ID   M3G_CONMR               Reviewed;          68 AA.
AC   P0C1N5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Conotoxin mr3g;
DE   AltName: Full=Mr3.6;
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 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   [2]
RP   PROTEIN SEQUENCE OF 52-67, HYDROXYLATION AT PRO-55 AND PRO-65, AMIDATION AT
RP   CYS-67, MASS SPECTROMETRY, AND BIOASSAY.
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.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues.
CC   -!- MASS SPECTROMETRY: Mass=1666.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17042781};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1N5; -.
DR   ConoServer; 1466; MrIIIG 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: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; Hydroxylation;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..51
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT                   /id="PRO_0000246047"
FT   PEPTIDE         52..67
FT                   /note="Conotoxin mr3g"
FT                   /id="PRO_0000246048"
FT   MOD_RES         55
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT   MOD_RES         67
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT   DISULFID        53..67
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        54..63
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        59..66
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   68 AA;  7337 MW;  767C587ADB123140 CRC64;
     MSKLGVLLTI CLLLFALTAV PLDGDQPADR PAERMQDDIS SERHPMFDAV RDCCPLPACP
     FGCNPCCG