3L22_AUSSU
ID 3L22_AUSSU Reviewed; 92 AA.
AC A8S6B0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Alpha-elapitoxin-As2a;
DE Short=Alpha-EPTX-As2a;
DE AltName: Full=Long neurotoxin 2;
DE Short=LNTX-2;
DE Flags: Precursor;
OS Austrelaps superbus (Lowland copperhead snake) (Hoplocephalus superbus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Austrelaps.
OX NCBI_TaxID=29156;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17906946; DOI=10.1007/s00018-007-7352-z;
RA St Pierre L., Fischer H., Adams D.J., Schenning M., Lavidis N.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Distinct activities of novel neurotoxins from Australian venomous snakes
RT for nicotinic acetylcholine receptors.";
RL Cell. Mol. Life Sci. 64:2829-2840(2007).
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; EF599319; ABW24176.1; -; mRNA.
DR AlphaFoldDB; A8S6B0; -.
DR SMR; A8S6B0; -.
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..92
FT /note="Alpha-elapitoxin-As2a"
FT /id="PRO_5000282346"
FT DISULFID 24..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"
SQ SEQUENCE 92 AA; 9914 MW; 4B96C5CBB38044F6 CRC64;
MKTLLLTLVV VTIVCLDLGD GLICYVDSKT SRTCPPGENV CFTETWCDAR CSLLGKRVDL
GCAATCPTAK PGVDITCCST DKCNPFPTQK HR