ID   3L27_NAJSP              Reviewed;          90 AA.
AC   O42257;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Long neurotoxin 7 {ECO:0000303|PubMed:14572646};
DE            Short=LNTX7 {ECO:0000303|PubMed:14572646};
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 [MRNA], PROTEIN SEQUENCE OF 22-36, TOXIC DOSE, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=14572646; DOI=10.1016/s0014-5793(03)01039-1;
RA   Jeyaseelan K., Poh S.L., Nair R., Armugam A.;
RT   "Structurally conserved alpha-neurotoxin genes encode functionally diverse
RT   proteins in the venom of Naja sputatrix.";
RL   FEBS Lett. 553:333-341(2003).
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:14572646}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:14572646}.
CC   -!- TOXIC DOSE: LD(50) is 0.14 mg/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:14572646}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC       subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF026893; AAB87417.1; -; mRNA.
DR   EMBL; AY081763; AAL87469.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42257; -.
DR   SMR; O42257; -.
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; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:14572646"
FT   CHAIN           22..90
FT                   /note="Long neurotoxin 7"
FT                   /evidence="ECO:0000305|PubMed:14572646"
FT                   /id="PRO_0000035431"
FT   DISULFID        24..41
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        35..62
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        47..51
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        66..77
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
FT   DISULFID        78..83
FT                   /evidence="ECO:0000250|UniProtKB:P25671"
SQ   SEQUENCE   90 AA;  9841 MW;  FAF8F5EB0FB7D6EC CRC64;
     MKTLLLTLVL VTIMCLDLGY TIRCFITPDV TSTDCPNGHV CYTKTWCDGF CSSRGRRVEL
     GCAATCPTVK PGVDIQCCST DNCNPFPTRP