CKP2_CONPI
ID CKP2_CONPI Reviewed; 19 AA.
AC P0C8E1;
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-Pr2 {ECO:0000303|PubMed:17962189};
DE Short=Con-Pr2 {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 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, SYNTHESIS, FUNCTION,
RP SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-3, GAMMA-CARBOXYGLUTAMATION AT
RP GLU-4; GLU-7 AND GLU-11, MASS SPECTROMETRY, AND COFACTOR.
RC TISSUE=Venom, and Venom duct;
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 the highest potency for the NR2B/GRIN2B subunit and a
CC smaller potency for the NR2D/GRIN2D subunits. It induces sleep in 10-
CC day-old mice when injected intracranially, and hyperactivity in 24-day-
CC 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=2462.8; 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; P0C8E1; -.
DR ConoServer; 3536; Conantokin-Pr2.
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; DP02321; -.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Gamma-carboxyglutamic acid;
KW Hydroxylation; Ion channel impairing toxin;
KW Ionotropic glutamate receptor inhibitor; Magnesium; Metal-binding;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Toxin.
FT PEPTIDE 1..19
FT /note="Conantokin-Pr2"
FT /evidence="ECO:0000269|PubMed:17962189"
FT /id="PRO_0000353128"
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 3
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:17962189"
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; 2316 MW; 69AEE317C3767DE3 CRC64;
DEPEYAEAIR EYQLKYGKI
