COP1_CONPU
ID COP1_CONPU Reviewed; 178 AA.
AC A0A5C2A2T2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Conodipine-P1 {ECO:0000303|PubMed:30765458};
DE Short=Cdpi-P1 {ECO:0000303|PubMed:30765458};
DE EC=3.1.1.4 {ECO:0000269|PubMed:30765458};
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-P1 alpha subunit {ECO:0000303|PubMed:30765458};
DE Contains:
DE RecName: Full=Conodipine-P1 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:QEO32922.1};
RN [1] {ECO:0000312|EMBL:QEO32922.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-96; 131-157 AND 167-178,
RP MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, HYDROXYLATION AT PRO-38; PRO-42;
RP PRO-49 AND PRO-137, AND PYROGLUTAMATE FORMATION AT GLN-131.
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:0000269|PubMed:30765458}.
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:0000269|PubMed:30765458};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:30765458};
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=13535.80; Method=MALDI; Note=The measured mass
CC is of a heterodimer of an alpha and a beta chain.;
CC Evidence={ECO:0000269|PubMed:30765458};
CC -!- MASS SPECTROMETRY: [Conodipine-P1 alpha subunit]: Mass=8595.11;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:30765458};
CC -!- MASS SPECTROMETRY: [Conodipine-P1 beta subunit]: Mass=5634.82;
CC Method=MALDI; 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; MK493027; QEO32922.1; -; mRNA.
DR AlphaFoldDB; A0A5C2A2T2; -.
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:0000269|PubMed:30765458"
FT CHAIN 25..97
FT /note="Conodipine-P1 alpha subunit"
FT /evidence="ECO:0000303|PubMed:30765458"
FT /id="PRO_0000449351"
FT PROPEP 98..130
FT /note="Interchain peptide"
FT /evidence="ECO:0000303|PubMed:30765458"
FT /id="PRO_0000449352"
FT CHAIN 131..178
FT /note="Conodipine-P1 beta subunit"
FT /evidence="ECO:0000303|PubMed:30765458"
FT /id="PRO_0000449353"
FT ACT_SITE 54
FT /evidence="ECO:0000250|UniProtKB:P00608"
FT MOD_RES 38
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:30765458"
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:0000269|PubMed:30765458"
FT MOD_RES 137
FT /note="4-hydroxyproline; partial"
FT /evidence="ECO:0000269|PubMed:30765458"
SQ SEQUENCE 178 AA; 19968 MW; E8DD2E4197754496 CRC64;
MKLLAPVLWA MAALGVTWLV AVDSKESCTK HSNGCSTPLR LPCQEYFRPA CDIHDNCYHC
GTIFGISRKE CDDAFLKDMN TLCKKLGSNS ATCPARGKRE VTSHRATSIA HSRLWKTALD
QKSFLNRKAR QAILLTPNSC LYWANNFYMA VHVFGARSYS RTTDPKDCQG LKHCLPNH
