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Mu-conotoxin PIIIA (Mu-conotoxin P3.7)

 CM3A_CONPU              Reviewed;          73 AA.
P58925;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
22-NOV-2017, entry version 86.
RecName: Full=Mu-conotoxin PIIIA {ECO:0000303|PubMed:9614224};
AltName: Full=Mu-conotoxin P3.7;
Flags: Precursor;
Conus purpurascens (Purple cone).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Conus.
NCBI_TaxID=41690;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Venom duct;
PubMed=15924437; DOI=10.1021/bi047541b;
Corpuz G.P., Jacobsen R.B., Jimenez E.C., Watkins M., Walker C.,
Colledge C., Garrett J.E., McDougal O., Li W., Gray W.R.,
Hillyard D.R., Rivier J., McIntosh J.M., Cruz L.J., Olivera B.M.;
"Definition of the M-conotoxin superfamily: characterization of novel
peptides from molluscivorous Conus venoms.";
Biochemistry 44:8176-8186(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 47-73, SYNTHESIS OF 50-71, AND
MUTAGENESIS OF ARG-63.
TISSUE=Venom duct;
PubMed=9614224;
Shon K.-J., Olivera B.M., Watkins M., Jacobsen R.B., Gray W.R.,
Floresca C.Z., Cruz L.J., Hillyard D.R., Brink A., Terlau H.,
Yoshikami D.;
"Mu-conotoxin PIIIA, a new peptide for discriminating among
tetrodotoxin-sensitive Na channel subtypes.";
J. Neurosci. 18:4473-4481(1998).
[3]
FUNCTION.
PubMed=10627583;
Safo P., Rosenbaum T., Shcherbatko A., Choi D.-Y., Han E.,
Toledo-Aral J.J., Olivera B.M., Brehm P., Mandel G.;
"Distinction among neuronal subtypes of voltage-activated sodium
channels by mu-conotoxin PIIIA.";
J. Neurosci. 20:76-80(2000).
[4]
FUNCTION.
PubMed=18950653; DOI=10.1016/j.toxicon.2008.10.017;
Holford M., Zhang M.-M., Gowd K.H., Azam L., Green B.R., Watkins M.,
Ownby J.-P., Yoshikami D., Bulaj G., Olivera B.M.;
"Pruning nature: biodiversity-derived discovery of novel sodium
channel blocking conotoxins from Conus bullatus.";
Toxicon 53:90-98(2009).
[5]
FUNCTION, AND SYNTHESIS OF 50-71.
PubMed=22229737; DOI=10.1111/j.1476-5381.2012.01837.x;
Favreau P., Benoit E., Hocking H.G., Carlier L., D'Hoedt D.,
Leipold E., Markgraf R., Schlumberger S., Cordova M.A., Gaertner H.,
Paolini-Bertrand M., Hartley O., Tytgat J., Heinemann S.H.,
Bertrand D., Boelens R., Stocklin R., Molgo J.;
"A novel u-conopeptide, CnIIIC, exerts potent and preferential
inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic
acetylcholine receptors.";
Br. J. Pharmacol. 166:1654-1668(2012).
[6]
FUNCTION, AND SYNTHESIS OF 50-71.
PubMed=21652775; DOI=10.1073/pnas.1107027108;
Wilson M.J., Yoshikami D., Azam L., Gajewiak J., Olivera B.M.,
Bulaj G., Zhang M.M.;
"mu-Conotoxins that differentially block sodium channels Nav1.1
through 1.8 identify those responsible for action potentials in
sciatic nerve.";
Proc. Natl. Acad. Sci. U.S.A. 108:10302-10307(2011).
[7]
FUNCTION.
PubMed=23146020; DOI=10.1111/bph.12051;
Zhang M.M., Wilson M.J., Azam L., Gajewiak J., Rivier J.E., Bulaj G.,
Olivera B.M., Yoshikami D.;
"Co-expression of Na(V)beta subunits alters the kinetics of inhibition
of voltage-gated sodium channels by pore-blocking mu-conotoxins.";
Br. J. Pharmacol. 168:1597-1610(2013).
[8]
STRUCTURE BY NMR OF 50-71, SYNTHESIS OF 50-71, FUNCTION, AND DISULFIDE
BONDS FOR 3 SYNTHETIC ISOMERS.
PubMed=22407516; DOI=10.1002/anie.201107011;
Tietze A.A., Tietze D., Ohlenschlager O., Leipold E., Ullrich F.,
Kuhl T., Mischo A., Buntkowsky G., Gorlach M., Heinemann S.H.,
Imhof D.;
"Structurally diverse mu-conotoxin PIIIA isomers block sodium channel
NaV 1.4.";
Angew. Chem. Int. Ed. 51:4058-4061(2012).
[9]
STRUCTURE BY NMR OF 50-71, SYNTHESIS OF 50-71, AND DISULFIDE BONDS.
PubMed=12006587; DOI=10.1074/jbc.M201611200;
Nielsen K.J., Watson M., Adams D.J., Hammarstroem A.K., Gage P.W.,
Hill J.M., Craik D.J., Thomas L., Adams D., Alewood P.F., Lewis R.J.;
"Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of
persistent TTX-sensitive sodium channels.";
J. Biol. Chem. 277:27247-27255(2002).
-!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav).
