ID   COC2D_CONCL             Reviewed;          45 AA.
AC   A6YR31;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Mu-conotoxin-like Cal 12.1.2d;
DE   AltName: Full=Conotoxin CalTx 12.1.3A;
OS   Californiconus californicus (California cone) (Conus californicus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Californiconus.
OX   NCBI_TaxID=1736779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=21147978; DOI=10.1242/jeb.046086;
RA   Gilly W.F., Richmond T.A., Duda T.F. Jr., Elliger C., Lebaric Z.,
RA   Schulz J., Bingham J.P., Sweedler J.V.;
RT   "A diverse family of novel peptide toxins from an unusual cone snail, Conus
RT   californicus.";
RL   J. Exp. Biol. 214:147-161(2011).
CC   -!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels. This toxin
CC       reversibly blocks voltage-gated sodium channel in cephalopods, with no
CC       alteration in the voltage dependence of sodium conductance or on the
CC       kinetics of inactivation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XII (C-C-C-C-CC-C-C).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF644185; ABR92955.1; -; mRNA.
DR   AlphaFoldDB; A6YR31; -.
DR   ConoServer; 804; Cal12.1.2d.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Bromination; Disulfide bond; Hydroxylation; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..45
FT                   /note="Mu-conotoxin-like Cal 12.1.2d"
FT                   /id="PRO_0000392272"
FT   MOD_RES         17
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         38
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         40
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   DISULFID        3..16
FT                   /evidence="ECO:0000305"
FT   DISULFID        11..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..39
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   45 AA;  4904 MW;  DD404B6923008BEC CRC64;
     DVCDSLVGGR CIHNGCWCER SAPHGNCCNT SGCTARWWCP GTKFD