ID   3NO25_NAJSP             Reviewed;          86 AA.
AC   O42255;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Weak neurotoxin 5 {ECO:0000303|PubMed:12199703};
DE            Short=Wntx-5 {ECO:0000303|PubMed:12199703};
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], SYNTHESIS OF 22-86, AND FUNCTION.
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 and very low affinity to
CC       neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC       {ECO:0000269|PubMed:12199703}.
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. Ancestral
CC       subfamily. Orphan group II 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; AF026891; AAB87415.1; -; mRNA.
DR   EMBL; AY081761; AAL87467.1; -; Genomic_DNA.
DR   AlphaFoldDB; O42255; -.
DR   SMR; O42255; -.
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 5"
FT                   /evidence="ECO:0000305|PubMed:12199703"
FT                   /id="PRO_0000035475"
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"
SQ   SEQUENCE   86 AA;  9806 MW;  0EA0FB05D9B663C2 CRC64;
     MKTLLLTLVV VTIVCLDLGY TLTCLNCPEM FCGKFQTCRN GEKICFKKLQ QRRPFSLRYI
     RGCAATCPGT KPRDMVECCS TDRCNR