PA2_ADAPA
ID PA2_ADAPA Reviewed; 156 AA.
AC Q8WS88;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Phospholipase A2 A2-hormotoxin-Apt1a {ECO:0000303|PubMed:22683676};
DE Short=A2-HRTX-Apt1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=AcPLA2 {ECO:0000303|PubMed:12091102};
DE EC=3.1.1.4;
DE AltName: Full=Acarc;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE Flags: Precursor;
OS Adamsia palliata (Cloak anemone) (Adamsia carciniopados).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Nynantheae; Hormathiidae; Adamsia.
OX NCBI_TaxID=176095;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12091102; DOI=10.1016/s1096-4959(02)00073-8;
RA Talvinen K.A., Nevalainen T.J.;
RT "Cloning of a novel phospholipase A2 from the cnidarian Adamsia
RT carciniopados.";
RL Comp. Biochem. Physiol. 132B:571-578(2002).
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) that may have a role both
CC in defense and in digestion, since its expression and enzymatic
CC activity were found both in the acontia (defensive organs) and
CC tentacles. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-
CC acyl groups in 3-sn-phosphoglycerides. {ECO:0000303|PubMed:12091102}.
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF347072; AAL57187.1; -; mRNA.
DR AlphaFoldDB; Q8WS88; -.
DR SMR; Q8WS88; -.
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; IEA:InterPro.
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:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Nematocyst; Secreted;
KW Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..35
FT /evidence="ECO:0000305"
FT /id="PRO_0000239808"
FT CHAIN 38..156
FT /note="Phospholipase A2 A2-hormotoxin-Apt1a"
FT /id="PRO_0000239809"
FT ACT_SITE 83
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 62..156
FT /evidence="ECO:0000250"
FT DISULFID 64..80
FT /evidence="ECO:0000250"
FT DISULFID 79..138
FT /evidence="ECO:0000250"
FT DISULFID 86..131
FT /evidence="ECO:0000250"
FT DISULFID 115..129
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 17814 MW; 2D09EC727A9B957B CRC64;
MQLYTYFFTF SLVLILALAD QENKSLDFTQ EGGIAKRGAF QFSYLIKKYT GRNPLDYWGY
GCWCGLGGKG TPVDGVDWCC YHHDMCFNSI TQGPRPTCSK NAPYHKNYYF SGLKCSTGWL
TSKCGRAICA CDIAAVKCFM RNHFNNKYQN YKKNIC
