3LKF_BUNFL
ID 3LKF_BUNFL Reviewed; 66 AA.
AC P15815;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Kappa-flavitoxin {ECO:0000303|PubMed:3408728};
DE Short=Kappa-ftx {ECO:0000303|PubMed:8334127};
DE Short=Kappa-fvt;
DE AltName: Full=Long neurotoxin 2;
OS Bungarus flaviceps flaviceps (Red-headed krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8615;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=3408728; DOI=10.1021/bi00410a041;
RA Grant G.A., Frazier M.W., Chiappinelli V.A.;
RT "Amino acid sequence of kappa-flavitoxin: establishment of a new family of
RT snake venom neurotoxins.";
RL Biochemistry 27:3794-3798(1988).
RN [2]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=3828786; DOI=10.1016/0006-8993(87)91043-2;
RA Chiappinelli V.A., Wolf K.M., DeBin J.A., Holt I.L.;
RT "Kappa-flavitoxin: isolation of a new neuronal nicotinic receptor
RT antagonist that is structurally related to kappa-bungarotoxin.";
RL Brain Res. 402:21-29(1987).
RN [3]
RP FUNCTION.
RX PubMed=8334127; DOI=10.1021/bi00078a025;
RA McLane K.E., Weaver W.R., Lei S., Chiappinelli V.A., Conti-Tronconi B.M.;
RT "Homologous kappa-neurotoxins exhibit residue-specific interactions with
RT the alpha 3 subunit of the nicotinic acetylcholine receptor: a comparison
RT of the structural requirements for kappa-bungarotoxin and kappa-flavitoxin
RT binding.";
RL Biochemistry 32:6988-6994(1993).
CC -!- FUNCTION: Postsynaptic neurotoxin that binds and inhibits neuronal
CC nicotinic acetylcholine receptors (nAChR) with high affinity
CC (IC(50)<100 nM). Is a selective, and slowly reversible antagonist of
CC alpha-3/CHRNA3-containing and some alpha-4/CHRNA4-containing AChRs.
CC {ECO:0000269|PubMed:3828786, ECO:0000269|PubMed:8334127}.
CC -!- SUBUNIT: Homo- and heterodimer; non-covalently linked.
CC {ECO:0000250|UniProtKB:P15816}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3408728}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Kappa-neurotoxin sub-subfamily. {ECO:0000305}.
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DR PIR; A28644; A28644.
DR AlphaFoldDB; P15815; -.
DR SMR; P15815; -.
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 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..66
FT /note="Kappa-flavitoxin"
FT /id="PRO_0000093533"
FT DISULFID 3..21
FT /evidence="ECO:0000250|UniProtKB:P01398"
FT DISULFID 14..42
FT /evidence="ECO:0000250|UniProtKB:P01398"
FT DISULFID 27..31
FT /evidence="ECO:0000250|UniProtKB:P01398"
FT DISULFID 46..58
FT /evidence="ECO:0000250|UniProtKB:P01398"
FT DISULFID 59..64
FT /evidence="ECO:0000250|UniProtKB:P01398"
SQ SEQUENCE 66 AA; 7259 MW; 759C74D594C8892B CRC64;
RTCLISPSST SQTCPKGQDI CFTKAFCDRW CSSRGPVIEQ GCAATCPEFT SRYKSLLCCT
TDNCNH
