ID   M3D_CONMR               Reviewed;          67 AA.
AC   P0C1N1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Conotoxin mr3d;
DE   AltName: Full=Conotoxin Mr3.2;
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 53-66, HYDROXYLATION AT PRO-64, AMIDATION AT CYS-66,
RP   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=1462.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17042781};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1N1; -.
DR   ConoServer; 1471; MrIIID 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..52
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT                   /id="PRO_0000246039"
FT   PEPTIDE         53..66
FT                   /note="Conotoxin mr3d"
FT                   /id="PRO_0000246040"
FT   MOD_RES         64
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT   MOD_RES         66
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:17042781"
FT   DISULFID        53..66
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        54..62
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        58..65
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   67 AA;  7340 MW;  043A2CA6E49383C5 CRC64;
     MSKLGILLTI CLLLFPLTAV PLDGDQPADR PAERMQDDIS SEHHPFFDPV KRCCRLSCGL
     GCHPCCG