CM3CD_CONRE
ID CM3CD_CONRE Reviewed; 15 AA.
AC P85022;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 22-APR-2020, entry version 29.
DE RecName: Full=Conotoxin Reg12d {ECO:0000303|PubMed:17153339};
DE AltName: Full=Reg12k {ECO:0000305};
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, AND 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).
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 -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR ConoServer; 1488; Reg12k.
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 Direct protein sequencing; Disulfide bond; Hydroxylation; Secreted; Toxin.
FT PEPTIDE 1..15
FT /note="Conotoxin Reg12d"
FT /evidence="ECO:0000269|PubMed:17153339"
FT /id="PRO_0000259396"
FT MOD_RES 11
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:17153339"
FT DISULFID 2..12
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 3..10
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT DISULFID 8..13
FT /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ SEQUENCE 15 AA; 1631 MW; 9D18097BCCB37609 CRC64;
KCCMRPICTC PCCIG