ID   O16A_CONMA              Reviewed;          84 AA.
AC   P69753;
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-like MVIA;
DE            Short=Delta-MVIA;
DE   Flags: Precursor;
OS   Conus magus (Magical cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6492;
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=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; DJ379434; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   AlphaFoldDB; P69753; -.
DR   SMR; P69753; -.
DR   ConoServer; 1624; MVIA.
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   Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW   Hydroxylation; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   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_0000392700"
FT   PEPTIDE         52..83
FT                   /note="Delta-conotoxin-like MVIA"
FT                   /id="PRO_0000044869"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="Serine amide"
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"
SQ   SEQUENCE   84 AA;  9483 MW;  DC18D89D6A9B31FE CRC64;
     MKLTCVMIVA VLFLTTWTFV TADDSRYGLK NLFPKARHEM KNPEASKLNK RDGCYNAGTF
     CGIRPGLCCS EFCFLWCITF VDSG