ID   CA1C_CONPU              Reviewed;          14 AA.
AC   C0HLM2;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   23-FEB-2022, entry version 6.
DE   RecName: Full=Alpha-conotoxin PIC {ECO:0000303|PubMed:28917942};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-7,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:28917942};
RX   PubMed=28917942; DOI=10.1016/j.neuropharm.2017.09.020;
RA   Hoggard M.F., Rodriguez A.M., Cano H., Clark E., Tae H.S., Adams D.J.,
RA   Godenschwege T.A., Mari F.;
RT   "In vivo and in vitro testing of native alpha-conotoxins from the injected
RT   venom of Conus purpurascens.";
RL   Neuropharmacology 127:253-259(2017).
CC   -!- FUNCTION: Alpha-conotoxins bind to the nicotinic acetylcholine
CC       receptors (nAChR) and inhibit them. This toxin inhibits rodent (alpha-
CC       1-beta-1-delta-epsilon > alpha-1-beta-1-delta-gamma) and human (alpha-
CC       3-beta-1) nAChRs heterologously expressed in Xenopus oocytes, but has
CC       minimal effect on human alpha-7 nAChRs. Has no effect on the frequency
CC       of responses from the giant fiber (GF)-dorsal longitudinal and GF-tergo
CC       trochanteral muscle pathways in the D.melanogaster GF circuit
CC       (PubMed:28917942). Has possibly a distinct nAChR binding mode from
CC       other alpha-conotoxins, due to a different three residue motif (lacks
CC       the Ser-Xaa-Pro motif) (By similarity). {ECO:0000250|UniProtKB:Q2I2R8,
CC       ECO:0000269|PubMed:28917942}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28917942}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:28917942}.
CC   -!- DOMAIN: The cysteine framework is I (CC-C-C). Alpha4/7 pattern.
CC       {ECO:0000305}.
CC   -!- PTM: A non-hydroxylated version of this conotoxin has been synthesized.
CC       Hydroxylation of Pro-7 seems to increase the inhibition of rodent
CC       alpha-1-beta-1-delta-epsilon and alpha-1-beta-1-delta-gamma nAChRs.
CC       {ECO:0000269|PubMed:28917942}.
CC   -!- MASS SPECTROMETRY: Mass=1460.13; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28917942};
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. {ECO:0000305}.
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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; IDA:UniProtKB.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:2000272; P:negative regulation of signaling receptor activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Hydroxylation; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..14
FT                   /note="Alpha-conotoxin PIC"
FT                   /evidence="ECO:0000269|PubMed:28917942"
FT                   /id="PRO_0000448562"
FT   REGION          5..7
FT                   /note="Lacks the Ser-Xaa-Pro motif that is crucial for
FT                   potent interaction with nAChR"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         7
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:28917942"
SQ   SEQUENCE   14 AA;  1464 MW;  3594F19EE0A362C7 CRC64;
     SGCCKHPACG KNRC