CM4B_CONPE
ID CM4B_CONPE Reviewed; 70 AA.
AC P58927; Q9BH61; Q9BP54;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Mu-conotoxin PnIVB;
DE Flags: Precursor;
OS Conus pennaceus (Feathered cone) (Conus episcopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Darioconus.
OX NCBI_TaxID=37335;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL Mol. Biol. Evol. 18:120-131(2001).
RN [2]
RP PROTEIN SEQUENCE OF 54-70, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7612605; DOI=10.1021/bi00027a014;
RA Fainzilber M., Nakamura T., Gaathon A., Lodder J.C., Kits K.S.,
RA Burlingame A.L., Zlotkin E.;
RT "A new cysteine framework in sodium channel blocking conotoxins.";
RL Biochemistry 34:8649-8656(1995).
RN [3]
RP FUNCTION.
RX PubMed=7620628; DOI=10.1111/j.1460-9568.1995.tb00684.x;
RA Hasson A., Fainzilber M., Zlotkin E., Spira M.E.;
RT "Electrophysiological characterization of a novel conotoxin that blocks
RT molluscan sodium channels.";
RL Eur. J. Neurosci. 7:815-818(1995).
CC -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels (Nav).
CC Blocks reversibly sodium channels in molluskan neurons, but has no
CC effect on sodium currents in bovine chromaffin cells or in rat brain
CC synaptosomes. Induces paralysis in bivalve mollusks (Mytilus). No
CC effect are observed on fish (Gambusia) and fly larvae (Sarcophaga). Is
CC approximately 6 times more potent than PnIVA in blockade of the sodium
CC current in Lymnaea neurons. {ECO:0000269|PubMed:7620628}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC -!- PTM: Contains 3 disulfide bonds (By similarity). They are not added,
CC since framework IV presents two different connectivities (I-V, II-III,
CC IV-VI and I-III, II-V, IV-VI). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=1862.8; Method=LSI;
CC Evidence={ECO:0000269|PubMed:7612605};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; AF214931; AAG60359.1; -; mRNA.
DR EMBL; AF215093; AAG60514.1; -; mRNA.
DR EMBL; AF215094; AAG60515.1; -; mRNA.
DR AlphaFoldDB; P58927; -.
DR ConoServer; 1559; PnIVB.
DR ConoServer; 618; PnIVB precursor.
DR ConoServer; 771; PnIVB precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR004214; Conotoxin.
DR Pfam; PF02950; Conotoxin; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin; Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..51
FT /evidence="ECO:0000305|PubMed:7612605"
FT /id="PRO_0000392725"
FT PEPTIDE 54..70
FT /note="Mu-conotoxin PnIVB"
FT /evidence="ECO:0000269|PubMed:7612605"
FT /id="PRO_0000044497"
FT SITE 57
FT /note="Important for binding and activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 70 AA; 7770 MW; 8A90EEDF3F90B301 CRC64;
MMSKLGVLLI ICLLLCPLTA VPQDGDQPAD QPAERMQDDI SSEHHPFFDP VKRCCKYGWT
CWLGCSPCGC
