ID   CT13_CONTE              Reviewed;          61 AA.
AC   Q3YEH7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Conotoxin 3 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Conotoxin TeA31 {ECO:0000303|PubMed:16765485};
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=16765485; DOI=10.1016/j.peptides.2006.05.002;
RA   Luo S., Zhangsun D., Zhang B., Chen X., Feng J.;
RT   "Direct cDNA cloning of novel conotoxins of the T-superfamily from Conus
RT   textile.";
RL   Peptides 27:2640-2646(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-61, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   BROMINATION AT TRP-58.
RC   TISSUE=Venom;
RX   PubMed=19380747; DOI=10.1073/pnas.0900745106;
RA   Ueberheide B.M., Fenyo D., Alewood P.F., Chait B.T.;
RT   "Rapid sensitive analysis of cysteine rich peptide venom components.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:6910-6915(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND BROMINATION
RP   AT TRP-58.
RC   TISSUE=Venom;
RX   PubMed=22709442; DOI=10.1021/pr300312h;
RA   Bhatia S., Kil Y.J., Ueberheide B., Chait B.T., Tayo L., Cruz L., Lu B.,
RA   Yates J.R. III, Bern M.;
RT   "Constrained de novo sequencing of conotoxins.";
RL   J. Proteome Res. 11:4191-4200(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:19380747}.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC). {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- PTM: Contains 2 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC   -!- MASS SPECTROMETRY: [Conotoxin TeA31]: Mass=1391.34; Mass_error=0.02;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:19380747};
CC   -!- MASS SPECTROMETRY: [Conotoxin 3]: Mass=1547.443; Mass_error=0.02;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:19380747};
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; DQ141136; AAZ85401.1; -; mRNA.
DR   AlphaFoldDB; Q3YEH7; -.
DR   ConoServer; 1673; TeA31 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Bromination; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..48
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000274090"
FT   PEPTIDE         50..61
FT                   /note="Conotoxin 3"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000371304"
FT   PEPTIDE         51..61
FT                   /note="Conotoxin TeA31"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000274091"
FT   MOD_RES         58
FT                   /note="6'-bromotryptophan"
FT                   /evidence="ECO:0000269|PubMed:19380747,
FT                   ECO:0000269|PubMed:22709442"
SQ   SEQUENCE   61 AA;  6925 MW;  618F8FF5690EBC12 CRC64;
     MRCLPVFVIL LLLIASVPSD AVQLKTKDDM PLPSFNGNAR RTPRMLSNKR ICCYPNVWCC
     D