CA4A_CONPU
ID CA4A_CONPU Reviewed; 68 AA.
AC P55963; E2DEK7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Alpha-conotoxin PIVA {ECO:0000305};
DE AltName: Full=Alpha-A-conotoxin PIVA {ECO:0000303|PubMed:7673220};
DE Flags: Precursor;
OS Conus purpurascens (Purple cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Chelyconus.
OX NCBI_TaxID=41690;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Puillandre N., Olivera B.M.;
RT "Superfamily, scaffold and functions: review and phylogenetic
RT classification of conotoxins.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 42-66, HYDROXYLATION AT PRO-48; PRO-54 AND PRO-61,
RP AMIDATION AT GLN-66, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7673220; DOI=10.1074/jbc.270.38.22361;
RA Hopkins C., Grilley M., Miller C., Shon K.-J., Cruz L.J., Gray W.R.,
RA Dykert J., Rivier J.E., Yoshikami D., Olivera B.M.;
RT "A new family of Conus peptides targeted to the nicotinic acetylcholine
RT receptor.";
RL J. Biol. Chem. 270:22361-22367(1995).
RN [3]
RP SYNTHESIS OF 42-66, AND FUNCTION.
RX PubMed=16430227; DOI=10.1021/bi052016d;
RA Teichert R.W., Lopez-Vera E., Gulyas J., Watkins M., Rivier J.,
RA Olivera B.M.;
RT "Definition and characterization of the short alphaA-conotoxins: a single
RT residue determines dissociation kinetics from the fetal muscle nicotinic
RT acetylcholine receptor.";
RL Biochemistry 45:1304-1312(2006).
RN [4]
RP STRUCTURE BY NMR OF 42-66, AND DISULFIDE BONDS.
RX PubMed=9048550; DOI=10.1021/bi962301k;
RA Han K.-H., Hwang K.-J., Kim S.-M., Kim S.-K., Gray W.R., Olivera B.M.,
RA Rivier J.E., Shon K.-J.;
RT "NMR structure determination of a novel conotoxin, [Pro 7,13] alpha A-
RT conotoxin PIVA.";
RL Biochemistry 36:1669-1677(1997).
CC -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to
CC the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
CC This toxin has higher affinity for the adult subtype (alpha-1/beta-
CC 1/gamma/delta subunits) (IC(50)=2.3 nM) of the receptor than for the
CC fetal subtype (alpha-1/beta-1/epsilon/delta subunits) (IC(50)=22 nM).
CC {ECO:0000269|PubMed:16430227}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7673220}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:7673220}.
CC -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR EMBL; GQ981399; ADN79118.1; -; mRNA.
DR PIR; A58647; A58647.
DR PDB; 1P1P; NMR; -; A=42-66.
DR PDBsum; 1P1P; -.
DR AlphaFoldDB; P55963; -.
DR SMR; P55963; -.
DR TCDB; 8.B.32.1.10; the nicotinic acetylcholine receptor-targeting alpha-conotoxin (a-conotoxin) family.
DR ConoServer; 1449; PIVA.
DR ConoServer; 1612; PIVA [Hyp7P,Hyp13P].
DR EvolutionaryTrace; P55963; -.
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 InterPro; IPR012498; Toxin_14.
DR Pfam; PF07829; Toxin_14; 1.
DR Pfam; PF07365; Toxin_8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin; Amidation;
KW Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..41
FT /evidence="ECO:0000269|PubMed:7673220"
FT /id="PRO_0000444204"
FT PEPTIDE 42..66
FT /note="Alpha-conotoxin PIVA"
FT /evidence="ECO:0000269|PubMed:7673220"
FT /id="PRO_0000044466"
FT MOD_RES 48
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:7673220"
FT MOD_RES 54
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:7673220"
FT MOD_RES 61
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7673220"
FT MOD_RES 66
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|PubMed:7673220"
FT DISULFID 43..57
FT /evidence="ECO:0000269|PubMed:7673220,
FT ECO:0000269|PubMed:9048550"
FT DISULFID 44..52
FT /evidence="ECO:0000269|PubMed:7673220,
FT ECO:0000269|PubMed:9048550"
FT DISULFID 55..64
FT /evidence="ECO:0000269|PubMed:7673220,
FT ECO:0000269|PubMed:9048550"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1P1P"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1P1P"
SQ SEQUENCE 68 AA; 7386 MW; 618EA3012F2CB90D CRC64;
MFTVFLLVVL ATTVVSFTSD RASDDRNTND KASRLLSHVV RGCCGSYPNA ACHPCSCKDR
PSYCGQGR