ID   3NO2_NAJOX              Reviewed;          65 AA.
AC   P85520;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUN-2019, sequence version 2.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Oxiana weak toxin {ECO:0000303|PubMed:19377518, ECO:0000303|Ref.1};
DE            Short=OWT {ECO:0000303|PubMed:19377518};
OS   Naja oxiana (Central Asian cobra) (Oxus cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8657;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RA   Starkov V.G., Tsetlin V.I., Utkin Y.N.;
RT   "New analogues of weak toxins from cobra venom.";
RL   Submitted (APR-2008) to UniProtKB.
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19377518; DOI=10.1134/s1068162009010026;
RA   Starkov V.G., Polyak Y.L., Vulfius E.A., Kryukova E.V., Tsetlin V.I.,
RA   Utkin Y.N.;
RT   "New weak toxins from the cobra venom.";
RL   Russ. J. Bioorg. Chem. 35:15-24(2009).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=26221036; DOI=10.1074/jbc.m115.648824;
RA   Kudryavtsev D.S., Shelukhina I.V., Son L.V., Ojomoko L.O., Kryukova E.V.,
RA   Lyukmanova E.N., Zhmak M.N., Dolgikh D.A., Ivanov I.A., Kasheverov I.E.,
RA   Starkov V.G., Ramerstorfer J., Sieghart W., Tsetlin V.I., Utkin Y.N.;
RT   "Neurotoxins from snake venoms and alpha-conotoxin ImI inhibit functionally
RT   active ionotropic gamma-aminobutyric acid (GABA) receptors.";
RL   J. Biol. Chem. 290:22747-22758(2015).
CC   -!- FUNCTION: Binds to muscle and neuronal nicotinic acetylcholine
CC       receptors (nAChR) (Ref.1). It binds to extracellular domain of rat
CC       alpha-7/CHRNA7 nAChR (IC(50)=2.2 uM) and to Torpedo californica
CC       membranes (IC(50)=30 uM) (Ref.1). {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=7485; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19377518, ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: Does not inhibit GABA(A) channel composed of alpha-1-
CC       beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) subunits.
CC       {ECO:0000269|PubMed:26221036}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC       subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P85520; -.
DR   SMR; P85520; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..65
FT                   /note="Oxiana weak toxin"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000337170"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        6..11
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        17..42
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   CONFLICT        29
FT                   /note="D -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   65 AA;  7496 MW;  5B5EEBF1507C2B55 CRC64;
     LTCLICPEKY CNKVHTCRNG EKICFKKFDQ RKLLGKRYIR GCAATCPEAK PREIVECCST
     DKCNH