O16A_CONCN
ID O16A_CONCN Reviewed; 82 AA.
AC P69750;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Delta-conotoxin-like CnVIA;
DE Short=Delta-CnVIA;
DE Flags: Precursor;
OS Conus consors (Singed cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX NCBI_TaxID=101297;
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] OF 52-82.
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).
RN [3]
RP MISCELLANEOUS.
RX PubMed=19457347; DOI=10.1016/j.jprot.2009.01.019;
RA Biass D., Dutertre S., Gerbault A., Menou J.L., Offord R., Favreau P.,
RA Stocklin R.;
RT "Comparative proteomic study of the venom of the piscivorous cone snail
RT Conus consors.";
RL J. Proteomics 72:210-218(2009).
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 -!- MISCELLANEOUS: Found in the dissected venom (DV), but not in the
CC injectable (milked) venom (IV).
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; DJ379501; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR AlphaFoldDB; P69750; -.
DR ConoServer; 1626; CnVIA.
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 InterPro; IPR012321; Conotoxin_omega-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;
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_0000392697"
FT PEPTIDE 52..82
FT /note="Delta-conotoxin-like CnVIA"
FT /id="PRO_0000044867"
FT DISULFID 54..69
FT /evidence="ECO:0000250"
FT DISULFID 61..73
FT /evidence="ECO:0000250"
FT DISULFID 68..78
FT /evidence="ECO:0000250"
SQ SEQUENCE 82 AA; 9132 MW; FAC32C4093364D6E CRC64;
MKLTCMMIVA VLFLTAWTFV TADDSRNGLE NLSPKARHEM KNPEASKSNK RYECYSTGTF
CGINGGLCCS NLCLFFVCLT FS