ID   3SE1_DENAN              Reviewed;          61 AA.
AC   P0C1Y9; P01403;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Fasciculin-1 {ECO:0000303|PubMed:2254925, ECO:0000303|PubMed:6530667};
DE            Short=Fas-1;
DE            Short=Fas1;
DE   AltName: Full=Fasciculin-I;
DE            Short=FAS-I;
DE   AltName: Full=Toxin TA1;
OS   Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8618;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=6530667;
RA   Karlsson E., Mbugua P.M., Rodriguez-Ithurralde D.;
RT   "Fasciculins, anticholinesterase toxins from the venom of the green mamba
RT   Dendroaspis angusticeps.";
RL   J. Physiol. (Paris) 79:232-240(1984).
RN   [2]
RP   CRYSTALLIZATION.
RX   PubMed=2254925; DOI=10.1016/s0022-2836(05)80313-4;
RA   Menez R., Ducruix A.;
RT   "Preliminary X-ray analysis of crystals of fasciculin 1, a potent
RT   acetylcholinesterase inhibitor from green mamba venom.";
RL   J. Mol. Biol. 216:233-234(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=1429564; DOI=10.2210/pdb1fas/pdb;
RA   Le Du M.-H., Marchot P., Bougis P.E., Fontecilla-Camps J.-C.;
RT   "1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase
RT   toxin from green mamba snake venom.";
RL   J. Biol. Chem. 267:22122-22130(1992).
CC   -!- FUNCTION: Interferes with neuromuscular transmission by inhibiting the
CC       enzyme acetylcholinesterase (AChE) present at the neuromuscular
CC       junction. It selectively binds and inhibits with a 1:1 stoichiometry
CC       the mammalian and electric fish AChE at picomolar concentrations. It is
CC       highly specific for the peripheral site of AChE and blocks the entry of
CC       acetylcholine into the active site of the enzyme, thereby preventing
CC       its breakdown. It has been called fasciculin since after injection into
CC       mice it causes severe, generalized and long-lasting (5-7 hours)
CC       fasciculations. {ECO:0000269|PubMed:6530667}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6530667}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Acn-esterase inhibitor sub-subfamily. {ECO:0000305}.
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DR   PIR; A01674; T4EP1A.
DR   PDB; 1FAS; X-ray; 1.80 A; A=1-61.
DR   PDBsum; 1FAS; -.
DR   AlphaFoldDB; P0C1Y9; -.
DR   SMR; P0C1Y9; -.
DR   MINT; P0C1Y9; -.
DR   PRIDE; P0C1Y9; -.
DR   EvolutionaryTrace; P0C1Y9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR018354; Snake_toxin_con_site.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   CHAIN           1..61
FT                   /note="Fasciculin-1"
FT                   /evidence="ECO:0000269|PubMed:6530667"
FT                   /id="PRO_0000093653"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000269|PubMed:1429564,
FT                   ECO:0000312|PDB:1FAS"
FT   DISULFID        17..39
FT                   /evidence="ECO:0000269|PubMed:1429564,
FT                   ECO:0000312|PDB:1FAS"
FT   DISULFID        41..52
FT                   /evidence="ECO:0000269|PubMed:1429564,
FT                   ECO:0000312|PDB:1FAS"
FT   DISULFID        53..59
FT                   /evidence="ECO:0000269|PubMed:1429564,
FT                   ECO:0000312|PDB:1FAS"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   STRAND          22..31
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   STRAND          34..40
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:1FAS"
FT   TURN            57..60
FT                   /evidence="ECO:0007829|PDB:1FAS"
SQ   SEQUENCE   61 AA;  6807 MW;  50A38EF3633C2AB4 CRC64;
     TMCYSHTTTS RAILTNCGEN SCYRKSRRHP PKMVLGRGCG CPPGDDYLEV KCCTSPDKCN
     Y