O236E_CONTE
ID O236E_CONTE Reviewed; 73 AA.
AC Q9BPB4;
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(3)-TxVI;
DE AltName: Full=Conotoxin Glu7/Gla(3)-TxVI;
DE AltName: Full=Conotoxin TxMEKL-04111;
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 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-73, MASS SPECTROMETRY,
RP HYDROXYLATION AT PRO-49 AND PRO-54, GAMMA-CARBOXYGLUTAMATION AT GLU-53 AND
RP GLU-60, AND BROMINATION AT TRP-64.
RC TISSUE=Venom, and Venom gland;
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 -!- MASS SPECTROMETRY: Mass=3180.6; Method=MALDI; Note=free 53-Glu.;
CC Evidence={ECO:0000269|PubMed:16817904};
CC -!- MASS SPECTROMETRY: Mass=3225.0; Method=MALDI; Note=53-
CC carboxyglutamate.; Evidence={ECO:0000269|PubMed:16817904};
CC -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR EMBL; AF215021; AAG60449.1; -; mRNA.
DR AlphaFoldDB; Q9BPB4; -.
DR SMR; Q9BPB4; -.
DR ConoServer; 708; Gla(3)-TxVI 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation; Knottin;
KW Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..44
FT /id="PRO_0000404794"
FT PEPTIDE 47..73
FT /note="Conotoxin Gla(3)-TxVI"
FT /id="PRO_0000404795"
FT MOD_RES 49
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:16817904"
FT MOD_RES 53
FT /note="4-carboxyglutamate; partial"
FT /evidence="ECO:0000269|PubMed:16817904"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:16817904"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000269|PubMed:16817904"
FT MOD_RES 64
FT /note="6'-bromotryptophan"
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..71
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="A -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="F -> L (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="NG -> GN (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 73 AA; 8363 MW; 3EAD8ECF53A2C912 CRC64;
MQKLIILLLV AAVLMSAQAV LQEKRPKEKI KFLSKRKTDA EKQQKRLCPD YTEPCSHAHE
CCSWNCYNGH CTG
