ID   O26_CONTE               Reviewed;          70 AA.
AC   Q9BPA9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=TxMEKL-P2 {ECO:0000303|PubMed:23031820, ECO:0000312|EMBL:AAG60456.1};
DE   AltName: Full=Conotoxin 6 {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 42-70, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   BROMINATION AT TRP-60.
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, HYDROXYLATION AT
RP   PRO-49, AND BROMINATION AT TRP-59 AND TRP-60.
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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP   DUCT, AND BROMINATION AT TRP-59 AND TRP-60.
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. All three forms are
CC       mostly present in part 5 of venom duct (distal part near the pharynx)
CC       and less abundantly present in part 4. {ECO:0000305|PubMed:19380747,
CC       ECO:0000305|PubMed:23031820}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:P0C834}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- PTM: Contains 3 disulfide bonds. {ECO:0000269|PubMed:19380747}.
CC   -!- PTM: Exists in 5 different forms, depending on bromination and
CC       hydroxylation. Form P2 does not contain brominated tryptophan
CC       (PubMed:23031820), form P2-WBr has one brominated tryptophan at
CC       position 60 (PubMed:22709442, PubMed:23031820), form P2-2WBr has two
CC       brominated tryptophans at position 59 and 60 (PubMed:23031820), form
CC       hydroxyPro-P2-WBr has a hydroxyproline at position 49 and a brominated
CC       tryptophan at position 59 (PubMed:22709442), and form hydroxyPro-P2-
CC       2WBr has an hydroxyproline at position 49 and two brominated tryptophan
CC       at position 59 and 60 (PubMed:22709442). {ECO:0000269|PubMed:22709442,
CC       ECO:0000269|PubMed:23031820}.
CC   -!- MASS SPECTROMETRY: Mass=3302.092; Mass_error=0.02; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:19380747};
CC   -!- SIMILARITY: Belongs to the conotoxin O2 superfamily. {ECO:0000305}.
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DR   EMBL; AF215028; AAG60456.1; -; mRNA.
DR   AlphaFoldDB; Q9BPA9; -.
DR   SMR; Q9BPA9; -.
DR   ConoServer; 715; TxMEKL-P2 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   Bromination; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..41
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000371265"
FT   PEPTIDE         42..70
FT                   /note="TxMEKL-P2"
FT                   /evidence="ECO:0000269|PubMed:19380747"
FT                   /id="PRO_0000371266"
FT   MOD_RES         49
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   MOD_RES         59
FT                   /note="6'-bromotryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442,
FT                   ECO:0000269|PubMed:23031820"
FT   MOD_RES         60
FT                   /note="6'-bromotryptophan; partial"
FT                   /evidence="ECO:0000269|PubMed:19380747,
FT                   ECO:0000269|PubMed:22709442, ECO:0000269|PubMed:23031820"
FT   DISULFID        43..57
FT                   /evidence="ECO:0000250|UniProtKB:P0C834"
FT   DISULFID        50..62
FT                   /evidence="ECO:0000250|UniProtKB:P0C834"
FT   DISULFID        56..69
FT                   /evidence="ECO:0000250|UniProtKB:P0C834"
SQ   SEQUENCE   70 AA;  7701 MW;  C7B96B8E5ECE45AF CRC64;
     MEKLTILLLV AAVLTSTQAL IQGGGDERQK AKINFLSRSD RDCRGYDAPC SSGAPCCDWW
     TCSARTNRCF