CM3E_CONMR
ID CM3E_CONMR Reviewed; 71 AA.
AC Q5EHP3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Conotoxin mr3e;
DE AltName: Full=Mr3.4;
DE AltName: Full=Mr3.7;
DE Flags: Precursor;
OS Conus marmoreus (Marble cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX NCBI_TaxID=42752;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 55-70, AMIDATION AT ASP-70,
RP DISULFIDE BONDS, MASS SPECTROMETRY, SYNTHESIS OF 55-70, BIOASSAY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom duct;
RX PubMed=17042781; DOI=10.1111/j.1742-4658.2006.05493.x;
RA Han Y.-H., Wang Q., Jiang H., Liu L., Xiao C., Yuan D.-D., Shao X.-X.,
RA Dai Q.-Y., Cheng J.-S., Chi C.-W.;
RT "Characterization of novel M-superfamily conotoxins with new disulfide
RT linkage.";
RL FEBS J. 273:4972-4982(2006).
RN [2]
RP STRUCTURE BY NMR OF 55-70, AND DISULFIDE BONDS.
RX PubMed=17437523; DOI=10.1111/j.1742-4658.2007.05795.x;
RA Du W.-H., Han Y.-H., Huang F.-J., Li J., Chi C.-W., Fang W.-H.;
RT "Solution structure of an M-1 conotoxin with a novel disulfide linkage.";
RL FEBS J. 274:2596-2602(2007).
CC -!- FUNCTION: Intracranially injection into mice does not elicit symptoms.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17042781}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:17042781}.
CC -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC 1 branch, since 1 residue stands between the fourth and the fifth
CC cysteine residues. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1743.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17042781};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; AY880683; AAW78560.1; -; mRNA.
DR PDB; 2EFZ; NMR; -; A=55-70.
DR PDBsum; 2EFZ; -.
DR AlphaFoldDB; Q5EHP3; -.
DR BMRB; Q5EHP3; -.
DR SMR; Q5EHP3; -.
DR ConoServer; 1081; MrIIIE precursor.
DR EvolutionaryTrace; Q5EHP3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Amidation; Direct protein sequencing; Disulfide bond;
KW Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..54
FT /evidence="ECO:0000269|PubMed:17042781"
FT /id="PRO_0000289866"
FT PEPTIDE 55..70
FT /note="Conotoxin mr3e"
FT /id="PRO_0000289867"
FT MOD_RES 70
FT /note="Aspartic acid 1-amide"
FT /evidence="ECO:0000269|PubMed:17042781"
FT DISULFID 56..68
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:17437523, ECO:0000312|PDB:2EFZ"
FT DISULFID 57..66
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:17437523, ECO:0000312|PDB:2EFZ"
FT DISULFID 62..69
FT /evidence="ECO:0000269|PubMed:17042781,
FT ECO:0000269|PubMed:17437523, ECO:0000312|PDB:2EFZ"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2EFZ"
SQ SEQUENCE 71 AA; 7976 MW; D4EF684276F2A0D9 CRC64;
MLKMGVVLFI VLVLFPLATL QLDADQPVER YAENKRLLNP DERRGIILHA LGQRVCCPFG
GCHELCYCCD G
