ID   3L221_NAJAN             Reviewed;          71 AA.
AC   P34074;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Long neurotoxin 1;
DE            Short=NXL1;
OS   Naja annulata annulata (Banded water cobra) (Boulengerina annulata
OS   annulata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8610;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=15284021; DOI=10.1016/j.toxicon.2004.02.018;
RA   Ogawa Y., Yanoshita R., Kuch U., Samejima Y., Mebs D.;
RT   "Complete amino acid sequence and phylogenetic analysis of a long-chain
RT   neurotoxin from the venom of the African banded water cobra, Boulengerina
RT   annulata.";
RL   Toxicon 43:855-858(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-28, FUNCTION, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=1814007; DOI=10.1016/0041-0101(91)90118-b;
RA   Weinstein S.A., Schmidt J.J., Smith L.A.;
RT   "Lethal toxins and cross-neutralization of venoms from the African water
RT   cobras, Boulengerina annulata annulata and Boulengerina christyi.";
RL   Toxicon 29:1315-1327(1991).
CC   -!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and
CC       neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC       hinders acetylcholine binding to the receptor, thereby impairing
CC       neuromuscular and neuronal transmission. {ECO:0000250|UniProtKB:P60615,
CC       ECO:0000269|PubMed:1814007}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1814007}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:15284021}.
CC   -!- TOXIC DOSE: LD(50) is 0.086 mg/kg by intraperitoneal injection.
CC       {ECO:0000269|PubMed:1814007}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC       subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   PIR; C39327; C39327.
DR   AlphaFoldDB; P34074; -.
DR   SMR; P34074; -.
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   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..71
FT                   /note="Long neurotoxin 1"
FT                   /evidence="ECO:0000269|PubMed:15284021"
FT                   /id="PRO_0000093532"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        14..41
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        26..30
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        45..56
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        57..62
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   VARIANT         28
FT                   /note="N -> V"
FT   VARIANT         36
FT                   /note="R -> A"
SQ   SEQUENCE   71 AA;  7768 MW;  92860BEB031F14A8 CRC64;
     IRCFITPRVS SQACPDGHVC YTKTWCDNFC GINGKRVDLG CAATCPTVKP GVDIKCCSTD
     NCNPFPTRKR P