ID   CA43_CONST              Reviewed;          34 AA.
AC   P0C830;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Kappa-conotoxin-like S4.3;
OS   Conus striatus (Striated cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6493;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=16183187; DOI=10.1016/j.biochi.2005.08.001;
RA   Pi C., Liu Y., Peng C., Jiang X., Liu J., Xu B., Yu X., Yu Y., Jiang X.,
RA   Wang L., Dong M., Chen S., Xu A.-L.;
RT   "Analysis of expressed sequence tags from the venom ducts of Conus
RT   striatus: focusing on the expression profile of conotoxins.";
RL   Biochimie 88:131-140(2006).
CC   -!- FUNCTION: Kappa-conotoxins bind and inhibit voltage-gated potassium
CC       channels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC   -!- PTM: Contains 3 disulfide bonds (By similarity). They are not added,
CC       since framework IV presents two different connectivities (I-V, II-III,
CC       IV-VI and I-III, II-V, IV-VI). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0C830; -.
DR   SMR; P0C830; -.
DR   ConoServer; 3547; S4.3.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydroxylation; Ion channel impairing toxin;
KW   Neurotoxin; Potassium channel impairing toxin; Pyrrolidone carboxylic acid;
KW   Secreted; Toxin.
FT   PEPTIDE         1..34
FT                   /note="Kappa-conotoxin-like S4.3"
FT                   /id="PRO_0000345099"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         22
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         32
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        7
FT                   /note="O-linked (HexNAc...) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   34 AA;  3626 MW;  A00F1A67578E9CD6 CRC64;
     QKELVPSKTT TCCGYSPGTM CPSCMCTNTC PPQK