ID   CM3H_CONRE              Reviewed;          52 AA.
AC   A0A2I6EDL4;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Conotoxin reg3h {ECO:0000303|PubMed:29283511};
DE   AltName: Full=Reg3.3 {ECO:0000303|PubMed:29283511};
DE            Short=Rg3.3 {ECO:0000312|EMBL:AUJ88061.1};
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 34-52, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-38; PRO-48 AND PRO-51, AND
RP   AMIDATION AT ASN-52.
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       1 branch, since 1 residue stands between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2111.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29283511};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; MF588937; AUJ88061.1; -; mRNA.
DR   AlphaFoldDB; A0A2I6EDL4; -.
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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          <1..1
FT                   /evidence="ECO:0000305"
FT   PROPEP          2..33
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000444764"
FT   PEPTIDE         34..52
FT                   /note="Conotoxin reg3h"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000444765"
FT   MOD_RES         38
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         48
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         51
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   MOD_RES         52
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT   DISULFID        35..49
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        36..47
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        41..50
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:AUJ88061.1"
FT   NON_TER         52
FT                   /evidence="ECO:0000312|EMBL:AUJ88061.1"
SQ   SEQUENCE   52 AA;  5747 MW;  C8321FF1DF2A2AD4 CRC64;
     ALPLDGDQPA DQPAERMQDI SPELNPLFHP VKRGCCSPWN CIQLRACPCC PN