ID   3NB_BOIDE               Reviewed;         111 AA.
AC   Q06ZW0; B1NF31;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Denmotoxin {ECO:0000303|PubMed:16864572, ECO:0000303|PubMed:18343233};
DE   Flags: Precursor;
OS   Boiga dendrophila (Mangrove snake) (Gold-ringed cat snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Boiga.
OX   NCBI_TaxID=46286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-81 AND 86-111, FUNCTION,
RP   SUBUNIT, SUBCELLULAR LOCATION, SYNTHESIS OF 35-111, MASS SPECTROMETRY,
RP   PYROGLUTAMATE FORMATION AT GLN-35, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF
RP   37-111, AND DISULFIDE BONDS.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=16864572; DOI=10.1074/jbc.m605850200;
RA   Pawlak J., Mackessy S.P., Fry B.G., Bhatia M., Mourier G.,
RA   Fruchart-Gaillard C., Servent D., Menez R., Stura E., Menez A., Kini R.M.;
RT   "Denmotoxin, a three-finger toxin from the colubrid snake Boiga dendrophila
RT   (Mangrove Catsnake) with bird-specific activity.";
RL   J. Biol. Chem. 281:29030-29041(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=18343233; DOI=10.1016/j.biochi.2008.02.016;
RA   Pawlak J., Kini R.M.;
RT   "Unique gene organization of colubrid three-finger toxins: complete cDNA
RT   and gene sequences of denmotoxin, a bird-specific toxin from colubrid snake
RT   Boiga dendrophila (Mangrove Catsnake).";
RL   Biochimie 90:868-877(2008).
CC   -!- FUNCTION: This bird-specific postsynaptic neurotoxin irreversibly binds
CC       and inhibits the chick muscle alpha-1-beta-1-gamma-delta (CHRNA1-
CC       CHRNB1-CHRNG-CHNRD) nicotinic acetylcholine receptor (nAChR) 100-fold
CC       more compared with the mouse receptor. The weak binding to mouse
CC       receptor is reversible. {ECO:0000269|PubMed:16864572}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16864572}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16864572}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:16864572}.
CC   -!- MASS SPECTROMETRY: Mass=8507.92; Mass_error=0.30; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16864572};
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral
CC       subfamily. Boigatoxin sub-subfamily. {ECO:0000305}.
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DR   EMBL; DQ366293; ABC95749.1; -; mRNA.
DR   EMBL; EF452300; ABR14059.1; -; Genomic_DNA.
DR   PDB; 2H5F; X-ray; 1.90 A; A/B=35-111.
DR   PDBsum; 2H5F; -.
DR   AlphaFoldDB; Q06ZW0; -.
DR   SMR; Q06ZW0; -.
DR   EvolutionaryTrace; Q06ZW0; -.
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   3D-structure; Acetylcholine receptor inhibiting toxin;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Postsynaptic neurotoxin; Pyrrolidone carboxylic acid; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..34
FT                   /evidence="ECO:0000269|PubMed:16864572"
FT                   /id="PRO_0000313786"
FT   CHAIN           35..111
FT                   /note="Denmotoxin"
FT                   /evidence="ECO:0000305|PubMed:16864572"
FT                   /id="PRO_5000141247"
FT   MOD_RES         35
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:16864572"
FT   DISULFID        44..68
FT                   /evidence="ECO:0000269|PubMed:16864572,
FT                   ECO:0000312|PDB:2H5F"
FT   DISULFID        47..55
FT                   /evidence="ECO:0000269|PubMed:16864572,
FT                   ECO:0000312|PDB:2H5F"
FT   DISULFID        61..87
FT                   /evidence="ECO:0000269|PubMed:16864572,
FT                   ECO:0000312|PDB:2H5F"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000269|PubMed:16864572,
FT                   ECO:0000312|PDB:2H5F"
FT   DISULFID        103..108
FT                   /evidence="ECO:0000269|PubMed:16864572,
FT                   ECO:0000312|PDB:2H5F"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          59..63
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          81..90
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:2H5F"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:2H5F"
SQ   SEQUENCE   111 AA;  12076 MW;  5F0EE0C09187B0D7 CRC64;
     MKTLLLAVAV VAFVCLGSAD QLGLGRQQID WGQGQAVGLP HGFCIQCNRK TWSNCSIGHR
     CLPYHMTCYT LYKPDENGEM KWAVKGCARM CPTAKSGERV KCCTGASCNS D