ID   CKR1A_CONRO             Reviewed;         103 AA.
AC   P0DKY9;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Conantokin R1-A {ECO:0000303|PubMed:20572027};
DE            Short=Con R1-A {ECO:0000305};
DE            Short=ConRl-A {ECO:0000303|PubMed:20572027};
DE   Flags: Precursor;
OS   Conus rolani (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Asprella.
OX   NCBI_TaxID=745791;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SYNTHESIS OF 80-103, FUNCTION, CIRCULAR
RP   DICHROISM ANALYSIS, AND GAMMA-CARBOXYGLUTAMATION AT GLU-82; GLU-83 AND
RP   GLU-89.
RX   PubMed=20572027; DOI=10.1002/psc.1249;
RA   Gowd K.H., Watkins M., Twede V.D., Bulaj G.W., Olivera B.M.;
RT   "Characterization of conantokin Rl-A: molecular phylogeny as
RT   structure/function study.";
RL   J. Pept. Sci. 16:375-382(2010).
CC   -!- FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors.
CC       This toxin has the highest potency for the NR2B/GRIN2B subunit
CC       (IC(50)=0.11 uM), followed by NR2D/GRIN2D (IC(50)=0.48 uM), NR2A/GRIN2A
CC       (IC(50)=2.1 uM), and NR2C/GRIN2C (IC(50)=6.1 uM) subunits when tested
CC       on rat receptors. {ECO:0000269|PubMed:20572027}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P58806};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P58806};
CC       Note=Divalent cations stabilize the toxin the in alpha-helix
CC       conformation. {ECO:0000250|UniProtKB:P58806};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:20572027}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:20572027}.
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residue.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: The synthetic peptide exists as two interconvertible
CC       conformers. {ECO:0000305|PubMed:20572027}.
CC   -!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0DKY9; -.
DR   SMR; P0DKY9; -.
DR   ConoServer; 5842; conantokin-Rl1.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Gamma-carboxyglutamic acid; Ion channel impairing toxin;
KW   Ionotropic glutamate receptor inhibitor; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..79
FT                   /evidence="ECO:0000305|PubMed:20572027"
FT                   /id="PRO_0000421892"
FT   PEPTIDE         80..103
FT                   /note="Conantokin R1-A"
FT                   /evidence="ECO:0000305|PubMed:20572027"
FT                   /id="PRO_0000421893"
FT   REGION          34..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         82
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:20572027"
FT   MOD_RES         83
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07231,
FT                   ECO:0000305|PubMed:20572027"
FT   MOD_RES         89
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000305|PubMed:20572027"
SQ   SEQUENCE   103 AA;  11759 MW;  FB9D74E31DD74387 CRC64;
     MQLYTYLYLL VPLVTFHLIL GTGTLDHGGA LTERRSTDAT ALKPEPVLQK SAARSTDDNG
     KDRLTQMKRI LKKRGNNPRA DEEYLKFIEE QRKQGKLDPT KFP