O1K2_CONTE
ID O1K2_CONTE Reviewed; 77 AA.
AC P18513;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Conotoxin King-Kong 2 {ECO:0000305};
DE Short=KK-2 {ECO:0000312|EMBL:CAA37379.1};
DE Contains:
DE RecName: Full=Truncated King-Kong 2 {ECO:0000305|PubMed:22709442};
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 IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND AMIDATION AT
RP CYS-76.
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:0000269|PubMed:22709442}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:22709442}.
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; X53285; CAA37379.1; -; mRNA.
DR PIR; S12515; S12515.
DR AlphaFoldDB; P18513; -.
DR SMR; P18513; -.
DR ConoServer; 600; King-Kong 2 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; Disulfide bond; Knottin;
KW Neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /id="PRO_0000034987"
FT PEPTIDE 52..77
FT /note="Conotoxin King-Kong 2"
FT /evidence="ECO:0000269|PubMed:22709442"
FT /id="PRO_0000034988"
FT PEPTIDE 52..76
FT /note="Truncated King-Kong 2"
FT /evidence="ECO:0000269|PubMed:22709442"
FT /id="PRO_0000445113"
FT MOD_RES 76
FT /note="Cysteine amide"
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"
SQ SEQUENCE 77 AA; 8727 MW; EF18DDBEFD44CAB9 CRC64;
MKLTCMMIVA VLFLTAWTFV TADDSGNGLE NLFSKAHHEM KNPEASNLNK RCAPFLHPCT
FFFPNCCNSY CVQFICL