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3SX7_OPHHA
ID   3SX7_OPHHA              Reviewed;          78 AA.
AC   Q53B48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Short neurotoxin OH-46 {ECO:0000303|PubMed:15302536};
DE   AltName: Full=Three-finger toxin;
DE            Short=3FTx;
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: This three-finger toxin binds and inhibits the nicotinic
CC       acetylcholine receptor (nAChR). {ECO:0000250|UniProtKB:P83302}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 49 (Pro-31 in standard classification).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AY596938; AAT97260.1; -; mRNA.
DR   AlphaFoldDB; Q53B48; -.
DR   SMR; Q53B48; -.
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   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   SUPFAM; SSF57302; SSF57302; 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..78
FT                   /note="Short neurotoxin OH-46"
FT                   /id="PRO_5000093330"
FT   SITE            28
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and
FT                   neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            43
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and
FT                   neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            44
FT                   /note="Key residue for inhibition of muscle alpha-1-beta-1-
FT                   delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            45
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            46
FT                   /note="Key residue for inhibition of muscle alpha-1-beta-1-
FT                   delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and important for
FT                   inhibition of neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            47
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            48
FT                   /note="Key residue for inhibition of muscle alpha-1-beta-1-
FT                   delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and important
FT                   residue for inhibition of neuronal alpha-3-beta-2/CHRNA3-
FT                   CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            51
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and
FT                   neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            66
FT                   /note="Important residue for inhibition of muscle alpha-1-
FT                   beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and
FT                   neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   SITE            67
FT                   /note="Important residue for interaction with muscle alpha-
FT                   1-beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) and
FT                   neuronal alpha-3-beta-2/CHRNA3-CHRNB2 nAChR"
FT                   /evidence="ECO:0000250|UniProtKB:P83302"
FT   DISULFID        24..40
FT                   /evidence="ECO:0000250|UniProtKB:P0DKR6"
FT   DISULFID        33..58
FT                   /evidence="ECO:0000250|UniProtKB:P0DKR6"
FT   DISULFID        62..70
FT                   /evidence="ECO:0000250|UniProtKB:P0DKR6"
FT   DISULFID        71..76
FT                   /evidence="ECO:0000250|UniProtKB:P0DKR6"
SQ   SEQUENCE   78 AA;  8893 MW;  5197621679DCD59A CRC64;
     MKNLLLTFLV VTIVCLDLGY TLICHQVHGL QTCEPAQKFC QIRTTMFFPN HPVLLMGCTY
     NCPTERYSVC CSTDKCNK
 
 
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