ID   3L2L_LATLA              Reviewed;          87 AA.
AC   Q7T2I3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Long neurotoxin LlLong;
DE   Flags: Precursor; Fragment;
OS   Laticauda laticaudata (Blue-ringed sea krait) (Blue-lipped sea krait).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Laticaudinae; Laticauda.
OX   NCBI_TaxID=8630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=12957382; DOI=10.1016/s0378-1119(03)00637-1;
RA   Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T.;
RT   "Molecular evolution and diversification of snake toxin genes, revealed by
RT   analysis of intron sequences.";
RL   Gene 313:111-118(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:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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   EMBL; AB098533; BAC78205.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7T2I3; -.
DR   SMR; Q7T2I3; -.
DR   PRIDE; Q7T2I3; -.
DR   Proteomes; UP000694406; Unplaced.
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;
KW   Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          <1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..87
FT                   /note="Long neurotoxin LlLong"
FT                   /id="PRO_0000316166"
FT   DISULFID        23..41
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..83
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   87 AA;  9769 MW;  2151DE31AB10ED99 CRC64;
     KTLLLTLVVV TIICLDFGYT RICFKTPYVK SETCPPGQEL CYTKTWCDRF CSIRGKVIEL
     GCTATCPRAE PKEDTTCCSK DNCNPHP