CA16_CONPL
ID CA16_CONPL Reviewed; 58 AA.
AC P0C8V0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Alpha-conotoxin-like Pu1.6;
DE Flags: Precursor;
OS Conus pulicarius (Flea-bitten cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus.
OX NCBI_TaxID=93154;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RX PubMed=18625510; DOI=10.1016/j.toxicon.2008.05.004;
RA Biggs J.S., Olivera B.M., Kantor Y.I.;
RT "Alpha-conopeptides specifically expressed in the salivary gland of Conus
RT pulicarius.";
RL Toxicon 52:101-105(2008).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (By
CC similarity). Has possibly a distinct nAChR binding mode from other
CC alpha-conotoxins, due to a different three residue motif (lacks the
CC Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18625510}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:18625510}.
CC -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C8V0; -.
DR ConoServer; 2867; Pu1.6 precursor.
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 3: Inferred from homology;
KW Acetylcholine receptor inhibiting toxin; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..35
FT /evidence="ECO:0000255"
FT /id="PRO_0000366068"
FT PEPTIDE 36..58
FT /note="Alpha-conotoxin-like Pu1.6"
FT /id="PRO_0000366069"
FT REGION 46..48
FT /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT potent interaction with nAChR"
FT /evidence="ECO:0000305"
FT DISULFID 44..50
FT /evidence="ECO:0000250|UniProtKB:P56636"
FT DISULFID 45..58
FT /evidence="ECO:0000250|UniProtKB:P56636"
SQ SEQUENCE 58 AA; 6863 MW; F3255FA7C1D6990C CRC64;
MFTVFLLVVL VTTVVFSTSD HRPASNHENR RASKRISEMT WEECCTNPVC RQHYMHYC