ID   CA12_CONKI              Reviewed;          37 AA.
AC   D4HRK7;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Alpha-conotoxin-like Kn1.2 {ECO:0000303|PubMed:26948522};
DE   Flags: Precursor; Fragment;
OS   Conus kinoshitai (Kinoshita's cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Afonsoconus.
OX   NCBI_TaxID=376876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=20143226; DOI=10.1007/s00239-010-9321-7;
RA   Puillandre N., Watkins M., Olivera B.M.;
RT   "Evolution of conus peptide genes: duplication and positive selection in
RT   the A-Superfamily.";
RL   J. Mol. Evol. 70:190-202(2010).
RN   [2]
RP   FUNCTION, SYNTHESIS OF 40-55, AND AMIDATION AT CYS-36.
RX   PubMed=26948522; DOI=10.1002/anie.201600297;
RA   Carstens B.B., Berecki G., Daniel J.T., Lee H.S., Jackson K.A., Tae H.S.,
RA   Sadeghi M., Castro J., O'Donnell T., Deiteren A., Brierley S.M.,
RA   Craik D.J., Adams D.J., Clark R.J.;
RT   "Structure-activity studies of cysteine-rich alpha-conotoxins that inhibit
RT   high-voltage-activated calcium channels via GABA(B) receptor activation
RT   reveal a minimal functional motif.";
RL   Angew. Chem. Int. Ed. 55:4692-4696(2016).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC       the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC       similarity). This toxin inhibits high voltage-activated (HVA) calcium
CC       channel currents in rat DRG neurons (13% inhibition at 1 uM toxin)
CC       probably by activating GABA(B) receptors (GABBR1 and/or GABBR2)
CC       (PubMed:26948522). {ECO:0000250|UniProtKB:P0CE73,
CC       ECO:0000269|PubMed:26948522}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/4 pattern.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   EMBL; FJ937349; ACZ37200.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4HRK7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035792; C:host cell postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009958; Conotoxin_a-typ.
DR   Pfam; PF07365; Toxin_8; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Amidation; Disulfide bond;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PROPEP          <1..22
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT                   /id="PRO_0000445675"
FT   PEPTIDE         23..36
FT                   /note="Alpha-conotoxin-like Kn1.2"
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT                   /id="PRO_0000445676"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT   DISULFID        25..31
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT   DISULFID        26..36
FT                   /evidence="ECO:0000305|PubMed:26948522"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ACZ37200.1"
SQ   SEQUENCE   37 AA;  3878 MW;  588D697290E486B6 CRC64;
     ESDGAHAKAR ADKPARSATN RQPGCCNNPA CVKHRCG