AA.
AC   P0C1B7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   22-FEB-2023, entry version 48.
DE   RecName: Full=Dortoxin;
DE   AltName: Full=Dorsotoxin;
OS   Parabuthus transvaalicus (South African fattail scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Parabuthus.
OX   NCBI_TaxID=170972;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15804521; DOI=10.1016/j.toxicon.2005.01.020;
RA   Inceoglu A.B., Lango J., Pessah I.N., Hammock B.D.;
RT   "Three structurally related, highly potent, peptides from the venom of
RT   Parabuthus transvaalicus possess divergent biological activity.";
RL   Toxicon 45:727-733(2005).
CC   -!- FUNCTION: Binds to sodium channels (Nav) and affects the channel
CC       activation process (By similarity). In mice, causes hyperactivity that
CC       persists until death. {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   -!- MASS SPECTROMETRY: Mass=6641.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15804521};
CC   -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC       Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1B7; -.
DR   SMR; P0C1B7; -.
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   Gene3D; 3.30.30.10; Knottin, scorpion toxin-like; 1.
DR   InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SUPFAM; SSF57095; Scorpion toxin-like; 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..58
FT                   /note="Dortoxin"
FT                   /id="PRO_0000233630"
FT   DOMAIN          3..58
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        18..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        31..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   58 AA;  6648 MW;  732B4ED9FC645260 CRC64;
     ADVPGNYPLD KDGNTYTCLK LGENKDCQKV CKLHGVQYGY CYAFECWCKE YLDDKDSV
//