ID   CM3A_CONRE              Reviewed;          73 AA.
AC   A0A2I6EDN5;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Conotoxin reg3a {ECO:0000303|PubMed:29283511};
DE   AltName: Full=Reg3.18 {ECO:0000303|PubMed:29283511};
DE            Short=Rg3.18 {ECO:0000312|EMBL:AUJ88076.1};
DE   Flags: Precursor;
OS   Conus regius (Crown cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=101314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-72, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND HYDROXYLATION AT PRO-59; PRO-60; PRO-65 AND
RP   PRO-70.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=29283511; DOI=10.1111/febs.14372;
RA   Franco A., Dovell S., Moller C., Grandal M., Clark E., Mari F.;
RT   "Structural plasticity of Mini-M conotoxins: expression of all mini-M
RT   subtypes by Conus regius.";
RL   FEBS J. 285:887-902(2017).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29283511}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:29283511}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       3 branch, since 3 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:29283511}.
CC   -!- MASS SPECTROMETRY: Mass=1814.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29283511};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MF588952; AUJ88076.1; -; mRNA.
DR   AlphaFoldDB; A0A2I6EDN5; -.
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   Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..55
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000444758"
FT   PEPTIDE         56..72
FT                   /note="Conotoxin reg3a"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT                   /id="PRO_5014450508"
FT   MOD_RES         59
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         60
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         65
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         70
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         72
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   73 AA;  8109 MW;  AD0F625B6DD96F28 CRC64;
     MMSKLRVLLT ICLLLFPLSA LPLDGDQPAD QPAKRMWNGK LAARKPRFDK YDLVRGCCPP
     QWCGPDCTSP CCG