ID   O26G_CONTE              Reviewed;          76 AA.
AC   P58922; Q3YEG1; Q9BPB8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Conotoxin Gla(1)-TxVI;
DE   AltName: Full=TeA52;
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].
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].
RA   Luo S., Zhangsun D., Zhang B., Lin Q.;
RT   "Novel O-superfamily conotoxins, and their coding polynucleotides and
RT   use.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-76, BROMINATION AT
RP   TRP-48 AND TRP-76, HYDROXYLATION AT PRO-61, GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-50; GLU-63; GLU-67 AND GLU-70, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN   [4]
RP   PROTEIN SEQUENCE OF 46-76, BROMINATION AT TRP-48 AND TRP-76, HYDROXYLATION
RP   AT PRO-61, GAMMA-CARBOXYGLUTAMATION AT GLU-50; GLU-63; GLU-67 AND GLU-70,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10679974;
RX   DOI=10.1002/(sici)1096-9888(200002)35:2<145::aid-jms922>3.0.co;2-i;
RA   Kalume D.E., Stenflo J.P., Czerwiec E., Hambe B., Furie B.C., Furie B.,
RA   Roepstorff P.;
RT   "Structure determination of two conotoxins from Conus textile by a
RT   combination of matrix-assisted laser desorption/ionization time-of-flight
RT   and electrospray ionization mass spectrometry and biochemical methods.";
RL   J. Mass Spectrom. 35:145-156(2000).
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:0000305}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- MASS SPECTROMETRY: Mass=3672.78; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10679974};
CC   -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR   EMBL; AF215016; AAG60444.1; -; mRNA.
DR   EMBL; DQ141152; AAZ83753.1; -; mRNA.
DR   AlphaFoldDB; P58922; -.
DR   ConoServer; 1511; Gla(1)-TxVI.
DR   ConoServer; 703; Gla(1)-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; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Knottin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..45
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT                   /id="PRO_0000392712"
FT   PEPTIDE         46..76
FT                   /note="Conotoxin Gla(1)-TxVI"
FT                   /id="PRO_0000044879"
FT   MOD_RES         48
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         50
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         61
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         63
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         67
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         70
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   MOD_RES         76
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:10679974,
FT                   ECO:0000269|PubMed:16817904"
FT   DISULFID        51..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..73
FT                   /evidence="ECO:0000250"
FT   CONFLICT        34
FT                   /note="N -> K (in Ref. 2; AAZ83753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   76 AA;  8409 MW;  F15986F373CA134D CRC64;
     MEKLTILLLV AAVLMSTQAL VERAGENHSK ENINFLLKRK RAADRGMWGE CKDGLTTCLA
     PSECCSEDCE GSCTMW