位置:首页 > 蛋白库 > T4G1C_AGEOR
T4G1C_AGEOR
ID   T4G1C_AGEOR             Reviewed;          73 AA.
AC   Q5Y4V6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=U3-agatoxin-Ao1c {ECO:0000305};
DE            Short=U3-AGTX-Ao1c {ECO:0000305};
DE   AltName: Full=Beta/delta-agatoxin-3 {ECO:0000303|PubMed:20385552};
DE   AltName: Full=Mu-2Aga_04 {ECO:0000312|EMBL:AAU87888.1};
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 35-71, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT SER-71.
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=4145.4; 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}.
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; AY681328; AAU87888.1; -; mRNA.
DR   AlphaFoldDB; Q5Y4V6; -.
DR   SMR; Q5Y4V6; -.
DR   ArachnoServer; AS000084; U3-agatoxin-Ao1c.
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_5000093659"
FT   CHAIN           35..71
FT                   /note="U3-agatoxin-Ao1c"
FT                   /evidence="ECO:0000269|PubMed:20385552"
FT                   /id="PRO_5000093660"
FT   MOD_RES         71
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:20385552"
FT   DISULFID        36..52
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        51..67
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
FT   DISULFID        59..65
FT                   /evidence="ECO:0000250|UniProtKB:P11061"
SQ   SEQUENCE   73 AA;  8114 MW;  E7710DD659F82313 CRC64;
     MRTIISLLLL SAMVFAVIEA ISLEEGLQLF EGERGCVGEN QQCADWAGPH CCSGYYCTCR
     YFPKCICRKD SGK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024