AEP2_MESMA
ID AEP2_MESMA Reviewed; 85 AA.
AC Q86M31;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Neurotoxin BmKAEP2;
DE Short=AEP2;
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;
RA Ling M.-H., Wang C.-G., Wang D.-C., Chi C.-W.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Depressant insect beta-toxins cause a transient contraction
CC paralysis followed by a slow flaccid paralysis. They bind voltage-
CC independently at site-4 of sodium channels (Nav) and shift the voltage
CC of activation toward more negative potentials thereby affecting sodium
CC channel activation and promoting spontaneous and repetitive firing.
CC This toxin is active only on insects. Has potential anti-epilepsy
CC effect (By similarity). {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. Beta subfamily. {ECO:0000305}.
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DR EMBL; AF062564; AAC16698.1; -; mRNA.
DR AlphaFoldDB; Q86M31; -.
DR SMR; Q86M31; -.
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:0000250"
FT CHAIN 22..82
FT /note="Neurotoxin BmKAEP2"
FT /id="PRO_0000035213"
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"
SQ SEQUENCE 85 AA; 9331 MW; 80CDD38B9396DE8C CRC64;
MKLFLLLVIS ASMLIDGLVN ADGYIRGSNG CKVSCLWGNE GCNKECKAFG AYYGYCWTWG
LACWCEGLPD DKTWKSESNT CGGKK