T3G1B_AGEOR
ID T3G1B_AGEOR Reviewed; 74 AA.
AC Q5Y4V7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=U3-agatoxin-Ao1b;
DE Short=U3-AGTX-Ao1b;
DE AltName: Full=Mu-2Aga_03 {ECO:0000312|EMBL:AAU87887.1};
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).
CC -!- FUNCTION: Insecticidal neurotoxin that induces an irreversible spastic
CC paralysis when injected into insects. Modifies presynaptic voltage-
CC gated sodium channels (Nav), causing them to open at the normal resting
CC potential of the nerve. This leads to spontaneous release of
CC neurotransmitter and repetitive action potentials in motor neurons (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 02
CC (aga-3) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY681327; AAU87887.1; -; mRNA.
DR AlphaFoldDB; Q5Y4V7; -.
DR SMR; Q5Y4V7; -.
DR ArachnoServer; AS000085; U3-agatoxin-Ao1b.
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 2: Evidence at transcript level;
KW Amidation; Disulfide bond; Ion channel impairing toxin; Knottin;
KW Neurotoxin; Presynaptic 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:0000255"
FT /id="PRO_5000093657"
FT CHAIN 35..72
FT /note="U3-agatoxin-Ao1b"
FT /id="PRO_5000093658"
FT MOD_RES 72
FT /note="Serine 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"
FT DISULFID 60..66
FT /evidence="ECO:0000250"
SQ SEQUENCE 74 AA; 8326 MW; DB96B32058BC5360 CRC64;
MKAAISLIIF FAILFVVIEA ISYEEGKELF QKERAECVGD GQRCADWAGP YCCSGYYCSC
RSMPYCRCRS DSGK