ID   TXAG_ALLOP              Reviewed;          35 AA.
AC   P31328;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=U2-agatoxin-Aop1a;
DE            Short=U2-AGTX-Aop1a;
DE   AltName: Full=Agelenin;
OS   Allagelena opulenta (Funnel weaving spider) (Agelena opulenta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Agelenidae; Allagelena.
OX   NCBI_TaxID=29934;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RA   Hagiwara K., Sakai T., Miwa A., Kawai N., Nakajima T.;
RT   "Complete amino acid sequence of a new type of neurotoxin from the venom of
RT   the spider, Agelena opulenta.";
RL   Biomed. Res. 11:181-186(1990).
RN   [2]
RP   DISULFIDE BONDS, AND AMIDATION AT LEU-35.
RC   TISSUE=Venom;
RA   Hagiwara K., Inui T., Nakajima K., Kimura T., Kitada C., Fujino M.,
RA   Sakakibara S., Nakajima T.;
RT   "Agelenin, a spider neurotoxin: determination of the C-terminus as amide
RT   form, and investigation of the disulfide bond arrangement.";
RL   Biomed. Res. 12:357-363(1991).
RN   [3]
RP   SYNTHESIS, DISULFIDE BONDS, AND AMIDATION AT LEU-35.
RC   TISSUE=Venom;
RX   PubMed=1421801;
RA   Inui T., Hagiwara K., Nakajima K., Kimura T., Nakajima T., Sakakibara S.;
RT   "Synthesis and disulfide structure determination of agelenin:
RT   identification of the carboxy-terminus as an amide form.";
RL   Pept. Res. 5:140-144(1992).
RN   [4]
RP   STRUCTURE BY NMR, DISULFIDE BONDS, AMIDATION AT LEU-35, FUNCTION, AND TOXIC
RP   DOSE.
RX   PubMed=17644092; DOI=10.1016/j.febslet.2007.06.077;
RA   Yamaji N., Sugase K., Nakajima T., Miki T., Wakamori M., Mori Y.,
RA   Iwashita T.;
RT   "Solution structure of agelenin, an insecticidal peptide isolated from the
RT   spider Agelena opulenta, and its structural similarities to insect-specific
RT   calcium channel inhibitors.";
RL   FEBS Lett. 581:3789-3794(2007).
CC   -!- FUNCTION: Insect-selective toxin causing rapid but reversible paralysis
CC       in crickets. Suppresses the excitatory postsynaptic potentials evoked
CC       in lobster neuromuscular synaptic preparations, possibly by blocking
CC       the presynaptic calcium channel (Cav). Induces instantaneous reversible
CC       paralysis when injected into crickets. {ECO:0000269|PubMed:17644092}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC   -!- TOXIC DOSE: PD(50) is 291 pmol/g of crickets.
CC       {ECO:0000269|PubMed:17644092}.
CC   -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC       to that of U2-agatoxin-Ao1a (Agelenin) from Agelena orientalis (AC
CC       Q5Y4Y5). {ECO:0000305}.
CC   -!- MISCELLANEOUS: This toxin does not inhibit mammalian Cav2.1/CACNA1A,
CC       Cav2.2/CACNA1B and Cav2.3/CACNA1E calcium channels.
CC       {ECO:0000305|PubMed:17644092}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 01 (U2-agtx) family.
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DR   PIR; A60959; A60959.
DR   PDB; 2E2S; NMR; -; A=1-35.
DR   PDBsum; 2E2S; -.
DR   AlphaFoldDB; P31328; -.
DR   SMR; P31328; -.
DR   ArachnoServer; AS000286; U2-agatoxin-Aop1a.
DR   EvolutionaryTrace; P31328; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium 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; Calcium channel impairing toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   PEPTIDE         1..35
FT                   /note="U2-agatoxin-Aop1a"
FT                   /id="PRO_0000044985"
FT   SITE            9
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            28
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   SITE            33
FT                   /note="Critical for insecticidal activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:1421801,
FT                   ECO:0000269|PubMed:17644092, ECO:0000269|Ref.2"
FT   DISULFID        3..19
FT   DISULFID        10..24
FT   DISULFID        18..34
FT   STRAND          12..15
FT                   /evidence="ECO:0007829|PDB:2E2S"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:2E2S"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:2E2S"
SQ   SEQUENCE   35 AA;  3825 MW;  CBE6462825350D90 CRC64;
     GGCLPHNRFC NALSGPRCCS GLKCKELSIW DSRCL