ID   I166_CONTE              Reviewed;          82 AA.
AC   P0DPM4;
DT   12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Conotoxin Tx6.6 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Olivera B.M., Cartier G.E., Watkins M., Hillyard D.R., McIntosh J.M.,
RA   Layer R.T., Jones R.M.;
RT   "O-superfamily conotoxin peptides.";
RL   Patent number US6762165, 23-JUL-2004.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND AMIDATION AT
RP   ALA-82.
RC   TISSUE=Venom;
RX   PubMed=22709442; DOI=10.1021/pr300312h;
RA   Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA   Yates J.R. III, Bern M.;
RT   "Constrained de novo sequencing of conotoxins.";
RL   J. Proteome Res. 11:4191-4200(2012).
CC   -!- FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and
CC       block voltage-gated calcium channels (Cav). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22709442}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:22709442}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:Q26443}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DPM4; -.
DR   SMR; P0DPM4; -.
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; Disulfide bond;
KW   Ion channel impairing toxin; Secreted; Signal; Toxin;
KW   Voltage-gated calcium channel impairing toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..51
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445065"
FT   PEPTIDE         52..82
FT                   /note="Conotoxin Tx6.6"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000445066"
FT   MOD_RES         82
FT                   /note="Alanine amide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   DISULFID        53..71
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        60..76
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        70..81
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   82 AA;  9301 MW;  E7AA724EBA45E400 CRC64;
     MKLTCVMIVA VLFLTAWTLV MADDSNNGLA NLFSKLRDEM EDPEGSKLEK KDCQEKWDYC
     PVPFLGSRYC CDGFICPSFF CA