SCN3_MESMA
ID SCN3_MESMA Reviewed; 85 AA.
AC Q9BKJ0; Q6EN21; Q9GZC4;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Anti-neuroexcitation peptide 3;
DE Short=BmKANEP3;
DE AltName: Full=Anti-epilepsy peptide;
DE AltName: Full=Anti-neuroexcitation peptide III;
DE Short=ANEPIII;
DE AltName: Full=Toxin KIM;
DE Flags: Precursor;
OS Mesobuthus martensii (Manchurian scorpion) (Buthus martensii).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34649;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Zhang J.-H., Hua Z.C., Zhu D.X.;
RT "Cloning of anti-epilepsy peptide cDNA from scorpion Buthus martensii
RT Karsch.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Zhang J.-H., Hua Z.C., Zhu D.X.;
RT "Cloning of anti-neuroexcitation peptide III (ANEP) cDNA from Scorpion
RT Buthus martensii Karsch.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Zeng X.-C., Peng F., Li W.-X.;
RT "Nucleotide sequence of scorpion toxin.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=11321163; DOI=10.1081/pb-100103371;
RA Zhang J.-H., Hua Z.C., Xu Z., Zheng W.J., Zhu D.X.;
RT "Expression of anti-neuroexcitation peptide (ANEP) of scorpion Buthus
RT martensii Karsch in Escherichia coli.";
RL Prep. Biochem. Biotechnol. 31:49-57(2001).
CC -!- FUNCTION: Binds to sodium channels (Nav) and inhibits them (By
CC similarity). Recombinant ANEP delays the convulsion seizure of model
CC animals by 18% and shows anti-neuroexcitatory activity. {ECO:0000250,
CC ECO:0000269|PubMed:11321163}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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}.
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DR EMBL; AF122003; AAG01571.1; -; mRNA.
DR EMBL; AF242737; AAK28342.1; -; mRNA.
DR EMBL; AY040630; AAK94768.1; -; Genomic_DNA.
DR EMBL; AY040631; AAK94769.1; -; mRNA.
DR AlphaFoldDB; Q9BKJ0; -.
DR SMR; Q9BKJ0; -.
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 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..85
FT /note="Anti-neuroexcitation peptide 3"
FT /id="PRO_0000035265"
FT DOMAIN 22..82
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 31..81
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"
FT CONFLICT 47
FT /note="K -> I (in Ref. 2; AAK28342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 85 AA; 9271 MW; C1D6C93A2F82F8C2 CRC64;
MKLSLLLVIS ASMLIDGLVN ADGYIRGSNG CKISCLWGNE GCNKECKGFG AYYGYCWTWG
LACWCEGLPD DKTWKSESNT CGGKK