ID   CA4A_CONPR              Reviewed;          18 AA.
AC   P0C1W9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Alpha-conotoxin PeIVA;
OS   Conus pergrandis (Grand cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Embrikena.
OX   NCBI_TaxID=330676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SYNTHESIS, 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).
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 fetal (alpha-1/beta-
CC       1/gamma/delta subunits) subtype (IC(50)=<5 nM) of the receptor than for
CC       the adult (alpha-1/beta-1/epsilon/delta) subtype (IC(50)=4000 nM). It
CC       blocks the elicited currents completely and dissociates very slowly
CC       from the fetal muscle receptor. {ECO:0000269|PubMed:16430227}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is IV (CC-C-C-C-C).
CC   -!- PTM: Contains 3 disulfide bonds (By similarity). They are not added,
CC       since framework IV presents two different connectivities (I-V, II-III,
CC       IV-VI and I-III, II-V, IV-VI). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C1W9; -.
DR   ConoServer; 1689; PeIVA.
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.
PE   3: Inferred from homology;
KW   Acetylcholine receptor inhibiting toxin; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Neurotoxin; Postsynaptic neurotoxin; Secreted;
KW   Toxin.
FT   PEPTIDE         1..18
FT                   /note="Alpha-conotoxin PeIVA"
FT                   /id="PRO_0000249798"
FT   MOD_RES         5
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   18 AA;  1766 MW;  8D1CC6A4F7119C7E CRC64;
     CCGVPNAACH PCVCTGKC