PA21_ACAPL
ID PA21_ACAPL Reviewed; 159 AA.
AC Q3C2C2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phospholipase A2 AP-PLA2-I;
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 110-118 AND 127-156.
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: Homodimer.
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}.
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DR EMBL; AB211367; BAE46765.1; -; mRNA.
DR AlphaFoldDB; Q3C2C2; -.
DR SMR; Q3C2C2; -.
DR OMA; CMANARF; -.
DR OrthoDB; 1422829at2759; -.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..23
FT /evidence="ECO:0000269|PubMed:9643471"
FT /id="PRO_0000272033"
FT CHAIN 24..159
FT /note="Phospholipase A2 AP-PLA2-I"
FT /id="PRO_0000272034"
FT ACT_SITE 72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
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..159
FT /evidence="ECO:0000250"
FT DISULFID 53..69
FT /evidence="ECO:0000250"
FT DISULFID 68..139
FT /evidence="ECO:0000250"
FT DISULFID 75..132
FT /evidence="ECO:0000250"
FT DISULFID 85..125
FT /evidence="ECO:0000250"
FT DISULFID 110..130
FT /evidence="ECO:0000250"
SQ SEQUENCE 159 AA; 17830 MW; A4F4DC8F7B0D6266 CRC64;
MNFLVVIVTT VSLAGAASAG EIQNLYQFGK MVMCLGNLNV LEGLEYNGYG CYCGRGGKGT
PLDDTDRCCK QHDECYERAT DEMGCWSIET YATTYDYTKS KVSGKCTIKC KLESDYSRFT
IRKKCKAFIC ECDRIGAQCF ADKRSTFNRS LISYTKDKC
