ID   CMCE_CONRE              Reviewed;          16 AA.
AC   P85017; P0DPJ4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 3.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Conotoxin Reg12e {ECO:0000303|PubMed:17153339};
DE   AltName: Full=Conotoxin reg3e {ECO:0000303|PubMed:29283511};
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   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AMIDATION AT PRO-16, AND
RP   HYDROXYLATION AT PRO-11.
RC   TISSUE=Venom;
RX   PubMed=17153339; DOI=10.1007/978-3-540-30880-5_4;
RA   Franco A., Pisarewicz K., Moller C., Mora D., Fields G.B., Mari F.;
RT   "Hyperhydroxylation: a new strategy for neuronal targeting by venomous
RT   marine molluscs.";
RL   Prog. Mol. Subcell. Biol. 43:83-103(2006).
RN   [2]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   HYDROXYLATION AT PRO-11.
RC   TISSUE=Venom;
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:17153339}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:17153339}.
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   -!- PTM: Reg12e and reg3e are conotoxins with identical sequences, but
CC       different post-translational modifications. Reg12e is C-terminally
CC       amidated, while reg3e is not. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1738.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29283511};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P85017; -.
DR   ConoServer; 1493; Reg12e.
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   Amidation; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Secreted; Toxin.
FT   PEPTIDE         1..16
FT                   /note="Conotoxin Reg12e"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT                   /id="PRO_0000259391"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:17153339,
FT                   ECO:0000269|PubMed:29283511"
FT   MOD_RES         16
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT   DISULFID        2..13
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        3..10
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        8..12
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ   SEQUENCE   16 AA;  1728 MW;  7BAD18097BCCB376 CRC64;
     KCCMRPICTC PCCIGP