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SCX9_BUTOC
ID   SCX9_BUTOC              Reviewed;          70 AA.
AC   P04099;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2017, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Alpha-toxin Bot9 {ECO:0000303|PubMed:27528512};
DE   AltName: Full=BotIX {ECO:0000303|PubMed:27528512};
DE   AltName: Full=Neurotoxin 9 {ECO:0000305};
DE   AltName: Full=Neurotoxin IX {ECO:0000305};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   TOXIC DOSE.
RC   TISSUE=Venom {ECO:0000303|PubMed:27528512};
RX   PubMed=27528512; DOI=10.1002/1873-3468.12357;
RA   Martin-Eauclaire M.F., Salvatierra J., Bosmans F., Bougis P.E.;
RT   "The scorpion toxin Bot IX is a potent member of the alpha-like family and
RT   has a unique N-terminal sequence extension.";
RL   FEBS Lett. 590:3221-3232(2016).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-35, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:6729843};
RX   PubMed=6729843; DOI=10.1016/0041-0101(84)90028-x;
RA   Martin M.-F., Rochat H.;
RT   "Purification of thirteen toxins active on mice from the venom of the North
RT   African scorpion Buthus occitanus tunetanus.";
RL   Toxicon 22:279-291(1984).
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 toxin is active against
CC       rat Nav1.2/SCN2A and B.germanica Nav1. {ECO:0000269|PubMed:27528512}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27528512,
CC       ECO:0000269|PubMed:6729843}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:6729843}.
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=7985.61; Mass_error=0.11; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:27528512};
CC   -!- TOXIC DOSE: LD(50) is 100 ng/kg by subcutaneous injection in mice.
CC       {ECO:0000269|PubMed:27528512}.
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; A05136; A05136.
DR   AlphaFoldDB; P04099; -.
DR   SMR; P04099; -.
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..70
FT                   /note="Alpha-toxin Bot9"
FT                   /evidence="ECO:0000269|PubMed:27528512"
FT                   /id="PRO_0000066737"
FT   DOMAIN          6..69
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..68
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        20..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        26..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        30..52
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   CONFLICT        23
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        32..33
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   70 AA;  7998 MW;  E24EB04C32040548 CRC64;
     AEIKVRDGYI VYPNNCVYHC GLNPYCNDLC TKNGAKSGYC QWLTKWGNAC YCYALPEKVP
     IKDPSYKCYS
 
 
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