ID   CM3A_CONPI              Reviewed;          15 AA.
AC   P0CH15;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   23-FEB-2022, entry version 20.
DE   RecName: Full=Conotoxin pr3a {ECO:0000303|PubMed:20570703};
OS   Conus parius (Cone snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Phasmoconus.
OX   NCBI_TaxID=505247;
RN   [1]
RP   PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=20570703; DOI=10.1016/j.peptides.2010.05.020;
RA   Jimenez E.C., Olivera B.M.;
RT   "Divergent M- and O-superfamily peptides from venom of fish-hunting Conus
RT   parius.";
RL   Peptides 31:1678-1683(2010).
CC   -!- FUNCTION: Probable neurotoxin with unknown target (Probable). Possibly
CC       targets ion channels (Probable). In vivo, intraperitoneal injection
CC       into fish provokes paralysis after 5 minutes (PubMed:20570703).
CC       {ECO:0000269|PubMed:20570703, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20570703}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:20570703}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       2 branch, since 2 residues stand between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- PTM: Both Pro-5 and Pro-12 are not hydroxylated, and Tyr-15 is not
CC       amidated. {ECO:0000305|PubMed:20570703}.
CC   -!- MASS SPECTROMETRY: Mass=1692.4; Method=MALDI; Note=Monoisotopic mass.;
CC       Evidence={ECO:0000269|PubMed:20570703};
CC   -!- MISCELLANEOUS: Authors confirmed the assignment of this toxin to the M
CC       superfamily by cDNA sequencing.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW   Neurotoxin; Secreted; Toxin.
FT   PEPTIDE         1..15
FT                   /note="Conotoxin pr3a"
FT                   /evidence="ECO:0000269|PubMed:20570703"
FT                   /id="PRO_0000397113"
FT   DISULFID        1..14
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        2..10
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
FT   DISULFID        6..13
FT                   /evidence="ECO:0000250|UniProtKB:P0CI24"
SQ   SEQUENCE   15 AA;  1699 MW;  D3D374F4F7FA65F6 CRC64;
     CCNWPCSFGC IPCCY