3S11_NAJOX
ID 3S11_NAJOX Reviewed; 61 AA.
AC P01427;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Short neurotoxin 1;
DE AltName: Full=Neurotoxin II {ECO:0000303|PubMed:4747603, ECO:0000303|PubMed:8504813};
DE Short=NT II {ECO:0000303|PubMed:26221036};
DE Short=NTII {ECO:0000303|PubMed:8504813};
DE Short=NTX II;
DE AltName: Full=Neurotoxin alpha {ECO:0000303|PubMed:4850498};
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4850498; DOI=10.1016/0005-2795(74)90217-7;
RA Arnberg H., Eaker D., Fryklund L., Karlsson E.;
RT "Amino acid sequence of oxiana alpha, the main neurotoxin of the venom of
RT Naja naja oxiana.";
RL Biochim. Biophys. Acta 359:222-232(1974).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE.
RX PubMed=4747603; DOI=10.1016/0014-5793(73)80340-0;
RA Grishin E.V., Sukhikh A.P., Lukyanchuk N.N., Slobodyan L.N., Lipkin V.M.,
RA Ovchinnikov Y.A., Sorokin V.M.;
RT "Amino acid sequence of neurotoxin II from Naja naja oxiana venom.";
RL FEBS Lett. 36:77-78(1973).
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).
RN [4]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=8504813; DOI=10.1111/j.1432-1033.1993.tb17872.x;
RA Golovanov A.P., Lomize A.L., Arseniev A.S., Utkin Y.N., Tsetlin V.I.;
RT "Two-dimensional 1H-NMR study of the spatial structure of neurotoxin II
RT from Naja naja oxiana.";
RL Eur. J. Biochem. 213:1213-1223(1993).
CC -!- FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and
CC inhibit acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular transmission. {ECO:0000250|UniProtKB:P60775}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4850498}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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. Short-chain
CC subfamily. Type I alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR PIR; A01696; N1NJ1R.
DR PDB; 1NOR; NMR; -; A=1-61.
DR PDB; 2MJ4; NMR; -; A=1-61.
DR PDBsum; 1NOR; -.
DR PDBsum; 2MJ4; -.
DR AlphaFoldDB; P01427; -.
DR BMRB; P01427; -.
DR SMR; P01427; -.
DR EvolutionaryTrace; P01427; -.
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 SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..61
FT /note="Short neurotoxin 1"
FT /evidence="ECO:0000269|PubMed:4850498"
FT /id="PRO_0000093607"
FT DISULFID 3..23
FT /evidence="ECO:0000269|PubMed:8504813,
FT ECO:0000312|PDB:1NOR, ECO:0000312|PDB:2MJ4"
FT DISULFID 17..40
FT /evidence="ECO:0000269|PubMed:8504813,
FT ECO:0000312|PDB:1NOR, ECO:0000312|PDB:2MJ4"
FT DISULFID 42..53
FT /evidence="ECO:0000269|PubMed:8504813,
FT ECO:0000312|PDB:1NOR, ECO:0000312|PDB:2MJ4"
FT DISULFID 54..59
FT /evidence="ECO:0000269|PubMed:8504813,
FT ECO:0000312|PDB:1NOR, ECO:0000312|PDB:2MJ4"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1NOR"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1NOR"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:1NOR"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:1NOR"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1NOR"
SQ SEQUENCE 61 AA; 6885 MW; 74A0F7DA82FDF961 CRC64;
LECHNQQSSQ PPTTKTCSGE TNCYKKWWSD HRGTIIERGC GCPKVKPGVN LNCCRTDRCN
N
