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Alpha-conotoxin PeIA (Fragment)

 CA1A_CONPR              Reviewed;          38 AA.
Q1L777;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 1.
10-MAY-2017, entry version 40.
RecName: Full=Alpha-conotoxin PeIA {ECO:0000303|PubMed:15983035, ECO:0000303|PubMed:21252227, ECO:0000303|PubMed:23846688};
Flags: Precursor; Fragment;
Conus pergrandis (Grand cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=330676;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SYNTHESIS OF 22-37.
TISSUE=Hepatopancreas;
PubMed=15983035; DOI=10.1074/jbc.M504102200;
McIntosh J.M., Plazas P.V., Watkins M., Gomez-Casati M.E.,
Olivera B.M., Elgoyhen A.B.;
"A novel alpha-conotoxin, PeIA, cloned from Conus pergrandis,
discriminates between rat alpha9alpha10 and alpha7 nicotinic
cholinergic receptors.";
J. Biol. Chem. 280:30107-30112(2005).
[2]
FUNCTION, STRUCTURE BY NMR, DISULFIDE BOND, AND SYNTHESIS OF 22-37.
PubMed=21252227; DOI=10.1074/jbc.M110.196170;
Daly N.L., Callaghan B., Clark R.J., Nevin S.T., Adams D.J.,
Craik D.J.;
"Structure and activity of alpha-conotoxin PeIA at nicotinic
acetylcholine receptor subtypes and GABA(B) receptor-coupled N-type
calcium channels.";
J. Biol. Chem. 286:10233-10237(2011).
[3]
FUNCTION, MUTAGENESIS OF SER-30; VAL-31 AND GLU-35, AND SYNTHESIS OF
22-37.
PubMed=22914547; DOI=10.1124/mol.112.080853;
Hone A.J., Scadden M., Gajewiak J., Christensen S., Lindstrom J.,
McIntosh J.M.;
"alpha-Conotoxin PeIA[S9H,V10A,E14N] potently and selectively blocks
alpha6beta2beta3 versus alpha6beta4 nicotinic acetylcholine
receptors.";
Mol. Pharmacol. 82:972-982(2012).
[4]
FUNCTION, MUTAGENESIS OF SER-25; HIS-26; PRO-27; ALA-28; SER-30;
VAL-31; ASN-32; HIS-33; PRO-34; GLU-35 AND LEU-36, AND SYNTHESIS OF
22-37.
PubMed=23846688; DOI=10.1074/jbc.M113.482059;
Hone A.J., Ruiz M., Scadden M., Christensen S., Gajewiak J., Azam L.,
McIntosh J.M.;
"Positional scanning mutagenesis of alpha-conotoxin PeIA identifies
critical residues that confer potency and selectivity for
alpha6/alpha3beta2beta3 and alpha3beta2 nicotinic acetylcholine
receptors.";
J. Biol. Chem. 288:25428-25439(2013).
[5]
MUTAGENESIS OF ALA-28; SER-30; VAL-31; ASN-32 AND GLU-35, 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).
-!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
bind to the nicotinic acetylcholine receptors (nAChR) and thus
inhibit them. This synthetic peptide potently and reversibly
blocks alpha-9-alpha-10 nAChR (IC(50)=6.9-54.9 nM), alpha-3-beta-2
(IC(50)=9.7-97.5 nM) and alpha-6/alpha-3-beta-2-beta-3
(IC(50)=11.1-17.2 nM) (PubMed:15983035, PubMed:21252227,
PubMed:22914547, PubMed:23846688). Also shows a weak inhibition of
alpha-6/alpha-3-beta-4 (IC(50)=147 nM) and alpha-3-beta-4
(IC(50)=480-1500 nM) (PubMed:15983035, PubMed:22914547). This
synthetic toxin also inhibits N-type calcium channels
(Ca2.2/CACNA1B) (IC(50)=1.1 nM) via the activation of the G
protein-coupled GABA(B) receptor in DRG neurons (PubMed:21252227).
