ID   CKP1_CONPI              Reviewed;          19 AA.
AC   P0C8E0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Conantokin-Pr1 {ECO:0000303|PubMed:17962189};
DE            Short=Con-Pr1 {ECO:0000303|PubMed:17962189};
OS   Conus parius (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX   NCBI_TaxID=505247;
RN   [1]
RP   PROTEIN SEQUENCE, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-4; GLU-7 AND GLU-11, MASS SPECTROMETRY, AND
RP   COFACTOR.
RC   TISSUE=Venom;
RX   PubMed=17962189; DOI=10.1074/jbc.m706611200;
RA   Teichert R.W., Jimenez E.C., Twede V., Watkins M., Hollmann M., Bulaj G.,
RA   Olivera B.M.;
RT   "Novel conantokins from Conus parius venom are specific antagonists of N-
RT   methyl-D-aspartate receptors.";
RL   J. Biol. Chem. 282:36905-36913(2007).
CC   -!- FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors.
CC       This toxin has highest potency for the NR2B/GRIN2B subunit. It induces
CC       sleep in 10-day-old mice when injected intracranially, and
CC       hyperactivity in 24-day-old mice. {ECO:0000269|PubMed:17962189}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:17962189};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:17962189};
CC       Note=Adopts alpha-helical conformations in the presence of divalent
CC       cations and is unstructured in the absence of divalent cations.
CC       {ECO:0000269|PubMed:17962189};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17962189}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:17962189}.
CC   -!- MASS SPECTROMETRY: Mass=2352.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17962189};
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C8E0; -.
DR   ConoServer; 3537; Conantokin-Pr1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   DisProt; DP02320; -.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Gamma-carboxyglutamic acid;
KW   Ion channel impairing toxin; Ionotropic glutamate receptor inhibitor;
KW   Magnesium; Metal-binding; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..19
FT                   /note="Conantokin-Pr1"
FT                   /evidence="ECO:0000269|PubMed:17962189"
FT                   /id="PRO_0000353127"
FT   BINDING         7
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /note="via 4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231"
FT   BINDING         11
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /note="via 4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231"
FT   MOD_RES         4
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:17962189"
FT   MOD_RES         7
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:17962189"
FT   MOD_RES         11
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:17962189"
SQ   SEQUENCE   19 AA;  2220 MW;  737421677E167DE3 CRC64;
     GEDEYAEGIR EYQLIHGKI