SCX8_PARGR
ID SCX8_PARGR Reviewed; 82 AA.
AC B7SNV8; P85979;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Toxin Pg8 {ECO:0000303|PubMed:19233226};
DE Flags: Precursor;
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] {ECO:0000305, ECO:0000312|EMBL:ACD35698.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-82, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND TOXIC DOSE.
RC TISSUE=Venom {ECO:0000269|PubMed:19233226};
RX PubMed=19233226; DOI=10.1016/j.toxicon.2009.02.011;
RA Garcia-Gomez B.I., Olamendi-Portugal T.C., Paniagua J., van der Walt J.,
RA Dyason K., Possani L.D.;
RT "Heterologous expression of a gene that codes for Pg8, a scorpion toxin of
RT Parabuthus granulatus, capable of generating protecting antibodies in
RT mice.";
RL Toxicon 53:770-778(2009).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19233226}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19233226}.
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=7349.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19233226};
CC -!- TOXIC DOSE: LD(50) is 180 ug/kg in mice. {ECO:0000269|PubMed:19233226}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. Alpha subfamily. {ECO:0000255}.
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DR EMBL; EU514685; ACD35698.1; -; mRNA.
DR AlphaFoldDB; B7SNV8; -.
DR SMR; B7SNV8; -.
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; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:19233226"
FT CHAIN 20..82
FT /note="Toxin Pg8"
FT /evidence="ECO:0000269|PubMed:19233226"
FT /id="PRO_5000419245"
FT DOMAIN 21..81
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..80
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 82 AA; 9315 MW; B6D2085823BDFFC6 CRC64;
MNYLLVLTLA SLLALGVNGK KDGYPVDHAN CKYECWYDDK YCDDLCKKRK ADSGYCYKLN
ISCYCLGLPD NAAIKDYGRC RP
