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Alpha-conotoxin BuIA (Conotoxin Bu1.3)

 CA1A_CONBU              Reviewed;          60 AA.
P69657;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 1.
22-NOV-2017, entry version 50.
RecName: Full=Alpha-conotoxin BuIA {ECO:0000303|PubMed:15520009, ECO:0000303|PubMed:16979596, ECO:0000303|PubMed:17445276};
AltName: Full=Conotoxin Bu1.3 {ECO:0000303|PubMed:20143226};
Flags: Precursor;
Conus bullatus (Bubble cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=89438;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 44-56, AMIDATION AT CYS-56,
AND FUNCTION.
TISSUE=Venom duct;
PubMed=15520009; DOI=10.1074/jbc.M406281200;
Azam L., Dowell C., Watkins M., Stitzel J.A., Olivera B.M.,
McIntosh J.M.;
"Alpha-conotoxin BuIA, a novel peptide from Conus bullatus,
distinguishes among neuronal nicotinic acetylcholine receptors.";
J. Biol. Chem. 280:80-87(2005).
[2]
FUNCTION, AMIDATION AT CYS-56, AND SYNTHESIS OF 44-56.
PubMed=16964981; DOI=10.1021/bi0611715;
Shiembob D.L., Roberts R.L., Luetje C.W., McIntosh J.M.;
"Determinants of alpha-conotoxin BuIA selectivity on the nicotinic
acetylcholine receptor beta subunit.";
Biochemistry 45:11200-11207(2006).
[3]
MUTAGENESIS OF SER-47; THR-48; ALA-52; VAL-53; LEU-54 AND TYR-55,
SYNTHETIC HYDROXYPRO-49 AND HYDROXYPRO-50, AMIDATION AT CYS-56, AND
SYNTHESIS OF 44-56.
PubMed=20739611; DOI=10.1096/fj.10-166272;
Azam L., Maskos U., Changeux J.P., Dowell C.D., Christensen S.,
De Biasi M., McIntosh J.M.;
"Alpha-conotoxin BuIA[T5A;P6O]: a novel ligand that discriminates
between alpha6beta4 and alpha6beta2 nicotinic acetylcholine receptors
and blocks nicotine-stimulated norepinephrine release.";
FASEB J. 24:5113-5123(2010).
[4]
FUNCTION.
PubMed=22751014; DOI=10.1096/fj.12-204487;
Kim H.W., McIntosh J.M.;
"alpha6 nAChR subunit residues that confer alpha-conotoxin BuIA
selectivity.";
FASEB J. 26:4102-4110(2012).
[5]
MUTAGENESIS OF THR-48, SYNTHETIC HYDROXYPRO-49, AND SYNTHESIS OF
22-37.
PubMed=26330550; DOI=10.1124/mol.115.100982;
Hone A.J., McIntosh J.M., Azam L., Lindstrom J., Lucero L.,
Whiteaker P., Passas J., Blazquez J., Albillos A.;
"Alpha-conotoxins identify the alpha3beta4* subtype as the predominant
nicotinic acetylcholine receptor expressed in human adrenal chromaffin
cells.";
Mol. Pharmacol. 88:881-893(2015).
[6]
ERRATUM.
PubMed=26783122; DOI=10.1124/mol.115.100982err;
Hone A.J., McIntosh J.M., Azam L., Lindstrom J., Lucero L.,
Whiteaker P., Passas J., Blazquez J., Albillos A.;
"Correction to 'alpha-conotoxins identify the alpha3beta4* subtype as
the predominant nicotinic acetylcholine receptor expressed in human
adrenal chromaffin cells'.";
Mol. Pharmacol. 89:322-322(2016).
[7]
STRUCTURE BY NMR OF 44-56, SYNTHESIS OF 44-56, AMIDATION AT CYS-56,
AND DISULFIDE BONDS.
PubMed=16979596; DOI=10.1016/j.bbrc.2006.08.164;
Chi S.-W., Kim D.-H., Olivera B.M., McIntosh J.M., Han K.-H.;
"NMR structure determination of alpha-conotoxin BuIA, a novel neuronal
nicotinic acetylcholine receptor antagonist with an unusual 4/4
disulfide scaffold.";
Biochem. Biophys. Res. Commun. 349:1228-1234(2006).
[8]
STRUCTURE BY NMR OF 44-56, SYNTHESIS OF 44-56, AMIDATION AT CYS-56,
AND DISULFIDE BONDS.
PubMed=17445276; DOI=10.1186/1472-6807-7-28;
Jin A.H., Brandstaetter H., Nevin S.T., Tan C.C., Clark R.J.,
Adams D.J., Alewood P.F., Craik D.J., Daly N.L.;
"Structure of alpha-conotoxin BuIA: influences of disulfide
connectivity on structural dynamics.";
BMC Struct. Biol. 7:28-28(2007).
