SCX1_ANUPH
ID SCX1_ANUPH Reviewed; 90 AA.
AC Q5MJP5; P84207;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Phaiodotoxin;
DE Flags: Precursor;
GN Name=phtx {ECO:0000312|EMBL:AAW29437.1};
OS Anuroctonus phaiodactylus (Mafia scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Iurida; Chactoidea; Chactidae; Uroctoninae; Anuroctonus.
OX NCBI_TaxID=246982;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW29437.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-90, FUNCTION, BIOASSAY,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND DISULFIDE
RP BONDS.
RC TISSUE=Venom {ECO:0000269|PubMed:15606762};
RX PubMed=15606762; DOI=10.1111/j.1432-1033.2004.04439.x;
RA Valdez-Cruz N.A., Batista C.V.F., Zamudio F.Z., Bosmans F., Tytgat J.,
RA Possani L.D.;
RT "Phaiodotoxin, a novel structural class of insect-toxin isolated from the
RT venom of the Mexican scorpion Anuroctonus phaiodactylus.";
RL Eur. J. Biochem. 271:4753-4761(2004).
CC -!- FUNCTION: Sodium channel (Nav) specific neurotoxin. Causes impairment
CC of movement and mild paralysis in crickets at a dose of 0.5 ug per
CC animal. A dose of 0.8 ug per cricket causes clear flaccid paralysis. A
CC dose of 1.0 ug per cricket causes death within 2 hours.
CC {ECO:0000269|PubMed:15606762}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15606762}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:15606762}.
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=7971; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15606762};
CC -!- MISCELLANEOUS: Non-toxic to mice at a dose of 100 ug per 20 g mouse
CC weight. {ECO:0000305|PubMed:15606762}.
CC -!- SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily.
CC Sodium channel inhibitor family. {ECO:0000305}.
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DR EMBL; AY781122; AAW29437.1; -; mRNA.
DR AlphaFoldDB; Q5MJP5; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 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..18
FT /evidence="ECO:0000269|PubMed:15606762"
FT CHAIN 19..90
FT /note="Phaiodotoxin"
FT /evidence="ECO:0000269|PubMed:15606762"
FT /id="PRO_0000035234"
FT DOMAIN 19..90
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:15606762"
FT DISULFID 41..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:15606762"
FT DISULFID 45..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:15606762"
FT DISULFID 81..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210,
FT ECO:0000269|PubMed:15606762"
SQ SEQUENCE 90 AA; 10124 MW; BB6FD57A8A47F2A6 CRC64;
MKTIPLLFLL FIYFECDGKF IRHKDESFYE CGQLIGYQQY CVDACQAHGS KEKGYCKGMA
PFGLPGGCYC PKLPSNRVKM CFGALESKCA