ID   M3A_CONMR               Reviewed;          17 AA.
AC   P0C1M9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Conotoxin mr3a {ECO:0000303|PubMed:14717596, ECO:0000303|PubMed:15924437, ECO:0000303|PubMed:17042781};
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   PROTEIN SEQUENCE, STRUCTURE BY NMR, DISULFIDE BONDS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=14717596; DOI=10.1021/bi0353732;
RA   McDougal O.M., Poulter C.D.;
RT   "Three-dimensional structure of the mini-M conotoxin mr3a.";
RL   Biochemistry 43:425-429(2004).
RN   [2]
RP   PROTEIN SEQUENCE, SYNTHESIS, DISULFIDE BONDS, MASS SPECTROMETRY,
RP   HYDROXYLATION AT PRO-14, AND BIOASSAY.
RC   TISSUE=Venom;
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   PROTEIN SEQUENCE, 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: Intracranial injection into mice causes circular motion,
CC       barrel rolling and convulsions. {ECO:0000269|PubMed:15924437,
CC       ECO:0000269|PubMed:17042781}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14717596}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:14717596}.
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. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1721.6; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:15924437};
CC   -!- MASS SPECTROMETRY: Mass=1705.3; Method=Electrospray; Note=Without
CC       hydroxyPro-14.; Evidence={ECO:0000269|PubMed:17042781};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1M9; -.
DR   ConoServer; 1422; MrIIIA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydroxylation; Neurotoxin;
KW   Secreted; Toxin.
FT   PEPTIDE         1..17
FT                   /note="Conotoxin mr3a"
FT                   /evidence="ECO:0000269|PubMed:14717596,
FT                   ECO:0000269|PubMed:15924437, ECO:0000269|PubMed:17042781"
FT                   /id="PRO_0000246037"
FT   MOD_RES         14
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:15924437"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000269|PubMed:14717596,
FT                   ECO:0000269|PubMed:15924437"
FT   DISULFID        3..12
FT                   /evidence="ECO:0000269|PubMed:14717596,
FT                   ECO:0000269|PubMed:15924437"
FT   DISULFID        8..15
FT                   /evidence="ECO:0000269|PubMed:14717596,
FT                   ECO:0000269|PubMed:15924437"
SQ   SEQUENCE   17 AA;  1712 MW;  794A31F4EA4671A4 CRC64;
     GCCGSFACRF GCVPCCV