3NO28_NAJSP
ID 3NO28_NAJSP Reviewed; 86 AA.
AC Q802B3; Q9W7I4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Weak neurotoxin 8;
DE Short=Wntx-8;
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].
RC TISSUE=Venom gland;
RX PubMed=12199703; DOI=10.1046/j.1432-1033.2002.03113.x;
RA Poh S.L., Mourier G., Thai R., Armugam A., Molgo J., Servent D.,
RA Jeyaseelan K., Menez A.;
RT "A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken
RT alpha7 nicotinic acetylcholine receptors.";
RL Eur. J. Biochem. 269:4247-4256(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=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 low affinity to muscular (alpha-1-beta-1-delta-
CC epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal
CC (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC {ECO:0000250|UniProtKB:O42255}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O42255}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR EMBL; AF098923; AAD39353.1; -; mRNA.
DR EMBL; AY081760; AAL87466.1; -; Genomic_DNA.
DR AlphaFoldDB; Q802B3; -.
DR SMR; Q802B3; -.
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 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..86
FT /note="Weak neurotoxin 8"
FT /id="PRO_0000035477"
FT DISULFID 24..45
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 27..32
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 38..63
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 67..78
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT DISULFID 79..84
FT /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT VARIANT 9
FT /note="V -> L"
SQ SEQUENCE 86 AA; 9809 MW; 70DEFB05D9B66638 CRC64;
MKTLLLTLVV VTIVCLDLGY TLTCLNCPEM FCGKFQTCRN GEKICFKMLQ QRRPFSLRYI
RGCAATCPGT KPRDMVECCS TDRCNR