ID   TX31A_SELPU             Reviewed;          79 AA.
AC   P0DM66;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Orally active insecticidal peptide {ECO:0000303|PubMed:23894279};
DE            Short=Toxin OAIP 2 {ECO:0000303|PubMed:23894279};
DE   Flags: Precursor;
OS   Selenotypus plumipes (Australian featherleg tarantula).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Mygalomorphae; Theraphosidae; Selenotypus.
OX   NCBI_TaxID=1395661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23894279; DOI=10.1371/journal.pone.0066279;
RA   Wong E.S., Hardy M.C., Wood D., Bailey T., King G.F.;
RT   "SVM-based prediction of propeptide cleavage sites in spider toxins
RT   identifies toxin innovation in an australian tarantula.";
RL   PLoS ONE 8:E66279-E66279(2013).
CC   -!- FUNCTION: Probable ion channel inhibitor. Shows insecticidal activity
CC       when injected into mealworms. {ECO:0000269|PubMed:23894279}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23894279}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23894279}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 01 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DM66; -.
DR   SMR; P0DM66; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..44
FT                   /evidence="ECO:0000269|PubMed:23894279"
FT                   /id="PRO_0000424394"
FT   CHAIN           45..77
FT                   /note="Orally active insecticidal peptide"
FT                   /evidence="ECO:0000305|PubMed:23894279"
FT                   /id="PRO_0000424395"
FT   MOD_RES         77
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000250|UniProtKB:P84507"
FT   DISULFID        53..66
FT                   /evidence="ECO:0000250|UniProtKB:P84507"
FT   DISULFID        60..73
FT                   /evidence="ECO:0000250|UniProtKB:P84507"
SQ   SEQUENCE   79 AA;  9128 MW;  53C6B205FDB1867E CRC64;
     MRVLFIIAGL ALLSVVCYTS EMKERSSFNE VLSEFFAADE PQERDCLGQW ASCEPKNSKC
     CPNYACTWKY PWCRYRAGK