ID   O226A_CONTE             Reviewed;          72 AA.
AC   Q9BPB1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Conotoxin Gla(2)-TxVI/A;
DE   AltName: Full=Conotoxin TxMEKL-043;
DE   Flags: Precursor;
OS   Conus textile (Cloth-of-gold cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX   NCBI_TaxID=6494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=11158371; DOI=10.1093/oxfordjournals.molbev.a003786;
RA   Conticello S.G., Gilad Y., Avidan N., Ben-Asher E., Levy Z., Fainzilber M.;
RT   "Mechanisms for evolving hypervariability: the case of conopeptides.";
RL   Mol. Biol. Evol. 18:120-131(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 47-71, MASS SPECTROMETRY, HYDROXYLATION AT PRO-58,
RP   GAMMA-CARBOXYGLUTAMATION AT GLU-56, BROMINATION, AND AMIDATION AT SER-71.
RC   TISSUE=Venom;
RX   PubMed=16817904; DOI=10.1111/j.1742-4658.2006.05294.x;
RA   Czerwiec E., Kalume D.E., Roepstorff P., Hambe B., Furie B., Furie B.C.,
RA   Stenflo J.;
RT   "Novel gamma-carboxyglutamic acid-containing peptides from the venom of
RT   Conus textile.";
RL   FEBS J. 273:2779-2788(2006).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- PTM: Brominated at one of the Trp residues.
CC       {ECO:0000269|PubMed:16817904}.
CC   -!- MASS SPECTROMETRY: Mass=2966.75; Method=MALDI; Note=TxVI/A.;
CC       Evidence={ECO:0000269|PubMed:16817904};
CC   -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR   EMBL; AF215024; AAG60452.1; -; mRNA.
DR   AlphaFoldDB; Q9BPB1; -.
DR   ConoServer; 711; Gla(2)-TxVI/A 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   Amidation; Bromination; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW   Hydroxylation; Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..44
FT                   /id="PRO_0000404788"
FT   PEPTIDE         47..71
FT                   /note="Conotoxin Gla(2)-TxVI/A"
FT                   /id="PRO_0000404789"
FT   MOD_RES         56
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:16817904"
FT   MOD_RES         58
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:16817904"
FT   MOD_RES         71
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000269|PubMed:16817904"
FT   DISULFID        48..62
FT                   /evidence="ECO:0000250"
FT   DISULFID        55..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..70
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   72 AA;  8194 MW;  4838370754D93B63 CRC64;
     MQKLIILLLV AAVLMSTQAL FQEKRPMKKI DFLSKGKTDA EKQQKRSCSD DWQYCESPTD
     CCSWDCDVVC SG