COCA_CONCL
ID COCA_CONCL Reviewed; 84 AA.
AC A6YR42; P0DJC1;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Mu-conotoxin-like Cal 12.2a {ECO:0000303|PubMed:21147978};
DE AltName: Full=Conotoxin CalTx 12.2.1A;
DE AltName: Full=Conotoxin Cl12a {ECO:0000303|PubMed:20363338};
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 [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).
RN [2]
RP PROTEIN SEQUENCE OF 43-84, AND HYDROXYLATION AT PRO-48.
RC TISSUE=Venom;
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).
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 -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; EF644196; ABR92966.1; -; mRNA.
DR AlphaFoldDB; A6YR42; -.
DR ConoServer; 815; Cal12.2a 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 1: Evidence at protein level;
KW Bromination; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..42
FT /evidence="ECO:0000250"
FT /id="PRO_0000392279"
FT PEPTIDE 43..84
FT /note="Mu-conotoxin-like Cal 12.2a"
FT /id="PRO_0000392280"
FT MOD_RES 48
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:20363338"
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"
FT DISULFID 45..57
FT /evidence="ECO:0000305"
FT DISULFID 52..65
FT /evidence="ECO:0000250"
FT DISULFID 59..70
FT /evidence="ECO:0000250"
FT DISULFID 64..76
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 9049 MW; E1728EC51EC90A48 CRC64;
MKLTCVLVVL LLVLPFGDLI TTSNTEDNKR GATPWQNSLK ARGVCSTPEG SCVHNGCICQ
NAPCCHPSGC NWANVCPGFL WDKN
