M3_CONTE
ID M3_CONTE Reviewed; 68 AA.
AC Q9BPJ7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=TxMMSK-03 {ECO:0000303|PubMed:23031820, ECO:0000312|EMBL:AAG60354.1};
DE AltName: Full=Conotoxin 3 {ECO:0000305};
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 PROTEIN SEQUENCE OF 53-68, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP HYDROXYLATION AT PRO-65.
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, TISSUE SPECIFICITY, POSITION IN VENOM
RP DUCT, AND HYDROXYLATION AT PRO-65.
RC TISSUE=Venom;
RX PubMed=23031820; DOI=10.1016/j.toxicon.2012.09.013;
RA Dobson R., Collodoro M., Gilles N., Turtoi A., De Pauw E., Quinton L.;
RT "Secretion and maturation of conotoxins in the venom ducts of Conus
RT textile.";
RL Toxicon 60:1370-1379(2012).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. Both hydroxylated and
CC non-hydroxylated forms are mostly and only present in part 2 (proximal
CC of the venom bulb) of the venom duct, respectively.
CC {ECO:0000305|PubMed:19380747, ECO:0000305|PubMed:23031820}.
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: Contains 3 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC -!- MASS SPECTROMETRY: Mass=1756.537; 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 EMBL; AF214926; AAG60354.1; -; mRNA.
DR AlphaFoldDB; Q9BPJ7; -.
DR ConoServer; 613; TxMMSK-03 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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hydroxylation; Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..50
FT /evidence="ECO:0000269|PubMed:23031820"
FT /id="PRO_0000371275"
FT PEPTIDE 53..68
FT /note="TxMMSK-03"
FT /evidence="ECO:0000269|PubMed:23031820"
FT /id="PRO_0000371276"
FT MOD_RES 65
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:19380747,
FT ECO:0000269|PubMed:23031820"
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; 7603 MW; 54CA322FFA7CB1B0 CRC64;
MSKLGALLII CLLLFPLTAV PMDGDQPADR PAERMQDDIS FEQHPMFDAT RRCCNAGFCR
FGCTPCCY
