ID   CM3B_CONRE              Reviewed;          51 AA.
AC   P85021; A0A2I6EDN4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 2.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Conotoxin Reg3b {ECO:0000303|PubMed:29283511};
DE   AltName: Full=Reg12c {ECO:0000303|PubMed:17153339};
DE   AltName: Full=Reg12i {ECO:0000305};
DE   AltName: Full=Reg3.13 {ECO:0000303|PubMed:29283511};
DE            Short=Rg3.13 {ECO:0000312|EMBL:AUJ88071.1};
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], PROTEIN SEQUENCE OF 37-51, MASS SPECTROMETRY,
RP   STRUCTURE BY NMR OF 37-51, AND DISULFIDE BOND.
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 37-51, 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       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1669.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29283511};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MF588947; AUJ88071.1; -; mRNA.
DR   PDB; 6BX9; NMR; -; A=37-51.
DR   PDBsum; 6BX9; -.
DR   AlphaFoldDB; P85021; -.
DR   SMR; P85021; -.
DR   ConoServer; 7504; reg3b.
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   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          <1..4
FT                   /evidence="ECO:0000305"
FT   PROPEP          5..36
FT                   /evidence="ECO:0000269|PubMed:17153339,
FT                   ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000444719"
FT   PEPTIDE         37..51
FT                   /note="Conotoxin Reg3b"
FT                   /evidence="ECO:0000269|PubMed:17153339,
FT                   ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000259395"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        37..51
FT                   /evidence="ECO:0000269|PubMed:29283511,
FT                   ECO:0000312|PDB:6BX9"
FT   DISULFID        38..47
FT                   /evidence="ECO:0000269|PubMed:29283511,
FT                   ECO:0000312|PDB:6BX9"
FT   DISULFID        42..50
FT                   /evidence="ECO:0000269|PubMed:29283511,
FT                   ECO:0000312|PDB:6BX9"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AUJ88071.1"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:6BX9"
SQ   SEQUENCE   51 AA;  5689 MW;  8C12DD46FC31C596 CRC64;
     LTAIPLDGDQ PADQPAERME DGESTPNHPW FDPVKRCCTA LCSRYHCLPC C