SIX4_MESMA
ID SIX4_MESMA Reviewed; 64 AA.
AC Q17230;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Beta-insect depressant toxin BmKIT4;
DE Short=BmK IT4;
DE Short=Insect toxin 4;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Zhu X., Zhang T., Zhu Y.;
RT "Cloning and sequencing of two depressant insect selective neurotoxin cDNAs
RT from Buthus martensii Karsch.";
RL Chin. Sci. Bull. 41:1387-1391(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=11024486; DOI=10.1016/s0041-0101(00)00115-x;
RA Jiang G., Xu Y., Zhu X., Su Y., Zhu Y.;
RT "Prokaryotically expressed Buthus martensii Karsch insect depressant toxin
RT has insecticidal effects.";
RL Toxicon 39:469-476(2001).
CC -!- FUNCTION: Depressant insect beta-toxins cause a transient contraction
CC paralysis followed by a slow flaccid paralysis. They bind voltage-
CC independently at site-4 of sodium channels (Nav) and shift the voltage
CC of activation toward more negative potentials thereby affecting sodium
CC channel activation and promoting spontaneous and repetitive firing.
CC This toxin is active only on insects (By similarity). {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 -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92846; CAA63431.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q17230; -.
DR SMR; Q17230; -.
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 2: Evidence at transcript level;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Toxin; Voltage-gated sodium channel impairing toxin.
FT CHAIN 1..60
FT /note="Beta-insect depressant toxin BmKIT4"
FT /id="PRO_0000035203"
FT DOMAIN 1..61
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 60
FT /note="Cysteine amide"
FT /evidence="ECO:0000255"
FT DISULFID 10..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 14..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 21..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 25..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 64 AA; 7186 MW; 8A4A33F721C3EC0A CRC64;
DGYIRGSNGC KISCLWGNEG CNKECKGFGA YYGYCWTWGL ACWCEGLPDD KTWKSESNTC
GRKK