{ECO:0000269|PubMed:15983035, ECO:0000269|PubMed:21252227,
ECO:0000269|PubMed:22914547, ECO:0000269|PubMed:23846688}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P85013}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
-!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
{ECO:0000305}.
-!- PTM: The hydroxylation at position Pro-27 is critical, since an
hydroxylation at this position decreases potency of the toxin to
inhibit both alpha-3-beta-2 (1300-fold) and alpha-6/alpha-3-beta-
2-beta-3 (130-fold) nAChRs. {ECO:0000269|PubMed:23846688}.
-!- PTM: A non-modified residue at position Pro-34 is critical, since
an hydroxylation at this position decreases potency of the toxin
to inhibit alpha-3-beta-2 (1-45-fold) and increases potency to
inhibit alpha-6/alpha-3-beta-2-beta-3 (1.77-fold) nAChRs.
{ECO:0000269|PubMed:23846688}.
-!- MISCELLANEOUS: This toxin shows a very weak or no inhibition on
muscle alpha-1-beta-1-gamma-delta, neuronal alpha-7, and neuronal
alpha-4-beta-2 nAChR. {ECO:0000269|PubMed:15983035,
ECO:0000269|PubMed:21252227}.
-!- MISCELLANEOUS: The mutant [A28V, S30H, V31A, N32R, E35A] is
>15'000-fold more potent at inhibiting alpha-6/alpha-3-beta-2-
beta-3 than alpha-3-beta-2, and is essentially inactive on all
other non-alpha6-containing nAChRs including alpha-3-beta-4,
alpha-4-beta-2, alpha-4-beta-4 and alpha-7 (PubMed:23846688). This
mutant shows inhibition on alpha-6/alpha-3-beta-2-beta-3
(IC(50)=3.8 nM), beta-3-alpha-6-beta-2-alpha-4-beta-2 (IC(50)=6.3
nM), alpha-3-beta-4 (IC(50)=3.7 uM), alpha-3-beta-2 (IC(50)=6.1
uM), beta-4-alpha-3-beta-4-alpha-3-alpha-5 (IC(50)=9.2 uM), and
does not inhibit alpha-4-beta-2 and alpha-4-beta-4 nAChRs
(PubMed:26330550). {ECO:0000269|PubMed:23846688,
ECO:0000269|PubMed:26330550}.
-!- MISCELLANEOUS: The mutant [S30H, V31A, E35N] is >290-fold more
potent at inhibiting alpha-6/alpha-3-beta-2-beta-3 than alpha-
6/alpha-3-beta-4, demonstrating that it can discriminate between
alpha-6-beta-2-beta-3 and alpha-6-beta-4 nAChRs.
{ECO:0000269|PubMed:22914547}.
-!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ008450; AAY57814.1; -; Genomic_DNA.
PDB; 5JME; X-ray; 2.34 A; F/G/H/I=22-37.
PDBsum; 5JME; -.
ProteinModelPortal; Q1L777; -.
SMR; Q1L777; -.
ConoServer; 5; PeIA precursor.
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:0009405; P:pathogenesis; IEA:InterPro.
InterPro; IPR009958; Conotoxin_a-typ.
Pfam; PF07365; Toxin_8; 1.
3: Inferred from homology;
3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
Calcium channel impairing toxin; Disulfide bond;
Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin;
Secreted; Toxin.
PROPEP <1 21 {ECO:0000250}.
/FTId=PRO_0000247850.
PEPTIDE 22 37 Alpha-conotoxin PeIA.
{ECO:0000305|PubMed:15983035,
ECO:0000305|PubMed:21252227}.
/FTId=PRO_0000247851.
SITE 26 26 Important residue for inhibiting alpha-3-
beta-2 nAChR.
{ECO:0000269|PubMed:23846688}.
SITE 27 27 Important residue for inhibiting alpha-3-
beta-2 nAChR.
{ECO:0000269|PubMed:23846688}.
SITE 30 30 Residue that is not optimum for the most
potent inhibition of alpha-3-beta-2 and
alpha-6/alpha-3-beta-2-beta-3 and alpha-
6/alpha-3-beta-4.
{ECO:0000269|PubMed:22914547,
ECO:0000269|PubMed:23846688}.
