ID   TX1_SELPU               Reviewed;          94 AA.
AC   K7N5K9;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=U1-theraphotoxin-Sp1a {ECO:0000305};
DE            Short=U1-TRTX-Sp1a {ECO:0000305};
DE   AltName: Full=Orally active insecticidal peptide 1 {ECO:0000303|PubMed:24039872};
DE            Short=OAIP-1 {ECO:0000303|PubMed:24039872};
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, BIOASSAY,
RP   AND 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).
RN   [2]
RP   PROTEIN SEQUENCE OF 59-90, FUNCTION, BIOASSAY, SYNTHESIS OF 59-92, TOXIC
RP   DOSE, STRUCTURE BY NMR OF 59-91, AND DISULFIDE BONDS.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=24039872; DOI=10.1371/journal.pone.0073136;
RA   Hardy M.C., Daly N.L., Mobli M., Morales R.A., King G.F.;
RT   "Isolation of an orally active insecticidal toxin from the venom of an
RT   Australian tarantula.";
RL   PLoS ONE 8:E73136-E73136(2013).
CC   -!- FUNCTION: Probable ion channel inhibitor. Shows insecticidal activity.
CC       Acts synergistically with the neonicotinoid insecticide imidacloprid.
CC       Is neither a repellent that repels insects nor an attractant that is
CC       preferentially consumed by insects. Is very stable.
CC       {ECO:0000269|PubMed:23894279, ECO:0000269|PubMed:24039872}.
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.
CC       {ECO:0000269|PubMed:24039872}.
CC   -!- TOXIC DOSE: LD(50) is 1.84 +-0.8 nmol/g in mealworm.
CC       {ECO:0000269|PubMed:24039872}.
CC   -!- TOXIC DOSE: LD(50) is 170.5 +- 0.2 nmol/g when orally administered into
CC       mealworm. {ECO:0000269|PubMed:24039872}.
CC   -!- TOXIC DOSE: LD(50) is 104.2 +-0.6 pmol/g when orally administred into
CC       the cotton bollworm H.armigera. {ECO:0000269|PubMed:24039872}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. OAIP-1
CC       subfamily.
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DR   PDB; 2LL1; NMR; -; A=59-91.
DR   PDBsum; 2LL1; -.
DR   AlphaFoldDB; K7N5K9; -.
DR   BMRB; K7N5K9; -.
DR   SMR; K7N5K9; -.
DR   ArachnoServer; AS001495; U1-theraphotoxin-Spl1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..58
FT                   /evidence="ECO:0000269|PubMed:24039872"
FT                   /id="PRO_0000424392"
FT   CHAIN           59..92
FT                   /note="U1-theraphotoxin-Sp1a"
FT                   /evidence="ECO:0000305|PubMed:23894279"
FT                   /id="PRO_0000424393"
FT   MOD_RES         92
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..78
FT                   /evidence="ECO:0000269|PubMed:24039872,
FT                   ECO:0000312|PDB:2LL1"
FT   DISULFID        67..83
FT                   /evidence="ECO:0000269|PubMed:24039872,
FT                   ECO:0000312|PDB:2LL1"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000269|PubMed:24039872,
FT                   ECO:0000312|PDB:2LL1"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:2LL1"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:2LL1"
SQ   SEQUENCE   94 AA;  10749 MW;  88CDC464A003FCC5 CRC64;
     MIFLLPSIIS VMLLAEPVLM LGDTEDADLM EMVQLSRPFF NPIIRAVELV ELREERQRDC
     GHLHDPCPND RPGHRTCCIG LQCRYGKCLV RVGR