ID   3NO28_BUNFA             Reviewed;          86 AA.
AC   A2CKF6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Neurotoxin 3FTx-8a;
DE   AltName: Full=3FTx-VIIIa;
DE   Flags: Precursor;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-39, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17166178; DOI=10.1111/j.1742-4658.2006.05598.x;
RA   Tsai I.-H., Tsai H.-Y., Saha A., Gomes A.;
RT   "Sequences, geographic variations and molecular phylogeny of venom
RT   phospholipases and three-finger toxins of eastern India Bungarus fasciatus
RT   and kinetic analyses of its Pro31 phospholipases A2.";
RL   FEBS J. 274:512-525(2007).
CC   -!- FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1-delta-
CC       epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal
CC       (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR).
CC       {ECO:0000250|UniProtKB:O42255}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17166178}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7420; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17166178};
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC       subfamily. Orphan group II sub-subfamily. {ECO:0000305}.
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DR   EMBL; DQ835582; ABI33870.1; -; mRNA.
DR   AlphaFoldDB; A2CKF6; -.
DR   SMR; A2CKF6; -.
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; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:17166178"
FT   CHAIN           22..86
FT                   /note="Neurotoxin 3FTx-8a"
FT                   /evidence="ECO:0000305|PubMed:17166178"
FT                   /id="PRO_0000293102"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        27..32
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        38..63
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        67..78
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
FT   DISULFID        79..84
FT                   /evidence="ECO:0000250|UniProtKB:Q8AY51"
SQ   SEQUENCE   86 AA;  9722 MW;  D7B15B3881D1222C CRC64;
     MKTLLLTLVV VTIVCLDLGY TLTCLICPER YCQKVHTCRG EEKLCVKRFY DEKALGWRAK
     RGCAATCPEA KPKETVECCS TDKCNK