DORT_PARTR
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 25-MAY-2022, entry version 46.
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; -; 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; 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..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