ID   O16K1_CONTE             Reviewed;          77 AA.
AC   P18512; Q9U649;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Conotoxin King-Kong 1 {ECO:0000305};
DE            Short=KK-1 {ECO:0000312|EMBL:CAA37378.1};
DE   AltName: Full=TxMKLT1-015 {ECO:0000312|EMBL:AAF07978.1};
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=1691090; DOI=10.1002/j.1460-2075.1990.tb08204.x;
RA   Woodward S.R., Cruz L.J., Olivera B.M., Hillyard D.R.;
RT   "Constant and hypervariable regions in conotoxin propeptides.";
RL   EMBO J. 9:1015-1020(1990).
RN   [2]
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND OXIDATION AT
RP   MET-61.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:1691090}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:1691090}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000250|UniProtKB:Q26443}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; X53284; CAA37378.1; -; mRNA.
DR   EMBL; AF193267; AAF07978.1; -; mRNA.
DR   PIR; S12514; S12514.
DR   AlphaFoldDB; P18512; -.
DR   ConoServer; 599; King-Kong 1 precursor.
DR   ConoServer; 1100; TxMKLT1-015 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; Disulfide bond; Knottin; Neurotoxin;
KW   Oxidation; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000034985"
FT   PEPTIDE         52..77
FT                   /note="Conotoxin King-Kong 1"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT                   /id="PRO_0000034986"
FT   MOD_RES         61
FT                   /note="Methionine sulfoxide; partial"
FT                   /evidence="ECO:0000269|PubMed:22709442"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   DISULFID        66..76
FT                   /evidence="ECO:0000250|UniProtKB:Q26443"
FT   CONFLICT        60
FT                   /note="D -> E (in Ref. 1; CAA37378)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  8676 MW;  A3EB902AC834E5A4 CRC64;
     MKLTCMMIVA VLFLTAWTFA TADDSSNGLE NLFSKAHHEM KNPEASKLNK RCIEQFDPCD
     MIRHTCCVGV CFLMACI