ID   COCD_CONCL              Reviewed;          84 AA.
AC   A7LI92; D6C4I1;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Mu-conotoxin-like Cal 12.2d;
DE   AltName: Full=Conotoxin CalTx 12.2.1D;
DE   AltName: Full=Conotoxin Cl12.1;
DE   Flags: Precursor;
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 [GENOMIC DNA].
RX   PubMed=20363338; DOI=10.1016/j.ympev.2010.03.029;
RA   Biggs J.S., Watkins M., Puillandre N., Ownby J.P., Lopez-Vera E.,
RA   Christensen S., Moreno K.J., Bernaldez J., Licea-Navarro A., Corneli P.S.,
RA   Olivera B.M.;
RT   "Evolution of Conus peptide toxins: analysis of Conus californicus Reeve,
RT   1844.";
RL   Mol. Phylogenet. Evol. 56:1-12(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-84.
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   -!- PTM: Contains 4 disulfide bonds. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; FJ959123; ADB93093.1; -; Genomic_DNA.
DR   EMBL; EU022530; ABS59787.1; -; mRNA.
DR   AlphaFoldDB; A7LI92; -.
DR   ConoServer; 4009; Cal12.2d precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   2: Evidence at transcript level;
KW   Bromination; Disulfide bond; Hydroxylation; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..42
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000392285"
FT   PEPTIDE         43..84
FT                   /note="Mu-conotoxin-like Cal 12.2d"
FT                   /id="PRO_0000392286"
FT   MOD_RES         72
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         77
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         81
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   84 AA;  9023 MW;  E16EE2B51EC90A48 CRC64;
     MKLTCVLVVL LLVLPFGDLI TTSNTEDNKR GATPWQNSLK ARGVCSTPEG SCVHNGCICQ
     NAPCCHASGC NWANVCPGFL WDKN