SITE 31 31 Important residue for inhibiting alpha-3-
beta-2 nAChR.
{ECO:0000269|PubMed:23846688}.
SITE 32 32 Important residue for inhibiting alpha-3-
beta-2 nAChR.
{ECO:0000269|PubMed:23846688}.
SITE 33 33 Important residue for inhibiting alpha-3-
beta-2 and alpha-6/alpha-3-beta-2-beta-3
nAChR. {ECO:0000269|PubMed:23846688}.
MOD_RES 37 37 Cysteine amide. {ECO:0000250}.
DISULFID 23 29 {ECO:0000305|PubMed:21252227,
ECO:0000312|PDB:5JME}.
DISULFID 24 37 {ECO:0000305|PubMed:21252227,
ECO:0000312|PDB:5JME}.
MUTAGEN 25 25 S->A: 1.9-fold decrease in inhibition of
alpha-3-beta-2 nAChR and 1.4-fold
increase in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 26 26 H->A: 1350-fold and 65-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 26 26 H->N: 1.4-fold decrease in inhibition of
alpha-3-beta-2 nAChR and 6.4-fold
increase in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 27 27 P->A: 580-fold and 20-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 28 28 A->V: 4.5-fold decrease in inhibition of
alpha-3-beta-2 nAChR and 2.5-fold
increase in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 30 30 S->A: 3.3-fold and 2.4-fold increase in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 30 30 S->H: 14-fold, 11-fold and 10-fold
increase in inhibition of alpha-3-beta-2,
alpha-6/alpha-3-beta-2-beta-3 and alpha-
6/alpha-3-beta-4 nAChR, respectively.
{ECO:0000269|PubMed:22914547}.
MUTAGEN 30 30 S->R: 4.6-fold and 7.5-fold increase in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 31 31 V->A: 4.4-fold and 4.6-fold increase in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively, and 2-fold decrease in
inhibition of alpha-6/alpha-3-beta-4.
{ECO:0000269|PubMed:22914547}.
MUTAGEN 31 31 V->L: 5-fold increase in inhibition of
alpha-3-beta-2 nAChR and 1.1-fold
decrease in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 31 31 V->R: 2400-fold and 33-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 32 32 N->A: 2.4-fold and 1.7-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 32 32 N->E: 2.0-fold and 6.6-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 32 32 N->K: 2400-fold and 2.4-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 32 32 N->R: 1600-fold and 2.7-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 33 33 H->A: 2700-fold and 420-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 34 34 P->A: 3.3-fold decrease in inhibition of
alpha-3-beta-2 nAChR and 1.3-fold
increase in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 34 34 P->S: 1.5-fold decrease in inhibition of
alpha-3-beta-2 and no change in
inhibition of alpha-6/alpha-3-beta-2-
beta-3 nAChR, respectively.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 35 35 E->A: 5.2-fold decrease in inhibition of
alpha-3-beta-2 nAChR and 1.4-fold
increase in inhibition of alpha-6/alpha-
3-beta-2-beta-3 nAChR.
{ECO:0000269|PubMed:23846688}.
MUTAGEN 35 35 E->N: 15-fold, 2-fold and 3-fold decrease
in inhibition of alpha-3-beta-2, alpha-
6/alpha-3-beta-2-beta-3 and alpha-
6/alpha-3-beta-4 nAChR, respectively.
{ECO:0000269|PubMed:22914547}.
MUTAGEN 36 36 L->A: 7.2-fold and 4.8-fold decrease in
inhibition of alpha-3-beta-2 and alpha-
6/alpha-3-beta-2-beta-3 nAChR,
respectively.
{ECO:0000269|PubMed:23846688}.
NON_TER 1 1
HELIX 23 25 {ECO:0000244|PDB:5JME}.
HELIX 27 30 {ECO:0000244|PDB:5JME}.
TURN 34 36 {ECO:0000244|PDB:5JME}.
SEQUENCE 38 AA; 3900 MW; AE40EFB659EB0EFC CRC64;
FDGRNAAAND KASDLVALTV RGCCSHPACS VNHPELCG


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