ID   M3B_CONTE               Reviewed;          68 AA.
AC   P0C1N8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Conotoxin tx3b;
DE   AltName: Full=Tx3.3;
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], PROTEIN SEQUENCE OF 53-67, MASS SPECTROMETRY,
RP   AMIDATION AT CYS-67, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=15924437; DOI=10.1021/bi047541b;
RA   Corpuz G.P., Jacobsen R.B., Jimenez E.C., Watkins M., Walker C.,
RA   Colledge C., Garrett J.E., McDougal O., Li W., Gray W.R., Hillyard D.R.,
RA   Rivier J., McIntosh J.M., Cruz L.J., Olivera B.M.;
RT   "Definition of the M-conotoxin superfamily: characterization of novel
RT   peptides from molluscivorous Conus venoms.";
RL   Biochemistry 44:8176-8186(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, OXIDATION AT
RP   MET-61, AND AMIDATION AT CYS-67.
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   -!- FUNCTION: Intracranial injection into mice causes scratching,
CC       hyperactivity and circular motion.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15924437}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:15924437}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1521.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15924437};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1N8; -.
DR   ConoServer; 1401; TxIIIB 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; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Neurotoxin; Oxidation; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..52
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000246055"
FT   PEPTIDE         53..67
FT                   /note="Conotoxin tx3b"
FT                   /evidence="ECO:0000269|PubMed:15924437"
FT                   /id="PRO_0000246056"
FT   MOD_RES         61
FT                   /note="Methionine sulfoxide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   MOD_RES         67
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:22709442"
FT   DISULFID        53..67
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        54..63
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        59..66
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   68 AA;  7379 MW;  B96D87E38C18C100 CRC64;
     MSKLGALLTI CLLLFSLTAV PLDGDQHADQ PAQRLQDRIP TEDHPLFDPN KRCCPPVACN
     MGCKPCCG