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