ID   KURT1_PARGR             Reviewed;          62 AA.
AC   P0C5F0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Alpha-toxin PgKL1;
DE   AltName: Full=Kurtoxin-like 1;
DE   AltName: Full=Kurtoxin-like I;
DE            Short=KLI;
OS   Parabuthus granulatus (Granulated thick-tailed scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Parabuthus.
OX   NCBI_TaxID=242110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, MASS SPECTROMETRY, AND
RP   FUNCTION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=12459175; DOI=10.1016/s0006-291x(02)02706-7;
RA   Olamendi-Portugal T., Garcia B.I., Lopez-Gonzalez I., Van Der Walt J.,
RA   Dyason K., Ulens C., Tytgat J., Felix R., Darszon A., Possani L.D.;
RT   "Two new scorpion toxins that target voltage-gated Ca2+ and Na+ channels.";
RL   Biochem. Biophys. Res. Commun. 299:562-568(2002).
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 inhibits cardiac
CC       sodium channels and voltage-gated T-type calcium channels
CC       (Cav3.3/CACNA1I). {ECO:0000269|PubMed:12459175}.
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   -!- MASS SPECTROMETRY: Mass=7244.2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12459175};
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   AlphaFoldDB; P0C5F0; -.
DR   SMR; P0C5F0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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   Calcium channel impairing toxin; Cardiotoxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   CHAIN           1..62
FT                   /note="Alpha-toxin PgKL1"
FT                   /id="PRO_0000305104"
FT   DOMAIN          2..62
FT                   /note="LCN-type CS-alpha/beta"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        12..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        16..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        23..44
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT   DISULFID        27..46
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ   SEQUENCE   62 AA;  7252 MW;  ECB247F2C2403FE0 CRC64;
     KIDGYPVDNW NCKRICWYNN KYCYDLCKGL KADSGYCWGW TLSCYCEGLP DNARIKRGGR
     CN