ID   CMCL_CONRE              Reviewed;          53 AA.
AC   A0A2I6EDL5;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Reg12l {ECO:0000303|PubMed:17153339};
DE   AltName: Full=Reg3.4 {ECO:0000303|PubMed:29283511};
DE            Short=Rg3.4 {ECO:0000312|EMBL:AUJ88062.1};
DE   Flags: Precursor; Fragment;
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].
RC   TISSUE=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).
RN   [2]
RP   PROTEIN SEQUENCE OF 35-53, AND SUBCELLULAR LOCATION.
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).
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   -!- MISCELLANEOUS: The mature sequence of Reg3.4 described in Franco et
CC       al., 2017 corresponds to the mature sequence of conotoxin reg3l (AC
CC       P0DQO8). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MF588938; AUJ88062.1; -; mRNA.
DR   AlphaFoldDB; A0A2I6EDL5; -.
DR   SMR; A0A2I6EDL5; -.
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   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Toxin.
FT   PROPEP          <1..34
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444769"
FT   PEPTIDE         35..53
FT                   /note="Reg12l"
FT                   /evidence="ECO:0000269|PubMed:17153339"
FT                   /id="PRO_0000444770"
FT   DISULFID        36..50
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        37..48
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        42..51
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   NON_TER         1
FT                   /evidence="ECO:0000305|PubMed:29283511"
SQ   SEQUENCE   53 AA;  5945 MW;  4C12D7EA254E3A4D CRC64;
     RVLFRSGDQP ADQPAERMQD ISPEQNPLFH PDKRRCCPMP GCFAGPFCPC CPP