ID   CJA_CONDI               Reviewed;          98 AA.
AC   P0C8W0; E2DEL1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Conotoxin Di19A {ECO:0000305};
DE   AltName: Full=Conotoxin di16a {ECO:0000303|PubMed:18586046};
DE   Flags: Precursor;
OS   Conus distans (Distant cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Fraterconus.
OX   NCBI_TaxID=72281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-98,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-63, HYDROXYLATION AT PRO-53; PRO-68; PRO-93
RP   AND PRO-97, SYNTHESIS OF 50-98, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=18586046; DOI=10.1016/j.toxicon.2008.05.014;
RA   Chen P., Garrett J.E., Watkins M., Olivera B.M.;
RT   "Purification and characterization of a novel excitatory peptide from Conus
RT   distans venom that defines a novel gene superfamily of conotoxins.";
RL   Toxicon 52:139-145(2008).
CC   -!- FUNCTION: Injection of the synthetic peptide causes a hyperexcitable
CC       phenotype in mice greater than three weeks of age at lower doses, and
CC       lethargy at higher doses. {ECO:0000269|PubMed:18586046}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XIX (C-C-C-CCC-C-C-C-C).
CC   -!- PTM: Contains 5 disulfide bonds. {ECO:0000269|PubMed:18586046}.
CC   -!- MASS SPECTROMETRY: Mass=5065.33; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18586046};
CC   -!- MISCELLANEOUS: Has no effect on glutamate (NMDA) receptors,
CC       Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.6/KCNA6, Nav1.2/SCN2A and Nav1.4/SCN4A
CC       channels, and acetylcholine receptors alpha-9/alpha-10.
CC       {ECO:0000305|PubMed:18586046}.
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DR   EMBL; GQ981403; ADN79122.1; -; mRNA.
DR   AlphaFoldDB; P0C8W0; -.
DR   ConoServer; 2842; Di19A precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..49
FT                   /evidence="ECO:0000305|PubMed:18586046"
FT                   /id="PRO_0000366093"
FT   PEPTIDE         50..98
FT                   /note="Conotoxin Di19A"
FT                   /evidence="ECO:0000269|PubMed:18586046"
FT                   /id="PRO_0000366094"
FT   MOD_RES         53
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18586046"
FT   MOD_RES         63
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:18586046"
FT   MOD_RES         68
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18586046"
FT   MOD_RES         93
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18586046"
FT   MOD_RES         97
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18586046"
SQ   SEQUENCE   98 AA;  10379 MW;  FCFD9E2A699011F2 CRC64;
     MSTLGILLPI ALLLPLANPA ENGDGQAMPR TRNLRSLSFG RTLRRLEKRG CDPTDGCQTT
     VCETDTGPCC CKPNFTCQIS NSGTKSCSCS GQPSDCPV