ID   M7J_CONCN               Reviewed;          77 AA.
AC   P0DKQ6; S6CQU2;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Omega-conotoxin-like CnVIIJ {ECO:0000303|PubMed:22705119};
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 [MRNA], MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=22705119; DOI=10.1016/j.jprot.2012.06.001;
RA   Violette A., Biass D., Dutertre S., Koua D., Piquemal D., Pierrat F.,
RA   Stocklin R., Favreau P.;
RT   "Large-scale discovery of conopeptides and conoproteins in the injectable
RT   venom of a fish-hunting cone snail using a combined proteomic and
RT   transcriptomic approach.";
RL   J. Proteomics 75:5215-5225(2012).
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:0000269|PubMed:22705119}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P05484}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- MASS SPECTROMETRY: Mass=3851.49; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:22705119};
CC   -!- MISCELLANEOUS: Found in injectable (milked) (IV) venom.
CC       {ECO:0000305|PubMed:22705119}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; HE856387; CCI55500.1; -; mRNA.
DR   AlphaFoldDB; P0DKQ6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Disulfide bond; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /evidence="ECO:0000305|PubMed:22705119"
FT                   /id="PRO_0000451776"
FT   PEPTIDE         43..77
FT                   /note="Omega-conotoxin-like CnVIIJ"
FT                   /evidence="ECO:0000269|PubMed:22705119"
FT                   /id="PRO_0000419889"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
FT   DISULFID        53..64
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
FT   DISULFID        60..71
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
SQ   SEQUENCE   77 AA;  8429 MW;  E0ED4BFF677E6852 CRC64;
     MKLTCVVIVA VLLLTACQLI TADDSRGTQK HRSLRSTTKV SKSTSCMKAG SYCRSTTRTC
     CGYCAYFGKF CIDFPSN