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Mu-conotoxin cal12b (Conotoxin Cal 12.1.1b) (Conotoxin CalTx 12.1.1B)

 COC1B_CONCL             Reviewed;          87 AA.
A6YR21;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 1.
15-MAR-2017, entry version 22.
RecName: Full=Mu-conotoxin cal12b;
AltName: Full=Conotoxin Cal 12.1.1b;
AltName: Full=Conotoxin CalTx 12.1.1B;
Flags: Precursor;
Californiconus californicus (California cone) (Conus californicus).
Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Gastropoda;
Caenogastropoda; Hypsogastropoda; Neogastropoda; Conoidea; Conidae;
Californiconus.
NCBI_TaxID=1736779;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-62, FUNCTION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY,
BROMINATION AT TRP-59; TRP-79; TRP-80 AND TRP-86, AND HYDROXYLATION AT
PRO-65 AND PRO-82.
TISSUE=Venom, and Venom duct;
PubMed=21147978; DOI=10.1242/jeb.046086;
Gilly W.F., Richmond T.A., Duda T.F. Jr., Elliger C., Lebaric Z.,
Schulz J., Bingham J.P., Sweedler J.V.;
"A diverse family of novel peptide toxins from an unusual cone snail,
Conus californicus.";
J. Exp. Biol. 214:147-161(2011).
-!- FUNCTION: Mu-conotoxins block voltage-gated sodium channels. This
toxin reversibly blocks voltage-gated sodium channel in
cephalopods (tested on squid giant-fiber-lobe neurons) with an
inhibitor constant (Ki) of 15 nmol/l, with no alteration in the
voltage dependence of sodium conductance or on the kinetics of
inactivation. Has no effect on sodium channels of the two
gastropod S.luhuanus and A.californica (which are not natural
prey). {ECO:0000269|PubMed:21147978}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21147978}.
-!- TISSUE SPECIFICITY: Expressed by the venom duct.
{ECO:0000269|PubMed:21147978}.
-!- DOMAIN: The cysteine framework is XII (C-C-C-C-CC-C-C).
-!- MASS SPECTROMETRY: Mass=5194; Method=MALDI; Range=43-87;
Evidence={ECO:0000269|PubMed:21147978};
-!- SIMILARITY: Belongs to the conotoxin O1 superfamily.
{ECO:0000305}.
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EMBL; EF644175; ABR92945.1; -; mRNA.
SMR; A6YR21; -.
ConoServer; 794; Cal12.1.1b precursor.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:InterPro.
InterPro; IPR004214; Conotoxin.
Pfam; PF02950; Conotoxin; 1.
1: Evidence at protein level;
Bromination; Direct protein sequencing; Disulfide bond;
Gamma-carboxyglutamic acid; Hydroxylation;
Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 42 {ECO:0000305|PubMed:21147978}.
/FTId=PRO_0000392264.
PEPTIDE 43 87 Mu-conotoxin cal12b.
/FTId=PRO_0000392265.
MOD_RES 59 59 6'-bromotryptophan.
{ECO:0000269|PubMed:21147978}.
MOD_RES 65 65 4-hydroxyproline.
{ECO:0000269|PubMed:21147978}.
MOD_RES 79 79 6'-bromotryptophan.
{ECO:0000269|PubMed:21147978}.
MOD_RES 80 80 6'-bromotryptophan.
{ECO:0000269|PubMed:21147978}.
MOD_RES 82 82 4-hydroxyproline.
{ECO:0000269|PubMed:21147978}.
MOD_RES 86 86 6'-bromotryptophan.
{ECO:0000269|PubMed:21147978}.
DISULFID 45 58 {ECO:0000305}.
DISULFID 53 70 {ECO:0000250}.
DISULFID 60 75 {ECO:0000250}.
DISULFID 69 81 {ECO:0000250}.
SEQUENCE 87 AA; 9720 MW; DAC89CC6F30C6C6F CRC64;
MKLTCVLVVL LLLLPYGDLI TNNYIRGAAR KVTPWRRNLK TRDVCDSLVG GHCIHNGCWC
DQDAPHGNCC DTDGCTAAWW CPGTKWD


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