ID   O165_CONBE              Reviewed;          80 AA.
AC   Q3YEG7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Conotoxin Bt6.5 {ECO:0000305};
DE   AltName: Full=Conotoxin BeB42 {ECO:0000303|PubMed:17177885};
DE   Flags: Precursor;
OS   Conus betulinus (Beech cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX   NCBI_TaxID=89764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=17177885; DOI=10.1111/j.1747-0285.2006.00443.x;
RA   Zhangsun D., Luo S., Wu Y., Zhu X., Hu Y., Xie L.;
RT   "Novel O-superfamily conotoxins identified by cDNA cloning from three
RT   vermivorous Conus species.";
RL   Chem. Biol. Drug Des. 68:256-265(2006).
CC   -!- FUNCTION: When injected intracranially in mice, induces a series of
CC       symptoms such as quivering, climbing, scratching, barrel rolling and
CC       paralysis of limbs. Unexpectedly, no effect is observed on ionic
CC       currents when tested on locust DUM neuron (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; DQ141146; AAZ83782.1; -; mRNA.
DR   AlphaFoldDB; Q3YEG7; -.
DR   SMR; Q3YEG7; -.
DR   ConoServer; 1134; BeB42 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Knottin; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000315478"
FT   PEPTIDE         48..80
FT                   /note="Conotoxin Bt6.5"
FT                   /id="PRO_0000315479"
FT   DISULFID        48..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   80 AA;  9053 MW;  2F8308B08DE50C5F CRC64;
     MKLTCVLIIA VLFLTACQLA TAKTYSTGRQ KHRALRSTDK NIKLSRRCND PGGSCTRHYH
     CCQLYCNKQE SVCLENEPAF