3SX2_MICFR
ID 3SX2_MICFR Reviewed; 59 AA.
AC P86421;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Frontoxin II {ECO:0000303|PubMed:20331995};
DE Short=FTx II {ECO:0000303|PubMed:20331995};
DE AltName: Full=Three-finger toxin;
DE Short=3FTx;
OS Micrurus frontalis (Coral snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=129461;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20331995; DOI=10.1016/j.toxicon.2010.02.030;
RA Moreira K.G., Prates M.V., Andrade F.A., Silva L.P., Beirao P.S.,
RA Kushmerick C., Naves L.A., Bloch C. Jr.;
RT "Frontoxins, three-finger toxins from Micrurus frontalis venom, decrease
RT miniature endplate potential amplitude at frog neuromuscular junction.";
RL Toxicon 56:55-63(2010).
CC -!- FUNCTION: Neurotoxin. Blocks muscular nicotinic acetylcholine receptors
CC (nAChR). {ECO:0000305|PubMed:20331995}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20331995}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20331995}.
CC -!- MASS SPECTROMETRY: Mass=6548.91; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20331995};
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86421; -.
DR SMR; P86421; -.
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; Toxin.
FT CHAIN 1..59
FT /note="Frontoxin II"
FT /evidence="ECO:0000269|PubMed:20331995"
FT /id="PRO_0000394460"
FT DISULFID 3..20
FT /evidence="ECO:0000250|UniProtKB:P07526"
FT DISULFID 14..39
FT /evidence="ECO:0000250|UniProtKB:P07526"
FT DISULFID 43..51
FT /evidence="ECO:0000250|UniProtKB:P07526"
FT DISULFID 52..57
FT /evidence="ECO:0000250|UniProtKB:P07526"
SQ SEQUENCE 59 AA; 6560 MW; 2FC83B55167FBEFF CRC64;
LICYVSKDGE TATCPPGQKC EKYAVSASHT GHWFYMYDCT STCHIGPYNV CCSTDLCNR