COC1B_CONCL
ID COC1B_CONCL Reviewed; 87 AA.
AC A6YR21;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Mu-conotoxin cal12b;
DE AltName: Full=Conotoxin Cal 12.1.1b;
DE AltName: Full=Conotoxin CalTx 12.1.1B;
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], PROTEIN SEQUENCE OF 43-62, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, BROMINATION AT
RP TRP-59; TRP-79; TRP-80 AND TRP-86, AND HYDROXYLATION AT PRO-65 AND PRO-82.
RC TISSUE=Venom, and 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 (tested
CC on squid giant-fiber-lobe neurons) with an inhibitor constant (Ki) of
CC 15 nmol/l, with no alteration in the voltage dependence of sodium
CC conductance or on the kinetics of inactivation. Has no effect on sodium
CC channels of the two gastropod S.luhuanus and A.californica (which are
CC not natural prey). {ECO:0000269|PubMed:21147978}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21147978}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000269|PubMed:21147978}.
CC -!- DOMAIN: The cysteine framework is XII (C-C-C-C-CC-C-C).
CC -!- MASS SPECTROMETRY: Mass=5194; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:21147978};
CC -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR EMBL; EF644175; ABR92945.1; -; mRNA.
DR AlphaFoldDB; A6YR21; -.
DR ConoServer; 794; Cal12.1.1b 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:0000305|PubMed:21147978"
FT /id="PRO_0000392264"
FT PEPTIDE 43..87
FT /note="Mu-conotoxin cal12b"
FT /id="PRO_0000392265"
FT MOD_RES 59
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:21147978"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21147978"
FT MOD_RES 79
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:21147978"
FT MOD_RES 80
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:21147978"
FT MOD_RES 82
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:21147978"
FT MOD_RES 86
FT /note="6'-bromotryptophan"
FT /evidence="ECO:0000269|PubMed:21147978"
FT DISULFID 45..58
FT /evidence="ECO:0000305"
FT DISULFID 53..70
FT /evidence="ECO:0000250"
FT DISULFID 60..75
FT /evidence="ECO:0000250"
FT DISULFID 69..81
FT /evidence="ECO:0000250"
SQ SEQUENCE 87 AA; 9720 MW; DAC89CC6F30C6C6F CRC64;
MKLTCVLVVL LLLLPYGDLI TNNYIRGAAR KVTPWRRNLK TRDVCDSLVG GHCIHNGCWC
DQDAPHGNCC DTDGCTAAWW CPGTKWD
