ID   PLK1_AGRDO              Reviewed;          35 AA.
AC   P58608;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Toxin Ado1 {ECO:0000303|PubMed:11423127};
OS   Agriosphodrus dohrni (Japanese assassin-bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Harpactorinae; Harpactorini; Agriosphodrus.
OX   NCBI_TaxID=184613;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Saliva;
RX   PubMed=11423127; DOI=10.1016/s0014-5793(01)02558-3;
RA   Corzo G., Adachi-Akahane S., Nagao T., Kusui Y., Nakajima T.;
RT   "Novel peptides from assassin bugs (Hemiptera: Reduviidae): isolation,
RT   chemical and biological characterization.";
RL   FEBS Lett. 499:256-261(2001).
RN   [2]
RP   STRUCTURE BY NMR, FUNCTION, AND DISULFIDE BOND.
RX   PubMed=14696181; DOI=10.1002/prot.10513;
RA   Bernard C., Corzo G., Adachi-Akahane S., Foures G., Kanemaru K.,
RA   Furukawa Y., Nakajima T., Darbon H.;
RT   "Solution structure of ADO1, a toxin extracted from the saliva of the
RT   assassin bug, Agriosphodrus dohrni.";
RL   Proteins 54:195-205(2004).
CC   -!- FUNCTION: Binds reversibly and blocks P/Q-type voltage-gated calcium
CC       channels (Cav). {ECO:0000269|PubMed:14696181}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11423127}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3781.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11423127};
CC   -!- SIMILARITY: Belongs to the venom Ptu1-like knottin family.
CC       {ECO:0000305}.
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DR   PDB; 1LMR; NMR; -; A=1-35.
DR   PDBsum; 1LMR; -.
DR   AlphaFoldDB; P58608; -.
DR   SMR; P58608; -.
DR   EvolutionaryTrace; P58608; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012325; Assassin_bug_toxin-like.
DR   Pfam; PF08117; Toxin_30; 1.
DR   PROSITE; PS60010; ASSASSIN_BUG_TOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin; Secreted;
KW   Toxin; Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..35
FT                   /note="Toxin Ado1"
FT                   /evidence="ECO:0000269|PubMed:11423127"
FT                   /id="PRO_0000044889"
FT   DISULFID        5..20
FT                   /evidence="ECO:0000269|PubMed:14696181,
FT                   ECO:0007744|PDB:1LMR"
FT   DISULFID        12..25
FT                   /evidence="ECO:0000269|PubMed:14696181,
FT                   ECO:0007744|PDB:1LMR"
FT   DISULFID        19..32
FT                   /evidence="ECO:0000269|PubMed:14696181,
FT                   ECO:0007744|PDB:1LMR"
FT   STRAND          23..26
FT                   /evidence="ECO:0007829|PDB:1LMR"
FT   TURN            27..30
FT                   /evidence="ECO:0007829|PDB:1LMR"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:1LMR"
SQ   SEQUENCE   35 AA;  3787 MW;  3E83D94C6D614E88 CRC64;
     ADDDCLPRGS KCLGENKQCC KGTTCMFYAN RCVGV