ID   3L231_OPHHA             Reviewed;          94 AA.
AC   Q53B55;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Long neurotoxin-like OH-31;
DE   Flags: Precursor;
OS   Ophiophagus hannah (King cobra) (Naja hannah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX   NCBI_TaxID=8665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15302536; DOI=10.1016/j.toxicon.2004.06.003;
RA   He Y.-Y., Lee W.-H., Zhang Y.;
RT   "Cloning and purification of alpha-neurotoxins from king cobra (Ophiophagus
RT   hannah).";
RL   Toxicon 44:295-303(2004).
CC   -!- FUNCTION: Binds with high affinity to muscular nicotinic acetylcholine
CC       receptors (nAChRs), whereas it binds with a low affinity to neuronal
CC       alpha-7/CHRNA7 nAChRs. {ECO:0000250|UniProtKB:P0C8R6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Has the length of long neurotoxins, but only 4 disulfide
CC       bonds, as short neurotoxins. In addition, the position of cysteine
CC       residues is not conserved. {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; AY596931; AAT97253.1; -; mRNA.
DR   AlphaFoldDB; Q53B55; -.
DR   SMR; Q53B55; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..94
FT                   /note="Long neurotoxin-like OH-31"
FT                   /id="PRO_0000316090"
FT   DISULFID        35..55
FT                   /evidence="ECO:0000305"
FT   DISULFID        37..66
FT                   /evidence="ECO:0000305"
FT   DISULFID        70..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..87
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   94 AA;  10154 MW;  FCB3555A59B53859 CRC64;
     MKTLLLTLVV VTILCLDLGL ELTNAPDSWS SRRTCLCPAW VPLRSRPVAG HSKQCGSRGR
     RVDLGCAATC PIVKPGVNIN CCSTDNCNPF PKRS