ID   U7B_CONDE               Reviewed;          28 AA.
AC   P0CH13;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Conotoxin de7b;
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, MASS SPECTROMETRY, HYDROXYLATION AT PRO-4,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-7, AND HYDROXYLATION AT PRO-14.
RC   TISSUE=Venom;
RX   PubMed=19118590; DOI=10.1016/j.peptides.2008.12.005;
RA   Aguilar M.B., Flores-Torres A., Batista C.V.F., Falcon A., Lopez-Vera E.,
RA   de la Cotera E.P.H.;
RT   "Structural characterization of five post-translationally modified
RT   isomorphs of a novel putative delta-conotoxin from the vermivorous snail
RT   Conus delessertii from the Mexican Caribbean Sea.";
RL   Peptides 30:458-466(2009).
CC   -!- FUNCTION: May inhibit sodium (Nav) or calcium channels (Cav).
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=3078.0; Method=Electrospray; Note=without
CC       PTMs.; Evidence={ECO:0000269|PubMed:19118590};
CC   -!- MASS SPECTROMETRY: Mass=3095.0; Method=Electrospray; Note=hydroxylated
CC       at 'Pro-14'.; Evidence={ECO:0000269|PubMed:19118590};
CC   -!- MASS SPECTROMETRY: Mass=3111.0; Method=Electrospray; Note=hydroxylated
CC       at 'Pro-4' and 'Pro-14'.; Evidence={ECO:0000269|PubMed:19118590};
CC   -!- MASS SPECTROMETRY: Mass=3139.0; Method=Electrospray; Note=carboxylated
CC       at 'Glu-7' and hydroxylated at 'Pro-14'.;
CC       Evidence={ECO:0000269|PubMed:19118590};
CC   -!- MASS SPECTROMETRY: Mass=3155.0; Method=Electrospray; Note=carboxylated
CC       at 'Glu-7' and hydroxylated at 'Pro-4' and 'Pro-14'.;
CC       Evidence={ECO:0000269|PubMed:19118590};
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DR   AlphaFoldDB; P0CH13; -.
DR   SMR; P0CH13; -.
DR   ConoServer; 3629; De7b.
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:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Calcium channel impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Ion channel impairing toxin;
KW   Knottin; Neurotoxin; Secreted; Toxin;
KW   Voltage-gated calcium channel impairing toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..28
FT                   /note="Conotoxin de7b"
FT                   /id="PRO_0000396801"
FT   MOD_RES         4
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:19118590"
FT   MOD_RES         7
FT                   /note="4-carboxyglutamate; partial"
FT                   /evidence="ECO:0000269|PubMed:19118590"
FT   MOD_RES         14
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:19118590"
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;  3085 MW;  2EF458B2D5CCDFE3 CRC64;
     DCIPGGENCD VFRPYRCCSG YCILLLCA