ID   O19_CONST               Reviewed;          82 AA.
AC   Q5K0D2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Omega-conotoxin-like 9;
DE   Flags: Precursor;
OS   Conus striatus (Striated cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=15652641; DOI=10.1016/j.peptides.2004.10.027;
RA   Kauferstein S., Melaun C., Mebs D.;
RT   "Direct cDNA cloning of novel conopeptide precursors of the O-
RT   superfamily.";
RL   Peptides 26:361-367(2005).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). {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; AJ851176; CAH64849.1; -; mRNA.
DR   AlphaFoldDB; Q5K0D2; -.
DR   ConoServer; 1065; Conotoxin-9 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: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.
DR   PROSITE; PS60004; OMEGA_CONOTOXIN; 1.
PE   2: Evidence at transcript level;
KW   Calcium channel impairing toxin; Cleavage on pair of basic residues;
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..51
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000034944"
FT   PEPTIDE         52..82
FT                   /note="Omega-conotoxin-like 9"
FT                   /id="PRO_0000034945"
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   82 AA;  9235 MW;  023A1F773367FD50 CRC64;
     MKLTCMMIAA VLFLTTWTFV TADDSRYGLK NLFPKARHEM KNPEASKLNK REGCSSGGTF
     CGIHPGLCCS EFCFLWCITF ID