CM3E_CONPU
ID CM3E_CONPU Reviewed; 75 AA.
AC P56529;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Psi-conotoxin PIIIE {ECO:0000303|PubMed:15924437, ECO:0000303|PubMed:9236004};
DE AltName: Full=Psi-conotoxin P3.8;
DE Flags: Precursor;
OS Conus purpurascens (Purple cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX NCBI_TaxID=41690;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-74, FUNCTION, SYNTHESIS
RP OF 51-74, HYDROXYLATION AT PRO-52; PRO-53 AND PRO-64, AMIDATION AT GLY-74,
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=9236004; DOI=10.1021/bi970235w;
RA Shon K.-J., Grilley M., Jacobsen R.B., Cartier G.E., Hopkins C., Gray W.R.,
RA Watkins M., Hillyard D.R., Rivier J.E., Torres J., Yoshikami D.,
RA Olivera B.M.;
RT "A noncompetitive peptide inhibitor of the nicotinic acetylcholine receptor
RT from Conus purpurascens venom.";
RL Biochemistry 36:9581-9587(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=15924437; DOI=10.1021/bi047541b;
RA Corpuz G.P., Jacobsen R.B., Jimenez E.C., Watkins M., Walker C.,
RA Colledge C., Garrett J.E., McDougal O., Li W., Gray W.R., Hillyard D.R.,
RA Rivier J., McIntosh J.M., Cruz L.J., Olivera B.M.;
RT "Definition of the M-conotoxin superfamily: characterization of novel
RT peptides from molluscivorous Conus venoms.";
RL Biochemistry 44:8176-8186(2005).
RN [3]
RP STRUCTURE BY NMR OF 51-74, HYDROXYLATION AT PRO-52; PRO-53 AND PRO-64,
RP AMIDATION AT GLY-74, AND DISULFIDE BONDS.
RX PubMed=9477946; DOI=10.1021/bi972186t;
RA Mitchell S.S., Shon K.-J., Foster M.P., Davis D.R., Olivera B.M.,
RA Ireland C.M.;
RT "Three-dimensional solution structure of conotoxin psi-PIIIE, an
RT acetylcholine gated ion channel antagonist.";
RL Biochemistry 37:1215-1220(1998).
RN [4]
RP STRUCTURE BY NMR OF 51-75, HYDROXYLATION AT PRO-52; PRO-53 AND PRO-64,
RP AMIDATION AT GLY-74, AND DISULFIDE BONDS.
RX PubMed=12767215; DOI=10.1021/bi027274e;
RA Van Wagoner R.M., Ireland C.M.;
RT "An improved solution structure for psi-conotoxin PiiiE.";
RL Biochemistry 42:6347-6352(2003).
CC -!- FUNCTION: Psi-conotoxins act on postsynaptic membranes, and act as non-
CC competitive antagonist of nicotinic acetylcholine receptors (nAChR). Is
CC more toxic than Psi-conotoxin PIIIF. In vivo, has paralytic activity
CC when injected intraperitoneally into goldfish.
CC {ECO:0000269|PubMed:9236004}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9236004}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:9236004}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 4 branch, since 4 residues stand between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=2716.0; Method=LSI;
CC Evidence={ECO:0000269|PubMed:9236004};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A58999; A58999.
DR PDB; 1AS5; NMR; -; A=51-73.
DR PDB; 1JLO; NMR; -; A=51-73.
DR PDBsum; 1AS5; -.
DR PDBsum; 1JLO; -.
DR AlphaFoldDB; P56529; -.
DR SMR; P56529; -.
DR ConoServer; 1406; PIIIE precursor.
DR EvolutionaryTrace; P56529; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
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 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..50
FT /evidence="ECO:0000305|PubMed:9236004"
FT /id="PRO_0000246005"
FT PEPTIDE 51..74
FT /note="Psi-conotoxin PIIIE"
FT /evidence="ECO:0000269|PubMed:9236004"
FT /id="PRO_0000035059"
FT MOD_RES 52
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9236004, ECO:0000269|PubMed:9477946"
FT MOD_RES 53
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9236004, ECO:0000269|PubMed:9477946"
FT MOD_RES 64
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9236004, ECO:0000269|PubMed:9477946"
FT MOD_RES 74
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9236004, ECO:0000269|PubMed:9477946"
FT DISULFID 54..66
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9477946, ECO:0007744|PDB:1AS5,
FT ECO:0007744|PDB:1JLO"
FT DISULFID 55..71
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9477946, ECO:0007744|PDB:1AS5,
FT ECO:0007744|PDB:1JLO"
FT DISULFID 60..72
FT /evidence="ECO:0000269|PubMed:12767215,
FT ECO:0000269|PubMed:9477946, ECO:0007744|PDB:1AS5,
FT ECO:0007744|PDB:1JLO"
FT VARIANT 56
FT /note="M -> L"
FT VARIANT 59
FT /note="R -> K"
FT VARIANT 74
FT /note="G -> R"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1AS5"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1JLO"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1JLO"
SQ SEQUENCE 75 AA; 8348 MW; 0FEA0497100A9E01 CRC64;
MSKLGALLTI CLLLFPITAL LMDGDQPADR PAERMDYDIS SEVHRLLERR HPPCCMYGRC
RRYPGCSSAS CCQGG
