SCX1_BUTMA
ID SCX1_BUTMA Reviewed; 67 AA.
AC P0DJH8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Alpha-toxin Bu1;
OS Buthacus macrocentrus (Turkish scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Buthacus.
OX NCBI_TaxID=1143368;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-65, FUNCTION, TOXIC DOSE,
RP IDENTIFICATION BY MASS SPECTROMETRY, AMIDATION AT ARG-65, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=22245624; DOI=10.1016/j.toxicon.2011.12.013;
RA Caliskan F., Quintero-Hernandez V., Restano-Cassulini R., Batista C.V.,
RA Zamudio F.Z., Coronas F.I., Possani L.D.;
RT "Turkish scorpion Buthacus macrocentrus: general characterization of the
RT venom and description of Bu1, a potent mammalian Na-channel alpha-toxin.";
RL Toxicon 59:408-415(2012).
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. Since the experiments have been
CC done on F11 cells (immortalized cell line derived from rat DRG neurons
CC mainly expressing Nav1.3/SCN3A, but also Nav1.7/SCN9A and
CC Nav1.2/SCN2A), it is supposed to act on these channels. The slow of
CC inactivation process is partially reversible. Is lethal to mice.
CC {ECO:0000269|PubMed:22245624}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22245624}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22245624}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000250|UniProtKB:P0DQN8}.
CC -!- TOXIC DOSE: 10 ug of this toxin kills a mouse of 20g body weight within
CC 20 minutes after intraperitoneal injection.
CC {ECO:0000269|PubMed:22245624}.
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 EMBL; JQ038136; AFG28506.1; -; mRNA.
DR AlphaFoldDB; P0DJH8; -.
DR SMR; P0DJH8; -.
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="Alpha-toxin Bu1"
FT /id="PRO_0000417436"
FT DOMAIN 3..65
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 65
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:22245624"
FT DISULFID 13..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 17..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 23..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 27..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 67 AA; 7485 MW; B2FBC35EFCF8C70B CRC64;
GVRDAYIADD KNCVYTCAKN SYCNTECTKN GAESGYCQWL GKYGNGCWCI KLPDKVPIRI
PGRCRGR