SIX3F_LEIHE
ID SIX3F_LEIHE Reviewed; 85 AA.
AC P0C5I8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Beta-insect depressant toxin Lqh-dprIT3f;
DE Flags: Precursor;
OS Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus
OS hebraeus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Leiurus.
OX NCBI_TaxID=6884;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TOXIC
RP DOSE.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15966742; DOI=10.1021/bi050235t;
RA Strugatsky D., Zilberberg N., Stankiewicz M., Ilan N., Turkov M., Cohen L.,
RA Pelhate M., Gilles N., Gordon D., Gurevitz M.;
RT "Genetic polymorphism and expression of a highly potent scorpion depressant
RT toxin enable refinement of the effects on insect Na channels and illuminate
RT the key role of Asn-58.";
RL Biochemistry 44:9179-9187(2005).
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 block action
CC potentials, primarily by depolarizing the axonal membrane and
CC suppressing the sodium current. This depressant toxin is active only on
CC insects. It is found in a relatively small amount in the venom.
CC {ECO:0000269|PubMed:15966742}.
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 -!- TOXIC DOSE: PD(50) is 19 ng/100 mg of body weight of Sarcophaga larvae
CC for contraction paralysis, and 85 ng/100 mg for flaccid paralysis.
CC {ECO:0000269|PubMed:15966742}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Beta subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C5I8; -.
DR SMR; P0C5I8; -.
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; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT CHAIN 22..82
FT /note="Beta-insect depressant toxin Lqh-dprIT3f"
FT /id="PRO_0000307616"
FT DOMAIN 22..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 82
FT /note="Glycine amide"
FT /evidence="ECO:0000250"
FT DISULFID 31..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 85 AA; 9204 MW; CBB84208419C3941 CRC64;
MKLLLLLTIS ASMLIEGLVN ADGYIRGGDG CKVSCVINHV FCDNECKAAG GSYGYCWGWG
LACWCEGLPA DREWDYETDT CGGKK
