ID   O266_CONAA              Reviewed;          80 AA.
AC   A0A3G3C7V6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   23-FEB-2022, entry version 12.
DE   RecName: Full=Gamma-conotoxin-like Am6.6 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus amadis (Amadis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Leptoconus.
OX   NCBI_TaxID=198732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-77, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT PRO-76, AND
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-56; GLU-59 AND GLU-71.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=30593932; DOI=10.1016/j.jprot.2018.12.028;
RA   Vijayasarathy M., Balaram P.;
RT   "Cone snail prolyl-4-hydroxylase alpha-subunit sequences derived from
RT   transcriptomic data and mass spectrometric analysis of variable proline
RT   hydroxylation in C. amadis venom.";
RL   J. Proteomics 194:37-48(2019).
CC   -!- FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation
CC       pacemaker channels (HCN). {ECO:0000250|UniProtKB:P56711}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30593932}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30593932}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin O2 family. {ECO:0000305}.
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DR   EMBL; MH282827; AYP73034.1; -; mRNA.
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   Pfam; PF02950; Conotoxin; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation;
KW   Ion channel impairing toxin; Knottin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..45
FT                   /evidence="ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453603"
FT   PEPTIDE         46..77
FT                   /note="Gamma-conotoxin-like Am6.6"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT                   /id="PRO_5018236541"
FT   PROPEP          78..80
FT                   /evidence="ECO:0000305|PubMed:30593932"
FT                   /id="PRO_0000453604"
FT   MOD_RES         56
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   MOD_RES         59
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   MOD_RES         71
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   MOD_RES         76
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:30593932"
FT   DISULFID        47..61
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        54..65
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        60..70
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
SQ   SEQUENCE   80 AA;  9204 MW;  3DA1AD08A7BC2C76 CRC64;
     MEKLTILLLV AAILMSTQAL NQEQRQQAKI NLLSKKKPSA ERWRRGCTWW FGRCAEDGEC
     CSNSCDQTYC ELYAFPSRAI