T4G1G_AGEOR
ID T4G1G_AGEOR Reviewed; 74 AA.
AC Q5Y4V2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=U3-agatoxin-Ao1g {ECO:0000305};
DE Short=U3-AGTX-Ao1g {ECO:0000305};
DE AltName: Full=Beta/delta-agatoxin-2 {ECO:0000303|PubMed:20385552};
DE AltName: Full=Mu-2Aga_08 {ECO:0000312|EMBL:AAU87892.1};
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).
RN [2]
RP PROTEIN SEQUENCE OF 35-72, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT ASN-72.
RC TISSUE=Venom;
RX PubMed=20385552; DOI=10.1074/jbc.m110.125211;
RA Billen B., Vassilevski A., Nikolsky A., Debaveye S., Tytgat J., Grishin E.;
RT "Unique bell-shaped voltage-dependent modulation of Na+ channel gating by
RT novel insect-selective toxins from the spider Agelena orientalis.";
RL J. Biol. Chem. 285:18545-18554(2010).
CC -!- FUNCTION: Insecticidal neurotoxin that modulates the insect Nav channel
CC (DmNaV1/tipE (para/tipE)) in a unique manner, with both the activation
CC and inactivation processes being affected. The voltage dependence of
CC activation is shifted toward more hyperpolarized potentials (analogous
CC to site 4 toxins) and a non-inactivating persistent sodium current is
CC induced (site 3-like action). Interestingly, both effects take place in
CC a voltage-dependent manner, producing a bell-shaped curve between -80
CC and 0 mV. {ECO:0000269|PubMed:20385552}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20385552}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20385552}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=4214.5; Mass_error=0.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20385552};
CC -!- MISCELLANEOUS: Does not affect mammalian sodium channels (Nav).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 03
CC (aga-4) subfamily. Aga sub-subfamily. {ECO:0000305}.
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DR EMBL; AY681332; AAU87892.1; -; mRNA.
DR AlphaFoldDB; Q5Y4V2; -.
DR SMR; Q5Y4V2; -.
DR ArachnoServer; AS000080; U3-agatoxin-Ao1g.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR016328; Beta/delta-agatoxin_fam.
DR PROSITE; PS60015; MU_AGATOXIN; 1.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..34
FT /evidence="ECO:0000269|PubMed:20385552"
FT /id="PRO_5000093667"
FT CHAIN 35..72
FT /note="U3-agatoxin-Ao1g"
FT /evidence="ECO:0000269|PubMed:20385552"
FT /id="PRO_5000093668"
FT MOD_RES 72
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:20385552"
FT DISULFID 37..53
FT /evidence="ECO:0000250|UniProtKB:P11061"
FT DISULFID 44..58
FT /evidence="ECO:0000250|UniProtKB:P11061"
FT DISULFID 52..68
FT /evidence="ECO:0000250|UniProtKB:P11061"
FT DISULFID 60..66
FT /evidence="ECO:0000250|UniProtKB:P11061"
SQ SEQUENCE 74 AA; 8141 MW; DF0E2D22F0976A42 CRC64;
MRAIISLLLI STMVFGVIEA VSVEEGLKIF EGERGGCVGE SQQCADWSGP YCCKGYYCTC
RYFPKCICVN DNGK
