ID   3S1A1_NAJSP             Reviewed;          83 AA.
AC   Q9YGJ6; Q91138;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Alpha-neurotoxin NTX-1;
DE            Short=NTX1;
DE   Flags: Precursor;
OS   Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=33626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=10077532;
RA   Afifiyan F., Armugam A., Tan C.H., Gopalakrishnakone P., Jeyaseelan K.;
RT   "Postsynaptic alpha-neurotoxin gene of the spitting cobra, Naja naja
RT   sputatrix: structure, organization, and phylogenetic analysis.";
RL   Genome Res. 9:259-266(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-83.
RC   TISSUE=Venom gland;
RA   Jeyaseelan K., Armugam A., Lachumanan R., Earnest L., Tan N.H., Tan C.H.,
RA   Gopalakrishnakone P.P.;
RT   "Cloning of genes encoding neurotoxin in the venom of naja naja
RT   sputatrix.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   EMBL; AF096999; AAD08812.1; -; Genomic_DNA.
DR   EMBL; L42002; AAA66025.1; -; mRNA.
DR   AlphaFoldDB; Q9YGJ6; -.
DR   SMR; Q9YGJ6; -.
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   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..83
FT                   /note="Alpha-neurotoxin NTX-1"
FT                   /id="PRO_0000035457"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        38..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        64..75
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   DISULFID        76..81
FT                   /evidence="ECO:0000250|UniProtKB:P0C1Z0"
FT   CONFLICT        26
FT                   /note="N -> D (in Ref. 2; AAA66025)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   83 AA;  9220 MW;  F9CAD71A93B7AF75 CRC64;
     MKTLLLTLLV VTIVCLDLGY TLECHNQQSS ETPTTTGCSG GETNCYKKSW RDHRGYRIER
     GCGCPSVKKG IEINCCTTDR CNN