CM3F_CONMR
ID CM3F_CONMR Reviewed; 71 AA.
AC P0C425; F6LPM8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Conotoxin mr3f;
DE AltName: Full=Conotoxin Mr3.9;
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].
RC TISSUE=Venom gland;
RX PubMed=22781954; DOI=10.1016/j.toxicon.2012.06.011;
RA Liu Z., Li H., Liu N., Wu C., Jiang J., Yue J., Jing Y., Dai Q.;
RT "Diversity and evolution of conotoxins in Conus virgo, Conus eburneus,
RT Conus imperialis and Conus marmoreus from the South China Sea.";
RL Toxicon 60:982-989(2012).
RN [2]
RP PROTEIN SEQUENCE OF 55-70, AMIDATION AT ASP-70, MASS SPECTROMETRY,
RP BIOASSAY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
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).
CC -!- FUNCTION: Intracranially injection into mice does not elicit symptoms.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22781954}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:22781954}.
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=1694.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17042781};
CC -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR EMBL; JF322916; ADZ74145.1; -; mRNA.
DR AlphaFoldDB; P0C425; -.
DR SMR; P0C425; -.
DR ConoServer; 1485; MrIIIF.
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 Amidation; Direct protein sequencing; Disulfide bond; Neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..53
FT /id="PRO_0000425739"
FT PEPTIDE 55..70
FT /note="Conotoxin mr3f"
FT /id="PRO_0000289868"
FT MOD_RES 70
FT /note="Aspartic acid 1-amide"
FT /evidence="ECO:0000269|PubMed:17042781"
FT DISULFID 56..68
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 57..66
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 62..69
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ SEQUENCE 71 AA; 7898 MW; 788F684097B04C2A CRC64;
MLKMGVVLFI VLVLFPLATL QLDADKPVER YAENKQLLNP DERRGIILHA LGQRVCCPFG
GCHELCLCCD G