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CJEA_CONPO
ID   CJEA_CONPO              Reviewed;          76 AA.
AC   Q0N4U8;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Alpha/kappa-conotoxin pl14a;
DE   Flags: Precursor;
OS   Conus planorbis (Planorbis cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Strategoconus.
OX   NCBI_TaxID=97183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 40-64, SYNTHESIS OF 40-64,
RP   MASS SPECTROMETRY, AMIDATION AT ARG-64, DISULFIDE BONDS, AND STRUCTURE BY
RP   NMR OF 40-64.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=16819832; DOI=10.1021/bi060263r;
RA   Imperial J.S., Bansal P.S., Alewood P.F., Daly N.L., Craik D.J.,
RA   Sporning A., Terlau H., Lopez-Vera E., Bandyopadhyay P.K., Olivera B.M.;
RT   "A novel conotoxin inhibitor of Kv1.6 channel and nAChR subtypes defines a
RT   new superfamily of conotoxins.";
RL   Biochemistry 45:8331-8340(2006).
CC   -!- FUNCTION: Highly inhibits both nicotinic acetylcholine receptors
CC       (neuronal (IC(50)=8.7 uM for alpha-3/beta-4) and neuromuscular
CC       (IC(50)=0.54 uM for alpha-1/beta-1/epsilon/delta) subtypes) and the
CC       voltage-gated potassium channel Kv1.6/KCNA6 subtype (IC(50)=1.59 uM).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is XIV (C-C-C-C).
CC   -!- MASS SPECTROMETRY: Mass=2909.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16819832};
CC   -!- MISCELLANEOUS: No or very small inhibition is observed on Kv1.1/KCNA1,
CC       Kv1.2/KCNA2, Kv1.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5 and Nav1.2/SCN2A.
CC       {ECO:0000305|PubMed:16819832}.
CC   -!- SIMILARITY: Belongs to the conotoxin J superfamily. {ECO:0000305}.
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DR   EMBL; DQ447640; ABE27006.1; -; mRNA.
DR   PDB; 2FQC; NMR; -; A=40-64.
DR   PDB; 2NAV; NMR; -; A=53-64.
DR   PDB; 2NAW; NMR; -; A=54-64.
DR   PDBsum; 2FQC; -.
DR   PDBsum; 2NAV; -.
DR   PDBsum; 2NAW; -.
DR   AlphaFoldDB; Q0N4U8; -.
DR   BMRB; Q0N4U8; -.
DR   SMR; Q0N4U8; -.
DR   ConoServer; 1183; PlXIVA precursor.
DR   EvolutionaryTrace; Q0N4U8; -.
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:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Postsynaptic neurotoxin; Potassium channel impairing toxin;
KW   Secreted; Signal; Toxin; Voltage-gated potassium channel impairing toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..39
FT                   /evidence="ECO:0000269|PubMed:16819832"
FT                   /id="PRO_0000260006"
FT   PEPTIDE         40..64
FT                   /note="Alpha/kappa-conotoxin pl14a"
FT                   /id="PRO_0000260007"
FT   PROPEP          65..76
FT                   /id="PRO_0000260008"
FT   MOD_RES         64
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:16819832"
FT   DISULFID        46..61
FT                   /evidence="ECO:0000269|PubMed:16819832"
FT   DISULFID        50..63
FT                   /evidence="ECO:0000269|PubMed:16819832"
FT   HELIX           44..52
FT                   /evidence="ECO:0007829|PDB:2FQC"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:2FQC"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:2FQC"
SQ   SEQUENCE   76 AA;  8298 MW;  3664513E79382249 CRC64;
     MPSVRSVTCC CLLWMMFSVQ LVTPGSPGTA QLSGHRTARF PRPRICNLAC RAGIGHKYPF
     CHCRGKRDAV SSSMAV
 
 
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