[9]
NOMENCLATURE.
PubMed=20143226; DOI=10.1007/s00239-010-9321-7;
Puillandre N., Watkins M., Olivera B.M.;
"Evolution of conus peptide genes: duplication and positive selection
in the A-Superfamily.";
J. Mol. Evol. 70:190-202(2010).
-!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
receptors (nAChR) and inhibit them. This peptide potently blocks
numerous mammalian nAChR subtypes: alpha-6/alpha-3-beta-2
(IC(50)=0.258 nM) > alpha-6/alpha-3-beta-4 (IC(50)=1.54 nM) >
alpha-3-beta-2 (IC(50)=5.72 nM) > alpha-3-beta-4 (IC(50)=27.7 nM)
> alpha-4-beta-4 (IC(50)=69.9 nM) > alpha-2-beta-4 (IC(50)=121 nM)
> alpha-7 (IC(50)=272 nM) > alpha-2-beta-2 (IC(50)=800 nM)
(PubMed:15520009). Recovery from toxin block is markedly slower
for beta-4 versus beta-2 subunit-containing nAChRs
(PubMed:15520009, PubMed:16964981). Residues Thr-83, Val-135 and
Phe-143 in the rat beta-2 subunit and Lys-81, Ile-133 and Gln-141
in the rat beta-4 subunit are critical to off-rate differences
(PubMed:16964981). Thus, this toxin represents a novel probe for
distinguishing between beta-2 and beta-4 subunit-containing nAChRs
(PubMed:15520009, PubMed:16964981). {ECO:0000269|PubMed:15520009,
ECO:0000269|PubMed:16964981, ECO:0000269|PubMed:17445276}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/4 pattern.
{ECO:0000305}.
-!- PTM: The native globular disulfide connectivity of this toxin
displays multiple conformations in solution. In contrast, the non-
native ribbon isomer has a well-defined conformation. This ribbon
isomer is inactive on alpha-3-beta-2 and alpha-3-beta-4 nAChR.
{ECO:0000269|PubMed:17445276}.
-!- PTM: Post-translational modification of Pro-49 into hydroxyproline
[P49O] induces a 2800-fold decrease in inhibition of alpha-
6/alpha-3-beta-2-beta-3 and 6-fold decrease in inhibition of
alpha-6/alpha-3-beta-4. {ECO:0000269|PubMed:20739611}.
-!- PTM: Post-translational modification of Pro-49 into hydroxyproline
[P49O] associated with the mutation [T48A] induces a preferential
inhibition of beta-4 subunit-containing nAChRs (over beta-2). On
mouse/rat subunits, this mutant induces potent blocks of alpha-
6/alpha-3-beta-4, moderate block of alpha-3-beta-4, weak block of
alpha-2-beta-4 nAChRs and no activity on alpha-2-beta-2, alpha-3-
beta-2, alpha-4-beta-2, alpha-4-beta-4, alpha-6/alpha-3-beta-2-
beta-3, alpha-7 and alpha-9-alpha-10 and alpha-1-beta-1-delta-
epsilon nAChRs (PubMed:20739611). On human subunits, this mutant
induces inhibitions on alpha-6/alpha-3-beta-4 (IC(50)=7.4 nM),
beta-4-alpha-3-beta-4-alpha-3-alpha-5 (IC(50)=147 nM) and alpha-3-
beta-4 (IC(50)166 nM), but no inhibition of alpha-3-beta-2, alpha-
4-beta-2, alpha-4-beta-4, alpha-6/alpha-3-beta-2-beta-3, beta-3-
alpha-6-beta-2-alpha-4-beta-2 nAChRs (PubMed:26330550).
{ECO:0000269|PubMed:20739611, ECO:0000269|PubMed:26330550}.
-!- PTM: Post-translational modification of Pro-50 into hydroxyproline
[P50O] induces a 9-fold decrease in inhibition of alpha-6/alpha-3-
beta-2-beta-3 and a 4-fold decrease in inhibition of alpha-
6/alpha-3-beta-4. {ECO:0000269|PubMed:20739611}.
-!- MISCELLANEOUS: Does not inhibit alpha-4-beta-2 nAChR (IC(50)=10400
nM or >20000 nM). {ECO:0000269|PubMed:15520009,
ECO:0000269|PubMed:22751014}.
-!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization
at 49-Pro-Pro-50. {ECO:0000269|PubMed:17445276}.
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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PDB; 2I28; NMR; -; A=44-56.
