ID   COP3_CONPU              Reviewed;         178 AA.
AC   A0A5C1ZW08;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Conodipine-P3 {ECO:0000303|PubMed:30765458};
DE            Short=Cdpi-P3 {ECO:0000303|PubMed:30765458};
DE            EC=3.1.1.4 {ECO:0000250|UniProtKB:A0A5C2A2T2};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000305};
DE   AltName: Full=Phospholipase A2 {ECO:0000305};
DE            Short=PLA2 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Conodipine-P3 alpha subunit {ECO:0000303|PubMed:30765458};
DE   Contains:
DE     RecName: Full=Conodipine-P3 beta subunit {ECO:0000303|PubMed:30765458};
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 {ECO:0000312|EMBL:QEO32924.1};
RN   [1] {ECO:0000312|EMBL:QEO32924.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-73, MASS SPECTROMETRY,
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND HYDROXYLATION AT
RP   PRO-42 AND PRO-49.
RX   PubMed=30765458; DOI=10.1074/mcp.ra118.000972;
RA   Moeller C., Davis W.C., Clark E., DeCaprio A., Mari F.;
RT   "Conodipine-P1-3, the First Phospholipases A2 Characterized from Injected
RT   Cone Snail Venom.";
RL   Mol. Cell. Proteomics 18:876-891(2019).
CC   -!- FUNCTION: Catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:A0A5C2A2T2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC         Evidence={ECO:0000250|UniProtKB:A0A5C2A2T2};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:A0A5C2A2T2};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain; probably disulfide-
CC       linked. {ECO:0000269|PubMed:30765458}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30765458}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:30765458}.
CC   -!- MASS SPECTROMETRY: Mass=13402; Method=MALDI; Note=The measured mass is
CC       of a heterodimer of an alpha and a beta chain.;
CC       Evidence={ECO:0000269|PubMed:30765458};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group IX subfamily.
CC       {ECO:0000305}.
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DR   EMBL; MK493029; QEO32924.1; -; mRNA.
DR   AlphaFoldDB; A0A5C1ZW08; -.
DR   SMR; A0A5C1ZW08; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.90.10; -; 1.
DR   InterPro; IPR038875; PLA2_conodipine-like.
DR   InterPro; IPR036444; PLipase_A2_dom_sf.
DR   PANTHER; PTHR37687; PTHR37687; 1.
DR   SUPFAM; SSF48619; SSF48619; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Hydroxylation; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250|UniProtKB:A0A5C2A2T2"
FT   CHAIN           25..97
FT                   /note="Conodipine-P3 alpha subunit"
FT                   /evidence="ECO:0000303|PubMed:30765458"
FT                   /id="PRO_0000449357"
FT   PROPEP          98..130
FT                   /note="Interchain peptide"
FT                   /evidence="ECO:0000303|PubMed:30765458"
FT                   /id="PRO_0000449358"
FT   CHAIN           131..178
FT                   /note="Conodipine-P3 beta subunit"
FT                   /evidence="ECO:0000303|PubMed:30765458"
FT                   /id="PRO_0000449359"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250|UniProtKB:P00608"
FT   MOD_RES         38
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:A0A5C2A2T2"
FT   MOD_RES         42
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:30765458"
FT   MOD_RES         49
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000269|PubMed:30765458"
FT   MOD_RES         131
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:A0A5C2A2T2"
FT   MOD_RES         137
FT                   /note="4-hydroxyproline; partial"
FT                   /evidence="ECO:0000250|UniProtKB:A0A5C2A2T2"
SQ   SEQUENCE   178 AA;  19835 MW;  0209F9EFE60D1CFA CRC64;
     MKLLAPVLWA MAALGVTWLV AVDSKESCTK HSNGCSTPLR LPCQEYFRPA CDIHDNCYHC
     GKTFGISREE CDKAFLKDMN TLCKKLGSNS ATCPARGKRE VTSHRATSIA HSRLWKTALD
     QKSFLNRKAR QVFFLLPTTC QGWAKNYHLA VKLAGANSYS VTTDLETCQG LEHCLPNH