3SXZ_OPHHA
ID 3SXZ_OPHHA Reviewed; 78 AA.
AC Q53B52;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Short neurotoxin OH-26 {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], PROTEIN SEQUENCE OF 22-46, TOXIC DOSE, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom, and 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:0000269|PubMed:15302536}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 160 ug/kg by intraperitoneal injection into mice.
CC {ECO:0000269|PubMed:15302536}.
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; AY596934; AAT97256.1; -; mRNA.
DR AlphaFoldDB; Q53B52; -.
DR SMR; Q53B52; -.
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 1: Evidence at protein level;
KW Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15302536"
FT CHAIN 22..78
FT /note="Short neurotoxin OH-26"
FT /evidence="ECO:0000305|PubMed:15302536"
FT /id="PRO_5000093326"
FT SITE 28
FT /note="Important residue for inhibition of muscle alpha-1-
FT beta-1-delta-epsilon and neuronal alpha-3-beta-2/CHRNA3-
FT 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 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 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 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; 8756 MW; 1FDF616466E58123 CRC64;
MKNLLLTFLV VTIVCLDLGY TLICHQRHGL QTCEPAQKFC FAQTVMPFPN HPLTLMGCTY
SCPTEKNAVC CSTDKCNR
