ID   M01_CONTE               Reviewed;          67 AA.
AC   Q9BPJ1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Conotoxin TxMMSK-01;
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=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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
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.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; AF214933; AAG60361.1; -; mRNA.
DR   AlphaFoldDB; Q9BPJ1; -.
DR   ConoServer; 620; TxMMSK-01 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   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW   Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..53
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000315535"
FT   PEPTIDE         54..66
FT                   /note="Conotoxin TxMMSK-01"
FT                   /id="PRO_0000315536"
FT   MOD_RES         64
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         66
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..66
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        55..62
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        59..65
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   67 AA;  7364 MW;  EF18D7A9F4ECAEE5 CRC64;
     MMSKLGVLLI TCLLLFPLTA VPLDGDQPAD QPAERLQDDI SSENHPFFDP VKRCCRLLCL
     SCNPCCG