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Conantokin-Br (Con-Br) (Conantoxin-S1) (Con-S1)

 CKBR_CONSL              Reviewed;         103 AA.
P0CG46;
13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 1.
18-JUL-2018, entry version 23.
RecName: Full=Conantokin-Br {ECO:0000303|PubMed:19309162};
Short=Con-Br {ECO:0000303|PubMed:19309162};
Short=ConBr {ECO:0000305};
AltName: Full=Conantoxin-S1 {ECO:0000303|PubMed:17153339};
Short=Con-S1 {ECO:0000303|PubMed:17153339};
Flags: Precursor;
Conus sulcatus (Sulcate cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus; Asprella.
NCBI_TaxID=101760;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 80-103, FUNCTION, MUTAGENESIS
OF 87-PHE-ILE-88; 84-TYR-SER-85 AND TYR-84, SITE, MOLECULAR MODELING,
AND GAMMA-CARBOXYGLUTAMATION AT GLU-82; GLU-83; GLU-89 AND GLU-93.
STRAIN=Conus sulcatus brettingham; TISSUE=Venom duct;
PubMed=19309162; DOI=10.1021/bi802259a;
Twede V.D., Teichert R.W., Walker C.S., Gruszczynski P.,
Kazmierkiewicz R., Bulaj G., Olivera B.M.;
"Conantokin-Br from Conus brettinghami and selectivity determinants
for the NR2D subunit of the NMDA receptor.";
Biochemistry 48:4063-4073(2009).
[2]
NOMENCLATURE.
PubMed=17153339;
Franco A., Pisarewicz K., Moller C., Mora D., Fields G.B., Mari F.;
"Hyperhydroxylation: a new strategy for neuronal targeting by venomous
marine molluscs.";
Prog. Mol. Subcell. Biol. 43:83-103(2006).
-!- FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA)
receptors. This toxin inhibits NR2 subunits N-methyl-D-aspartate
(NMDA) receptor-mediated calcium influx in central nervous system
neurons in the following order of preference: NR2B/GRIN2B
(IC(50)=0.14 uM), NR2D/GRIN2D (IC(50)=0.31 uM), NR2A/GRIN2A
(IC(50)=0.68 uM) and NR2C/GRIN2A (IC(50)=4.9 uM), when tested on
rat receptors. {ECO:0000269|PubMed:19309162}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P58806};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P58806};
Note=Divalent cations stabilize the toxin the in alpha-helix
conformation. {ECO:0000250|UniProtKB:P58806};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
-!- MISCELLANEOUS: The mature peptide does not contain cysteine
residue.
-!- SIMILARITY: Belongs to the conotoxin B superfamily. {ECO:0000305}.
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SMR; P0CG46; -.
PRIDE; P0CG46; -.
ConoServer; 4202; Conantokin-Br precursor.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
1: Evidence at protein level;
Calcium; Gamma-carboxyglutamic acid; Ion channel impairing toxin;
Ionotropic glutamate receptor inhibitor; Magnesium; Metal-binding;
Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 79 {ECO:0000305|PubMed:19309162}.
/FTId=PRO_0000395614.
PEPTIDE 80 103 Conantokin-Br.
{ECO:0000305|PubMed:19309162}.
/FTId=PRO_0000395615.
METAL 89 89 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000250|UniProtKB:P07231}.
METAL 93 93 Divalent metal cation; via 4-
carboxyglutamate.
{ECO:0000250|UniProtKB:P07231}.
SITE 84 84 Significant for the subtype selectivity
between NR2B/GRIN2B and NR2D/GRIN2D
(similar potency for both of them).
{ECO:0000305|PubMed:19309162}.
MOD_RES 82 82 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P07231,
ECO:0000305|PubMed:19309162}.
MOD_RES 83 83 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P07231,
ECO:0000305|PubMed:19309162}.
MOD_RES 89 89 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P07231,
ECO:0000305|PubMed:19309162}.
MOD_RES 93 93 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P07231,
ECO:0000305|PubMed:19309162}.
MUTAGEN 84 85 YS->VA: 37-fold decrease in potency for
NR2B/GRIN2B with a relative increase in
selectivity for this subunit; complete
decrease in potency for NR2D/GRIN2D.
{ECO:0000269|PubMed:19309162}.
MUTAGEN 84 84 Y->V: 23-fold decrease in potency for
NR2B/GRIN2B with a relative increase in
selectivity for this subunit; complete
decrease in potency for NR2D/GRIN2D.
{ECO:0000269|PubMed:19309162}.
MUTAGEN 87 88 FI->MAA: Important decrease in potency
for NR2B/GRIN2B; complete decrease in
potency for NR2D/GRIN2D.
{ECO:0000269|PubMed:19309162}.
SEQUENCE 103 AA; 11708 MW; 76FF2E398C94C894 CRC64;
MQLYTYLYLL VPLVTFHLIL GTGTLDHGGA LTERRSTDAT ALKPEPVLQK SAARSTDDNG
KDRLTQMKRI LKKRGKNARG DEEYSKFIER EREAGRLDLS KFP


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