ID   CKP_CONPU               Reviewed;         104 AA.
AC   P0C8E3;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Conantokin-P {ECO:0000303|PubMed:18586049};
DE            Short=Con-P {ECO:0000303|PubMed:18586049};
DE   Flags: Precursor;
OS   Conus purpurascens (Purple cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX   NCBI_TaxID=41690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 81-104, FUNCTION, DISULFIDE BOND,
RP   AND GAMMA-CARBOXYGLUTAMATION AT GLU-83; GLU-84; GLU-90; GLU-94 AND GLU-103.
RC   TISSUE=Venom duct;
RX   PubMed=18586049; DOI=10.1016/j.toxicon.2008.04.178;
RA   Gowd K.H., Twede V., Watkins M., Krishnan K.S., Teichert R.W., Bulaj G.,
RA   Olivera B.M.;
RT   "Conantokin-P, an unusual conantokin with a long disulfide loop.";
RL   Toxicon 52:203-213(2008).
CC   -!- FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors.
CC       This toxin has the highest potency for the NR2B/GRIN2B subunit,
CC       followed by NR2A/GRIN2A, NR2C/GRIN2C, and NR2D/GRIN2D subunits.
CC       {ECO:0000269|PubMed:18586049}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18586049}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:18586049}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Adopts an alpha-helical conformation in presence and in
CC       absence of divalent cations. Calcium facilitates disulfide bond
CC       formation of the synthetic peptide. {ECO:0000269|PubMed:18586049}.
CC   -!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C8E3; -.
DR   SMR; P0C8E3; -.
DR   ConoServer; 3531; Conantokin-P precursor.
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   InterPro; IPR005918; Conantokin_CS.
DR   Pfam; PF10550; Toxin_36; 1.
DR   PROSITE; PS60025; CONANTOKIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Gamma-carboxyglutamic acid;
KW   Ion channel impairing toxin; Ionotropic glutamate receptor inhibitor;
KW   Magnesium; Metal-binding; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Signal; Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..80
FT                   /evidence="ECO:0000305|PubMed:18586049"
FT                   /id="PRO_0000353130"
FT   PEPTIDE         81..104
FT                   /note="Conantokin-P"
FT                   /evidence="ECO:0000305|PubMed:18586049"
FT                   /id="PRO_0000353131"
FT   REGION          29..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90
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         94
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         83
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:18586049"
FT   MOD_RES         84
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:18586049"
FT   MOD_RES         90
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:18586049"
FT   MOD_RES         94
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:18586049"
FT   MOD_RES         103
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000305|PubMed:18586049"
FT   DISULFID        91..104
FT                   /evidence="ECO:0000305|PubMed:18586049"
SQ   SEQUENCE   104 AA;  12033 MW;  C6364066BBC1D04B CRC64;
     MQLYTYLYLL VPLVTFHLIL STGTLAHGGT LTERRSTDTT ALKPEPVLLQ KSDARSTDDN
     DKDRLTQMKR ILKKRGNKAR GEEEHSKYQE CLREIRVNKV QQEC