3SX6_OPHHA
ID 3SX6_OPHHA Reviewed; 78 AA.
AC Q2VBP2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Short neurotoxin SNTX6 {ECO:0000312|EMBL:ABB83627.1};
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=16689684; DOI=10.1042/bj20060004;
RA Li J., Zhang H., Liu J., Xu K.;
RT "Novel genes encoding six kinds of three-finger toxins in Ophiophagus
RT hannah (king cobra) and function characterization of two recombinant long-
RT chain neurotoxins.";
RL Biochem. J. 398:233-242(2006).
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; DQ273573; ABB83627.1; -; mRNA.
DR AlphaFoldDB; Q2VBP2; -.
DR SMR; Q2VBP2; -.
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 SNTX6"
FT /id="PRO_5000006483"
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 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; 8849 MW; A087621B42A39425 CRC64;
MKTLLLTFLV VTIVCLDLGY TLICHQLHGL QTCEPAQKFC QKRTTMFSPN HPVLLMGCTY
NCPTERYSVC CSTDKCNK
