ID   PA22_ACAPL              Reviewed;         158 AA.
AC   Q3C2C1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Phospholipase A2 AP-PLA2-II;
DE            Short=PLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase 2;
DE   Flags: Precursor;
OS   Acanthaster planci (Crown-of-thorns starfish).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Acanthasteridae; Acanthaster.
OX   NCBI_TaxID=133434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 131-158.
RX   PubMed=16275035; DOI=10.1016/j.cbpb.2005.10.001;
RA   Ota E., Nagai H., Nagashima Y., Shiomi K.;
RT   "Molecular cloning of two toxic phospholipases A2 from the crown-of-thorns
RT   starfish Acanthaster planci venom.";
RL   Comp. Biochem. Physiol. 143B:54-60(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-85, AND FUNCTION.
RC   TISSUE=Spine;
RX   PubMed=9643471; DOI=10.1016/s0041-0101(97)00085-8;
RA   Shiomi K.A., Kazama A., Shimakura K., Nagashima Y.;
RT   "Purification and properties of phospholipases A2 from the crown-of-thorns
RT   starfish (Acanthaster planci) venom.";
RL   Toxicon 36:589-599(1998).
CC   -!- FUNCTION: Starfish phospholipase A2 (PLA2) that has hemorrhagic and
CC       capillary permeability-increasing activities and hence is considered to
CC       be deeply involved in the local inflammation. Shows hemolytic activity
CC       only in the presence of phosphatidylcholine (PC). PLA2 catalyzes the
CC       calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC       phosphoglycerides. {ECO:0000269|PubMed:9643471}.
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};
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB211368; BAE46766.1; -; mRNA.
DR   AlphaFoldDB; Q3C2C1; -.
DR   SMR; Q3C2C1; -.
DR   Proteomes; UP000694845; Unplaced.
DR   GO; GO:0005576; C:extracellular region; 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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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; 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; PS00118; PA2_HIS; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis;
KW   Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Metal-binding; Reference proteome;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..23
FT                   /evidence="ECO:0000269|PubMed:9643471"
FT                   /id="PRO_0000272035"
FT   CHAIN           24..158
FT                   /note="Phospholipase A2 AP-PLA2-II"
FT                   /id="PRO_0000272036"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..158
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        85..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..129
FT                   /evidence="ECO:0000250"
FT   CONFLICT        30
FT                   /note="K -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="T -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   158 AA;  17490 MW;  A013B58205747C22 CRC64;
     MKTFLILAMA VALAKAQSTD EITNLVQFGK LVMCLGNIGY TEGLEYDGYG CFCGKGGKGT
     PVDATDRCCE VHDNCYGQAV EEGKCWSVET YGTTYWYDQS TSGSCSIRCW EEGDYNSLVP
     RKACKAAICE CDRKAAQCFA DNRPTFNRKY LNYAKDTC