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   24-JAN-2024, entry version 89.
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-1-
CC       gamma-delta (CHRNA1-CHRNB1-CHRNG-CHRND) subunits) (IC(50)=2.3 nM) of
CC       the receptor than for the fetal subtype (alpha-1-beta-1-epsilon-delta
CC       (CHRNA1-CHRNB1-CHRND-CHRNE) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//