ID   O16A_CONPE              Reviewed;          78 AA.
AC   P56712; Q9U658;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Omega-conotoxin PnVIA;
DE   Flags: Precursor;
OS   Conus pennaceus (Feathered cone) (Conus episcopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX   NCBI_TaxID=37335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 46-76, AMIDATION AT GLN-76, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=8863526; DOI=10.1046/j.1471-4159.1996.67052155.x;
RA   Kits K.S., Lodder J.C., van der Schors R.C., Li K.W., Geraerts W.P.M.,
RA   Fainzilber M.;
RT   "Novel omega-conotoxins block dihydropyridine-insensitive high voltage-
RT   activated calcium channels in molluscan neurons.";
RL   J. Neurochem. 67:2155-2163(1996).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). Acts on high voltage-
CC       activated (HVA) calcium currents in molluscan neurons.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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   -!- MASS SPECTROMETRY: Mass=3267.7; Mass_error=0.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8863526};
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; AF193258; AAF07969.1; -; mRNA.
DR   AlphaFoldDB; P56712; -.
DR   SMR; P56712; -.
DR   ConoServer; 1742; PnVIA.
DR   ConoServer; 1091; PnVIA precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
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   InterPro; IPR012321; Conotoxin_omega-typ_CS.
DR   Pfam; PF02950; Conotoxin; 1.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium channel impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Knottin; Neurotoxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000269|PubMed:8863526"
FT                   /id="PRO_0000392704"
FT   PEPTIDE         46..76
FT                   /note="Omega-conotoxin PnVIA"
FT                   /id="PRO_0000044876"
FT   MOD_RES         76
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:8863526"
FT   DISULFID        47..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   78 AA;  8615 MW;  90411ACEBB7FE3F8 CRC64;
     MKLTCMMIIA VLFLTAWTFV MADDPRDEPE ARDEMNPAAS KLNERGCLEV DYFCGIPFAN
     NGLCCSGNCV FVCTPQGK