3L21_NAJAC
ID 3L21_NAJAC Reviewed; 72 AA.
AC P01389;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Long neurotoxin 1;
DE AltName: Full=Toxin III {ECO:0000303|PubMed:1183429};
OS Naja anchietae (Anchieta's cobra) (Naja haje anchietae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=263737;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1183429; DOI=10.1111/j.1432-1033.1975.tb02355.x;
RA Kopeyan C., Miranda F., Rochat H.;
RT "Amino-acid sequence of toxin III of Naja haje.";
RL Eur. J. Biochem. 58:117-122(1975).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Binds with high affinity to muscular (alpha-1/CHRNA1) and
CC neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and
CC inhibits acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular and neuronal transmission.
CC {ECO:0000250|UniProtKB:P60615}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1183429}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1183429}.
CC -!- TOXIC DOSE: LD(50) is 0.067 mg/kg by subcutaneous injection.
CC {ECO:0000269|PubMed:1183429}.
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; A01660; N2NJ1A.
DR AlphaFoldDB; P01389; -.
DR SMR; P01389; -.
DR TopDownProteomics; P01389; -.
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..72
FT /note="Long neurotoxin 1"
FT /evidence="ECO:0000269|PubMed:1183429"
FT /id="PRO_0000093543"
FT DISULFID 3..21
FT /evidence="ECO:0000250|UniProtKB:P25671"
FT DISULFID 14..42
FT /evidence="ECO:0000250|UniProtKB:P25671"
FT DISULFID 27..31
FT /evidence="ECO:0000250|UniProtKB:P25671"
FT DISULFID 46..57
FT /evidence="ECO:0000250|UniProtKB:P25671"
FT DISULFID 58..63
FT /evidence="ECO:0000250|UniProtKB:P25671"
SQ SEQUENCE 72 AA; 7911 MW; 3DE0C49D59E91086 CRC64;
IRCFITPDVT SQACPDGQNI CYTKTWCDNF CGMRGKRVDL GCAATCPTVK PGVDIKCCST
DNCNPFPTRE RS