ID   O16B_CONPE              Reviewed;          82 AA.
AC   P56713; Q9BP48; Q9U661;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Omega-conotoxin PnVIB;
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 53-82, 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=3178.2; Mass_error=0.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8863526};
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; AF193255; AAF07966.1; -; mRNA.
DR   EMBL; AF215109; AAG60530.1; -; mRNA.
DR   AlphaFoldDB; P56713; -.
DR   SMR; P56713; -.
DR   ConoServer; 787; PnMKLT1-01112 (partial).
DR   ConoServer; 1741; PnVIB.
DR   ConoServer; 1088; PnVIB 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   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Presynaptic neurotoxin;
KW   Secreted; Signal; Toxin; Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..52
FT                   /evidence="ECO:0000269|PubMed:8863526"
FT                   /id="PRO_0000392705"
FT   PEPTIDE         53..82
FT                   /note="Omega-conotoxin PnVIB"
FT                   /id="PRO_0000044477"
FT   DISULFID        56..73
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        63..77
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        72..81
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   82 AA;  9081 MW;  543999326317191F CRC64;
     MKLTCMMIVA VLFLTAWTVV TAEPHSSNVL ENLYLKAHHE MENPEASKLN TRDDDCEPPG
     NFCGMIKIGP PCCSGWCFFA CA