SCX4_BUTOM
ID SCX4_BUTOM Reviewed; 65 AA.
AC P59354;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-like toxin Bom4 {ECO:0000305};
DE AltName: Full=Bom IV {ECO:0000303|PubMed:10103091};
DE Short=BomIV {ECO:0000305};
OS Buthus occitanus mardochei (Moroccan scorpion) (Buthus mardochei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX NCBI_TaxID=6869;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=10103091; DOI=10.1046/j.1460-9568.1999.00505.x;
RA Cestele S., Stankiewicz M., Mansuelle P., De Waard M., Dargent B.,
RA Gilles N., Pelhate M., Rochat H., Martin-Eauclaire M.-F., Gordon D.;
RT "Scorpion alpha-like toxins, toxic to both mammals and insects,
RT differentially interact with receptor site 3 on voltage-gated sodium
RT channels in mammals and insects.";
RL Eur. J. Neurosci. 11:975-985(1999).
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. This alpha-like toxin is highly
CC toxic to mice and insects. {ECO:0000269|PubMed:10103091}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10103091}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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=7287.96; Mass_error=0.37; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10103091};
CC -!- TOXIC DOSE: LD(50) is 1.15 ug/kg (23 ng/mouse) by
CC intracerebroventricular injection into mice.
CC {ECO:0000303|PubMed:10103091}.
CC -!- TOXIC DOSE: LD(50) is 19.7 nmol/g to cockroaches (Blattella germanica).
CC {ECO:0000303|PubMed:10103091}.
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 AlphaFoldDB; P59354; -.
DR SMR; P59354; -.
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..65
FT /note="Alpha-like toxin Bom4"
FT /evidence="ECO:0000269|PubMed:10103091"
FT /id="PRO_0000066745"
FT DOMAIN 2..64
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 12..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 16..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 22..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 26..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 65 AA; 7296 MW; 4305EB32436A4B90 CRC64;
GRDAYIAQPE NCVYECAKNS YCNDLCTKNG AKSGYCQWLG KYGNACWCED LPDNVPIRIP
GKCHF
