ID   O166_CONST              Reviewed;          72 AA.
AC   P0C831;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 40.
DE   RecName: Full=Omega-conotoxin-like S6.6;
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=16183187; DOI=10.1016/j.biochi.2005.08.001;
RA   Pi C., Liu Y., Peng C., Jiang X., Liu J., Xu B., Yu X., Yu Y., Jiang X.,
RA   Wang L., Dong M., Chen S., Xu A.-L.;
RT   "Analysis of expressed sequence tags from the venom ducts of Conus
RT   striatus: focusing on the expression profile of conotoxins.";
RL   Biochimie 88:131-140(2006).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). This toxin blocks N-,
CC       P- and Q-type calcium channels (By similarity). {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   AlphaFoldDB; P0C831; -.
DR   BMRB; P0C831; -.
DR   SMR; P0C831; -.
DR   ConoServer; 3543; S6.6 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   2: Evidence at transcript level;
KW   Amidation; Calcium channel impairing toxin; 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..45
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000345102"
FT   PEPTIDE         46..71
FT                   /note="Omega-conotoxin-like S6.6"
FT                   /id="PRO_0000345103"
FT   MOD_RES         71
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
FT   DISULFID        53..65
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
FT   DISULFID        60..71
FT                   /evidence="ECO:0000250|UniProtKB:P05484"
SQ   SEQUENCE   72 AA;  7741 MW;  4B4A5E46AFCE08CF CRC64;
     MKLTCVVIVA VLLLTACQLL TADDSRGTQK HRALRSDTKL SMSTRCKGKG APCRKTMYDC
     CSGSCGRRGK CG