PA2_CONGI
ID PA2_CONGI Reviewed; 119 AA.
AC D2X8K2;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Phospholipase A2 A2-actitoxin-Cgg2a {ECO:0000303|PubMed:22683676};
DE Short=A2-AITX-Cgg2a {ECO:0000303|PubMed:22683676};
DE EC=3.1.1.4 {ECO:0000269|PubMed:20562011};
DE AltName: Full=CgPLA2 {ECO:0000303|PubMed:20562011};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
OS Condylactis gigantea (Giant Caribbean anemone) (Condylactis passiflora).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Condylactis.
OX NCBI_TaxID=47073;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-32, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, SUBUNIT, AND 3D-STRUCTURE MODELING.
RX PubMed=20562011; DOI=10.1016/j.biochi.2010.05.007;
RA Romero L., Marcussi S., Marchi-Salvador D.P., Silva F.P. Jr., Fuly A.L.,
RA Stabeli R.G., da Silva S.L., Gonzalez J., Monte A.D., Soares A.M.;
RT "Enzymatic and structural characterization of a basic phospholipase A(2)
RT from the sea anemone Condylactis gigantea.";
RL Biochimie 92:1063-1071(2010).
RN [2]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
CC -!- FUNCTION: Sea anemone phospholipase A2 (PLA2). When incubated with
CC plasma, this protein shows a moderate anticoagulant activity (0.15 ug
CC of enzyme/200 uL of plasma), inhibiting clotting induced by thrombin.
CC This enzyme also induces myotoxicity, and edema. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:20562011}.
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:20562011};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:20562011};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:20562011};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20562011}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MISCELLANEOUS: Lacks hemolytic activity. {ECO:0000269|PubMed:20562011}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; GU046515; ADB13102.1; -; mRNA.
DR AlphaFoldDB; D2X8K2; -.
DR SMR; D2X8K2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0044522; P:envenomation resulting in myocyte killing in another organism; IDA:UniProtKB.
DR GO; GO:0007599; P:hemostasis; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0035899; P:negative regulation of blood coagulation in another organism; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis; Hemostasis impairing toxin; Hydrolase;
KW Inflammatory response; Metal-binding; Myotoxin; Nematocyst; Secreted;
KW Toxin.
FT CHAIN 1..119
FT /note="Phospholipase A2 A2-actitoxin-Cgg2a"
FT /id="PRO_0000413797"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT ACT_SITE 95
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 25..119
FT /evidence="ECO:0000250"
FT DISULFID 27..43
FT /evidence="ECO:0000250"
FT DISULFID 42..101
FT /evidence="ECO:0000250"
FT DISULFID 49..94
FT /evidence="ECO:0000250"
FT DISULFID 61..87
FT /evidence="ECO:0000250"
FT DISULFID 78..92
FT /evidence="ECO:0000250"
SQ SEQUENCE 119 AA; 13637 MW; 9E3A966D96568D30 CRC64;
GVWQFAYMIA KYTGRNPLDY WGYGCWCGLG GKGNPVDAVD RCCYVHDVCY NSITQGPRPT
CSRIAPYHKN YYFTGKKCST GWLTSKCGRA ICACDIAAVK CFRRNHFNKK YRLYKKNIC
