ID   O17A_CONDE              Reviewed;          28 AA.
AC   P0C1C9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Gamma-conotoxin-like de7a;
OS   Conus delessertii (Sozon's cone) (Conus sozoni).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conasprella; Kohniconus.
OX   NCBI_TaxID=2547900;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-4, GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-13 AND GLU-16, AMIDATION AT SER-28, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15626501; DOI=10.1016/j.peptides.2004.10.012;
RA   Aguilar M.B., Lopez-Vera E., Imperial J.S., Falcon A., Olivera B.M.,
RA   de la Cotera E.P.;
RT   "Putative gamma-conotoxins in vermivorous cone snails: the case of Conus
RT   delessertii.";
RL   Peptides 26:23-27(2005).
CC   -!- FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation
CC       pacemaker channels (HCN). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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   -!- MASS SPECTROMETRY: Mass=3170; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15626501};
CC   -!- MASS SPECTROMETRY: Mass=3090.2; Method=MALDI; Note=Decarboxylated.;
CC       Evidence={ECO:0000269|PubMed:15626501};
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1C9; -.
DR   SMR; P0C1C9; -.
DR   ConoServer; 1496; DeVIIA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..28
FT                   /note="Gamma-conotoxin-like de7a"
FT                   /id="PRO_0000234828"
FT   MOD_RES         4
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:15626501"
FT   MOD_RES         13
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15626501"
FT   MOD_RES         16
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:15626501"
FT   MOD_RES         28
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:15626501"
FT   DISULFID        2..18
FT                   /evidence="ECO:0000250"
FT   DISULFID        9..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..27
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   28 AA;  3073 MW;  551DE1CF53C194D3 CRC64;
     ACKPKNNLCA ITEMAECCSG FCLIYRCS