SCX8R_ANDMA
ID SCX8R_ANDMA Reviewed; 86 AA.
AC Q2YHM1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Neurotoxin 8-related gene product 1/2/3;
DE AltName: Full=Amm VIIIrgp1;
DE AltName: Full=Amm VIIIrgp2;
DE AltName: Full=Amm VIIIrgp3;
DE Flags: Precursor;
GN Name=NTVIIIrgp1;
OS Androctonus mauritanicus mauritanicus (Scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6860;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND AMIDATION AT ASN-84.
RC TISSUE=Muscle;
RX PubMed=16533515; DOI=10.1016/j.toxicon.2006.01.005;
RA Alami M., Ceard B., Legros C., Bougis P.E., Martin-Eauclaire M.-F.;
RT "Genomic characterisation of the toxin Amm VIII from the scorpion
RT Androctonus mauretanicus mauretanicus.";
RL Toxicon 47:531-536(2006).
CC -!- FUNCTION: Binds voltage-dependently at site-3 of sodium channels (Nav)
CC and inhibits the inactivation of the activated channels, thereby
CC blocking neuronal transmission. {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. Alpha subfamily. {ECO:0000305}.
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DR EMBL; AM159182; CAJ43745.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2YHM1; -.
DR SMR; Q2YHM1; -.
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 3: Inferred from homology;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..84
FT /note="Neurotoxin 8-related gene product 1/2/3"
FT /id="PRO_0000257745"
FT DOMAIN 22..84
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT MOD_RES 84
FT /note="Asparagine amide"
FT /evidence="ECO:0000305|PubMed:16533515"
FT DISULFID 32..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 36..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT CONFLICT 38
FT /note="R -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="I -> V (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="E -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 86 AA; 9598 MW; 37F3E161904BF01B CRC64;
MNYLTMISLA LLVMTGVESG VRDAYIADNK NCIFTCYRDS YCKTECIKNG AETGYCIWIG
EYGNACWCIK LPNKVPIKVP GKCNGR
