SX21_LEIHE
ID SX21_LEIHE Reviewed; 83 AA.
AC P68725;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Insect toxin 2-13;
DE AltName: Full=LqhIT2-13;
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 [GENOMIC DNA].
RX PubMed=9929387; DOI=10.1007/pl00006457;
RA Froy O., Sagiv T., Poreh M., Urbach D., Zilberberg N., Gurevitz M.;
RT "Dynamic diversification from a putative common ancestor of scorpion toxins
RT affecting sodium, potassium, and chloride channels.";
RL J. Mol. Evol. 48:187-196(1999).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16551474; DOI=10.1016/j.toxicon.2006.01.015;
RA Nascimento D.G., Rates B., Santos D.M., Verano-Braga T., Barbosa-Silva A.,
RA Dutra A.A.A., Biondi I., Martin-Eauclaire M.-F., De Lima M.E.,
RA Pimenta A.M.C.;
RT "Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering
RT analyses to infer phylogenetic relationships in some scorpions from the
RT Buthidae family (Scorpiones).";
RL Toxicon 47:628-639(2006).
CC -!- FUNCTION: Depressant insect toxins cause a transient contraction
CC paralysis followed by a slow flaccid paralysis. They bind voltage-
CC independently to sodium channels (Nav) and block action potentials,
CC primarily by depolarizing the axonal membrane and suppressing the
CC sodium current (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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P68725; -.
DR SMR; P68725; -.
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; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..80
FT /note="Insect toxin 2-13"
FT /id="PRO_0000035194"
FT DOMAIN 22..80
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 80
FT /note="Glycine amide"
FT /evidence="ECO:0000250"
FT DISULFID 31..79
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 83 AA; 9211 MW; 7AC8F444619FE3A2 CRC64;
MKLLLLLIIT ASMLIEGLVN ADVYIRRHDG CKISCTVNDK YCDNECKSEG GSYGYCYAFG
CWCEGLPNDK AWKSETNTCG GKK