PA2G5_RAT
ID PA2G5_RAT Reviewed; 137 AA.
AC P51433; Q6DQ96;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phospholipase A2 group V;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:P39877, ECO:0000250|UniProtKB:P97391};
DE AltName: Full=PLA2-10;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 5;
DE Flags: Precursor;
GN Name=Pla2g5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7947992; DOI=10.1016/0005-2760(94)90099-x;
RA Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.;
RT "Cloning, expression and partial characterization of a novel rat
RT phospholipase A2.";
RL Biochim. Biophys. Acta 1215:115-120(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Ovary;
RA Liang N.S., Su Q.B., Li Y., Yang F., Lu Y., Xie Y.A.;
RT "Cloning and sequence determination of rat group V phospholipase A2 from
RT ovary.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids. Hydrolyzes the ester bond of the
CC fatty acyl group attached at sn-2 position of phospholipids
CC (phospholipase A2 activity), preferentially releasing fatty acyl groups
CC with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl
CC (C18:2) groups (By similarity). Hydrolyzes low-density lipoprotein
CC (LDL) phospholipids releasing unsaturated fatty acids that drive
CC macrophage polarization toward an M2 phenotype (By similarity). May act
CC in an autocrine and paracrine manner. Contributes to lipid remodeling
CC of cellular membranes at different subcellular locations and generation
CC of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty
CC acyl chains of cardiolipin, a major component of the inner membrane of
CC mitochondria and bacterial membranes. Promotes phagocytosis of bacteria
CC in macrophages through production of lysophosphatidylethanolamines.
CC Displays bactericidal activity against Gram-positive bacteria by
CC directly hydrolyzing phospholipids of the bacterial membrane (By
CC similarity). Promotes phagocytosis and killing of ingested fungi likely
CC through controlling phagosome-lysosome fusion and phagosome maturation
CC (By similarity). Plays a role in biosynthesis of cysteinyl leukotrienes
CC (CysLTs) in myeloid cells. In eosinophils, triggers perinuclear
CC arachidonate release and LTC4 synthesis in a PLA2G4A-independent way.
CC In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A (By
CC similarity). Promotes immune complex clearance in macrophages via
CC stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger
CC phagocytosis. May regulate antigen processing in antigen-presenting
CC cells. In pulmonary macrophages regulates IL33 production required for
CC activation of group 2 innate lymphoid cells (By similarity). May play a
CC role in the biosynthesis of N-acyl ethanolamines that regulate energy
CC metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines (By similarity).
CC {ECO:0000250|UniProtKB:P39877, ECO:0000250|UniProtKB:P97391}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + 1-octadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+);
CC Xref=Rhea:RHEA:41215, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:74243, ChEBI:CHEBI:133606;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41216;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:P97391};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000250|UniProtKB:P97391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-
CC octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40467, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77256,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468;
CC Evidence={ECO:0000250|UniProtKB:P39877};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40463, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77253,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:P39877};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464;
CC Evidence={ECO:0000250|UniProtKB:P39877};
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 -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC {ECO:0000250|UniProtKB:P39877}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97391}. Cell
CC membrane {ECO:0000250|UniProtKB:P97391}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P97391}. Recycling endosome
CC {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, cis-Golgi network
CC {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:P97391}.
CC -!- PTM: This enzyme lacks one of the seven disulfide bonds found in
CC similar PA2 proteins.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; U03763; AAA82112.1; -; mRNA.
DR EMBL; AY651028; AAT68714.1; -; mRNA.
DR EMBL; BC085745; AAH85745.1; -; mRNA.
DR RefSeq; NP_058870.1; NM_017174.1.
DR RefSeq; XP_006239201.1; XM_006239139.3.
DR RefSeq; XP_008762432.1; XM_008764210.2.
DR AlphaFoldDB; P51433; -.
DR SMR; P51433; -.
DR STRING; 10116.ENSRNOP00000022715; -.
DR PaxDb; P51433; -.
DR Ensembl; ENSRNOT00000022716; ENSRNOP00000022715; ENSRNOG00000016838.
DR GeneID; 29354; -.
DR KEGG; rno:29354; -.
DR UCSC; RGD:62051; rat.
DR CTD; 5322; -.
DR RGD; 62051; Pla2g5.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000162222; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; P51433; -.
DR OMA; WVHDRCY; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P51433; -.
DR TreeFam; TF319283; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR UniPathway; UPA00085; -.
DR UniPathway; UPA00878; -.
DR UniPathway; UPA00879; -.
DR PRO; PR:P51433; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016838; Expressed in heart and 16 other tissues.
DR Genevisible; P51433; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032010; C:phagolysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:RGD.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:RGD.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:RGD.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; IDA:RGD.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0090265; P:positive regulation of immune complex clearance by monocytes and macrophages; ISS:UniProtKB.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:1905164; P:positive regulation of phagosome maturation; ISS:UniProtKB.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:RGD.
DR GO; GO:0043030; P:regulation of macrophage activation; ISO:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
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; Cell membrane; Cytoplasmic vesicle; Disulfide bond; Endosome;
KW Fatty acid metabolism; Golgi apparatus; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Phagocytosis;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..137
FT /note="Phospholipase A2 group V"
FT /id="PRO_0000022763"
FT ACT_SITE 67
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 46..137
FT /evidence="ECO:0000250"
FT DISULFID 48..64
FT /evidence="ECO:0000250"
FT DISULFID 63..117
FT /evidence="ECO:0000250"
FT DISULFID 70..110
FT /evidence="ECO:0000250"
FT DISULFID 79..103
FT /evidence="ECO:0000250"
FT DISULFID 97..108
FT /evidence="ECO:0000250"
SQ SEQUENCE 137 AA; 15996 MW; B21607EF741FA608 CRC64;
MKRLLTLAWF LACSVPAVPG GLLELKSMIE KVTGKNAVKN YGFYGCYCGW GGHGTPKDGT
DWCCRMHDRC YGLLEEKHCA IRTQSYDYRF TQDLVICEHD SFCPVRLCAC DRKLVYCLRR
NLWSYNRLYQ YYPNFLC