This toxin potently blocks rNav1.4/SCN4A (IC(50)=36-41 nM)
(PubMed:10627583, PubMed:21652775). It also moderately blocks
rNav1.1/SCN1A (IC(50)=120 nM), rNav1.2/SCN2A (IC(50)=620 nM),
rNav1.3/SCN3A (IC(50)=3.2 uM), mNav1.6/SCN8A (IC(50)=100 nM)
(PubMed:10627583, PubMed:21652775). This inhibition is reversible.
The block of Nav1.1, Nav1.2, and Nav1.6 is modified when beta-
subunits are coexpressed with alpha subunits. Hence, blocks of
channels containing the beta-1 and beta-3 subunits are more potent
(compared to channels without beta subunits), whereas blocks of
channels containing the beta-2 and beta-4 are less potent
(compared to channels without beta subunits). In vivo, this
peptide causes flaccid paralysis in both mice and fish.
{ECO:0000269|PubMed:10627583, ECO:0000269|PubMed:18950653,
ECO:0000269|PubMed:21652775, ECO:0000269|PubMed:22229737,
ECO:0000269|PubMed:22407516, ECO:0000269|PubMed:23146020}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01523}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000305|PubMed:9614224}.
-!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in
the M-4 branch, since 4 residues stand between the fourth and the
fifth cysteine residues. {ECO:0000305}.
-!- PTM: 3D-structure of 3 disulfide-bond connectivities isomers is
described (PIIIA-1 (C1-C5, C2-C6, C3-C4), PIIIA-2 (C1-C4, C2-C5,
C3-C6) and PIIIA-3 (C1-C2, C3-C4, C5-C6)) (PubMed:22407516). Only
PIIIA-2 contains the cysteine connectivity described as typical
for native mu-conotoxins. However, PIIIA-1 is more potent than
PIIIA-2, suggesting another possible disulfid connectivity. For
this reason, both connectivities have been indicated in features.
{ECO:0000269|PubMed:22407516}.
-!- MISCELLANEOUS: Exists in two forms, due to cis-trans isomerization
at Hyp-57. Adopts a predominately trans conformation (Probable).
{ECO:0000305|PubMed:12006587}.
-!- MISCELLANEOUS: This toxin does not or only weakly blocks
rNav1.5/SCN5A, rNav1.7/SCN9A (IC(50)=3.1-6.2 uM and >100 uM), and
rNav1.8/SCN10A. {ECO:0000269|PubMed:10627583,
ECO:0000269|PubMed:21652775}.
-!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
PDB; 1R9I; NMR; -; A=50-71.
PDBsum; 1R9I; -.
SMR; P58925; -.
TCDB; 8.B.28.1.2; the mu-conotoxin (mu-conotoxin) family.
ConoServer; 1407; PIIIA precursor.
EvolutionaryTrace; P58925; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
InterPro; IPR004214; Conotoxin.
InterPro; IPR008036; Conotoxin_mu-typ.
Pfam; PF02950; Conotoxin; 1.
PROSITE; PS60013; MU_CONOTOXIN; 1.
2: Evidence at transcript level;
3D-structure; Amidation; Cleavage on pair of basic residues;
Disulfide bond; Hydroxylation; Ion channel impairing toxin;
Neurotoxin; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin;
Voltage-gated sodium channel impairing toxin.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 49 {ECO:0000305|PubMed:9614224}.
/FTId=PRO_0000035053.
PEPTIDE 50 71 Mu-conotoxin PIIIA.
{ECO:0000305|PubMed:9614224}.
/FTId=PRO_0000035054.
SITE 63 63 Important for activity.
{ECO:0000269|PubMed:9614224}.
MOD_RES 50 50 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:12006587,
ECO:0000305|PubMed:9614224}.
MOD_RES 57 57 4-hydroxyproline.
{ECO:0000305|PubMed:9614224}.
MOD_RES 67 67 4-hydroxyproline.
{ECO:0000305|PubMed:9614224}.
MOD_RES 71 71 Cysteine amide.
{ECO:0000305|PubMed:9614224}.
DISULFID 53 70 In PIIIA-1; alternate.
{ECO:0000250|UniProtKB:P01523}.
DISULFID 53 65 In PIIIA-2; alternate.
{ECO:0000269|PubMed:12006587,
ECO:0000312|PDB:1R9I}.
DISULFID 54 71 In PIIIA-1; alternate.
{ECO:0000250|UniProtKB:P01523}.
DISULFID 54 70 In PIIIA-2; alternate.
{ECO:0000269|PubMed:12006587,
ECO:0000312|PDB:1R9I}.
DISULFID 60 71 In PIIIA-2; alternate.
{ECO:0000269|PubMed:12006587}.
DISULFID 60 65 In PIIIA-1; alternate.
{ECO:0000250|UniProtKB:P01523}.
MUTAGEN 63 63 R->A: Decrease in affinity to channel.
{ECO:0000269|PubMed:9614224}.
TURN 52 55 {ECO:0000244|PDB:1R9I}.
HELIX 59 61 {ECO:0000244|PDB:1R9I}.
TURN 63 67 {ECO:0000244|PDB:1R9I}.
SEQUENCE 73 AA; 8334 MW; 1AF52E344F6EE982 CRC64;
MSKLGVLLTI CLLLFPITAL PMDGDQPADR LAERMQDNIS SEEHPFEKRQ RLCCGFPKSC
RSRQCKPHRC CGR


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