ID   M3C_CONTE               Reviewed;          65 AA.
AC   P58846;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Conotoxin tx3c {ECO:0000303|PubMed:15924437};
DE   AltName: Full=Textile scratcher peptide {ECO:0000303|Ref.3};
DE   AltName: Full=Tx3.4 {ECO:0000303|PubMed:15924437};
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 53-64, SUBCELLULAR
RP   LOCATION, DISULFIDE BONDS, MASS SPECTROMETRY, HYDROXYLATION AT PRO-62, AND
RP   AMIDATION AT CYS-64.
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   PROTEIN SEQUENCE OF 53-64, SUBCELLULAR LOCATION, MASS SPECTROMETRY,
RP   DISULFIDE BONDS, HYDROXYLATION AT PRO-62, AND AMIDATION AT CYS-64.
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   PROTEIN SEQUENCE OF 53-64, FUNCTION, AND BIOASSAY.
RA   Ramilo C.A.;
RL   Thesis (1986), University of Manila, Philippines.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, HYDROXYLATION AT
RP   PRO-62, AND AMIDATION AT CYS-64.
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: Causes scratching in mice. {ECO:0000269|Ref.3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15924437,
CC       ECO:0000269|PubMed:19380747}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:15924437, ECO:0000305|PubMed:19380747}.
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   -!- PTM: The hydroxylation at Pro-62 is observed in PubMed:15924437,
CC       PubMed:19380747 and PubMed:22709442, and the non-hydroxylation is
CC       described in PubMed:22709442. {ECO:0000269|PubMed:15924437,
CC       ECO:0000269|PubMed:19380747, ECO:0000269|PubMed:22709442}.
CC   -!- MASS SPECTROMETRY: Mass=1305.31; Method=LSI;
CC       Evidence={ECO:0000269|PubMed:15924437};
CC   -!- MASS SPECTROMETRY: Mass=1304.369; Mass_error=0.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P58846; -.
DR   ConoServer; 1396; TxIIIC 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; Hydroxylation; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..50
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000246006"
FT   PEPTIDE         53..64
FT                   /note="Conotoxin tx3c"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000044503"
FT   MOD_RES         62
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:19380747, ECO:0000269|PubMed:22709442"
FT   MOD_RES         64
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:19380747, ECO:0000269|PubMed:22709442"
FT   DISULFID        53..64
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:19380747"
FT   DISULFID        54..60
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:19380747"
FT   DISULFID        57..63
FT                   /evidence="ECO:0000269|PubMed:15924437,
FT                   ECO:0000269|PubMed:19380747"
SQ   SEQUENCE   65 AA;  7171 MW;  DA293BCABCBB1052 CRC64;
     MFKLGVLLTI CLLLFSLNAV PLDGDQPADQ PAERLLDDIS FENNPFYDPA KRCCRTCFGC
     TPCCG