O16A_CONBU
ID O16A_CONBU Reviewed; 78 AA.
AC P69749;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Delta-conotoxin BuVIA {ECO:0000305};
DE AltName: Full=Conotoxin Bu7;
DE AltName: Full=Delta-conotoxin-like BVIA;
DE Short=Delta-BVIA;
DE Flags: Precursor;
OS Conus bullatus (Bubble cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Textilia.
OX NCBI_TaxID=89438;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Hillyard D.R., Mcintosh M.J., Jones R.M., Cartier E.G., Watkins M.,
RA Olivera B.M., Layer R.T.;
RT "O-superfamily conotoxin peptides.";
RL Patent number JP2003533178, 11-NOV-2003.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=21266071; DOI=10.1186/1471-2164-12-60;
RA Hu H., Bandyopadhyay P.K., Olivera B.M., Yandell M.;
RT "Characterization of the Conus bullatus genome and its venom-duct
RT transcriptome.";
RL BMC Genomics 12:60-60(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-78.
RC TISSUE=Venom duct;
RX PubMed=11683628; DOI=10.1021/bi010683a;
RA Bulaj G., DeLaCruz R., Azimi-Zonooz A., West P., Watkins M., Yoshikami D.,
RA Olivera B.M.;
RT "Delta-conotoxin structure/function through a cladistic analysis.";
RL Biochemistry 40:13201-13208(2001).
CC -!- FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium
CC channels (Nav) and inhibit the inactivation process. {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; DJ379498; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR AlphaFoldDB; P69749; -.
DR SMR; P69749; -.
DR ConoServer; 1627; BVIA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR InterPro; IPR012322; Conotoxin_d-typ_CS.
DR Pfam; PF02950; Conotoxin; 1.
DR PROSITE; PS60005; DELTA_CONOTOXIN; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW Secreted; Signal; Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /evidence="ECO:0000250"
FT /id="PRO_0000392696"
FT PEPTIDE 52..78
FT /note="Delta-conotoxin BuVIA"
FT /id="PRO_0000044469"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT DISULFID 54..69
FT /evidence="ECO:0000250"
FT DISULFID 61..73
FT /evidence="ECO:0000250"
FT DISULFID 68..77
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="V -> M (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..36
FT /note="NG -> KA (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 78 AA; 8702 MW; 1BF0AA911EBFDA47 CRC64;
MKLTCVMIVT VLFLTAWTFV TADDSTYGLK NLLPNGRHEM MNPEAPKLNK KDECSAPGAF
CLIRPGLCCS EFCFFACF
