ID   TXAGA_AGEOR             Reviewed;          70 AA.
AC   Q5Y4Y5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=U2-agatoxin-Ao1a;
DE            Short=U2-AGTX-Ao1a;
DE   AltName: Full=Agelenin;
DE   Flags: Precursor;
OS   Agelena orientalis (Funnel-web spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Agelenidae; Agelena.
OX   NCBI_TaxID=293813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15688451; DOI=10.1002/prot.20390;
RA   Kozlov S.A., Malyavka A., McCutchen B., Lu A., Schepers E., Herrmann R.,
RA   Grishin E.V.;
RT   "A novel strategy for the identification of toxinlike structures in spider
RT   venom.";
RL   Proteins 59:131-140(2005).
CC   -!- FUNCTION: Insect active toxin causing rapid but reversible paralysis in
CC       crickets. No activity shown in mammals. Suppresses the excitatory
CC       postsynaptic potentials evoked in lobster neuromuscular synaptic
CC       preparations, possibly by blocking the presynaptic calcium channel.
CC       Induces instantaneous reversible paralysis when injected into crickets.
CC       Does not show effect on mammalian Cav2.1/CACNA1A, Cav2.2/CACNA1B and
CC       Cav2.3/CACNA1E (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC       to that of U2-agatoxin-Aop1a (Agelenin) from Allagelena opulenta (AC
CC       P31328). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the neurotoxin 01 (U2-agtx) family.
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DR   EMBL; AY681297; AAU93655.1; -; mRNA.
DR   AlphaFoldDB; Q5Y4Y5; -.
DR   SMR; Q5Y4Y5; -.
DR   ArachnoServer; AS000287; U2-agatoxin-Ao1a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Amidation; Disulfide bond; Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..34
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000035531"
FT   CHAIN           35..69
FT                   /note="U2-agatoxin-Ao1a"
FT                   /id="PRO_0000035532"
FT   MOD_RES         69
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..68
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   70 AA;  7719 MW;  009AED63B65050D5 CRC64;
     MRAIISLFLI SAMVFSMIQA VPEEEGLQLS EDERGGCLPH NRFCNALSGP RCCSGLKCKE
     LSIWDSRCLG