PDB; 2NS3; NMR; -; A=44-56.
PDB; 4EZ1; X-ray; 2.49 A; K/L/M/N/O=44-56.
PDBsum; 2I28; -.
PDBsum; 2NS3; -.
PDBsum; 4EZ1; -.
ProteinModelPortal; P69657; -.
SMR; P69657; -.
ConoServer; 409; BuIA precursor.
EvolutionaryTrace; P69657; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0035792; C:other organism postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR009958; Conotoxin_a-typ.
InterPro; IPR018072; Conotoxin_a-typ_CS.
Pfam; PF07365; Toxin_8; 1.
PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
1: Evidence at protein level;
3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
Disulfide bond; Ion channel impairing toxin; Neurotoxin;
Postsynaptic neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 16 {ECO:0000255}.
PROPEP 17 43 {ECO:0000250}.
/FTId=PRO_0000034869.
PEPTIDE 44 56 Alpha-conotoxin BuIA.
{ECO:0000305|PubMed:15520009,
ECO:0000305|PubMed:16964981,
ECO:0000305|PubMed:16979596,
ECO:0000305|PubMed:17445276,
ECO:0000305|PubMed:20739611}.
/FTId=PRO_0000034870.
MOD_RES 56 56 Cysteine amide.
{ECO:0000305|PubMed:15520009,
ECO:0000305|PubMed:16964981,
ECO:0000305|PubMed:16979596,
ECO:0000305|PubMed:17445276,
ECO:0000305|PubMed:20739611}.
DISULFID 45 51 {ECO:0000244|PDB:2I28,
ECO:0000244|PDB:2NS3,
ECO:0000269|PubMed:16979596,
ECO:0000269|PubMed:17445276}.
DISULFID 46 56 {ECO:0000244|PDB:2I28,
ECO:0000244|PDB:2NS3,
ECO:0000269|PubMed:16979596,
ECO:0000269|PubMed:17445276}.
MUTAGEN 47 47 S->A: No change in inhibition of alpha-
6/alpha-3-beta-2-beta-3 nAChR. 4-fold
decrease in inhibition of alpha-6/alpha-
3-beta-4 nAChR.
{ECO:0000269|PubMed:20739611}.
MUTAGEN 48 48 T->A: 16-fold decrease in inhibition of
alpha-6/alpha-3-beta-2-beta-3 nAChR, 2-
fold decrease in inhibition of alpha-
6/alpha-3-beta-4 nAChR. Preferential
inhibition of beta-4 subunit-containing
nAChRs (over beta-2), potent block of
alpha-6/alpha-3-beta-4, moderate block of
alpha-3-beta-4 and weak block of alpha-2-
beta-4 nAChRs and no activity on alpha-2-
beta-2, alpha-3-beta-2, alpha-4-beta-2,
alpha-4-beta-4, alpha-6/alpha-3-beta-2-
beta-3, alpha-7 and alpha-9-alpha-10 and
alpha-1-beta-1-delta-epsilon nAChRs; when
associated with hydroxyPro-49 (see
miscellaneous).
{ECO:0000269|PubMed:20739611}.
MUTAGEN 52 52 A->S: 4-fold decrease in inhibition of
alpha-6/alpha-3-beta-2-beta-3 nAChR. 11-
fold decrease in inhibition of alpha-
6/alpha-3-beta-4 nAChR.
{ECO:0000269|PubMed:20739611}.
MUTAGEN 53 53 V->A: 37-fold decrease in inhibition of
alpha-6/alpha-3-beta-2-beta-3 nAChR. 2-
fold decrease in inhibition of alpha-
6/alpha-3-beta-4 nAChR.
{ECO:0000269|PubMed:20739611}.
MUTAGEN 54 54 L->A: 50-fold decrease in inhibition of
alpha-6/alpha-3-beta-2-beta-3 nAChR. 6-
fold decrease in inhibition of alpha-
6/alpha-3-beta-4 nAChR.
{ECO:0000269|PubMed:20739611}.
MUTAGEN 55 55 Y->A: 150-fold decrease in inhibition of
alpha-6/alpha-3-beta-2-beta-3 nAChR. 21-
fold decrease in inhibition of alpha-
6/alpha-3-beta-4 nAChR.
{ECO:0000269|PubMed:20739611}.
STRAND 46 48 {ECO:0000244|PDB:2I28}.
HELIX 49 55 {ECO:0000244|PDB:4EZ1}.
SEQUENCE 60 AA; 6394 MW; 86FF88338E0FCCE6 CRC64;
MFTVFLLVVL TTTVVSFPSD RASDGRNAAA NDKASDVVTL VLKGCCSTPP CAVLYCGRRR


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