PA2G5_HUMAN
ID PA2G5_HUMAN Reviewed; 138 AA.
AC P39877; Q8N435;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Phospholipase A2 group V;
DE EC=3.1.1.4 {ECO:0000269|PubMed:23533611, ECO:0000269|PubMed:8300559};
DE AltName: Full=PLA2-10;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 5;
DE Flags: Precursor;
GN Name=PLA2G5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Stomach;
RX PubMed=8300559; DOI=10.1016/s0021-9258(17)41952-1;
RA Chen J., Engle S.J., Seilhamer J.J., Tischfield J.A.;
RT "Cloning and recombinant expression of a novel human low molecular weight
RT Ca(2+)-dependent phospholipase A2.";
RL J. Biol. Chem. 269:2365-2368(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION.
RX PubMed=11694541; DOI=10.1074/jbc.m109699200;
RA Koduri R.S., Groenroos J.O., Laine V.J., Le Calvez C., Lambeau G.,
RA Nevalainen T.J., Gelb M.H.;
RT "Bactericidal properties of human and murine groups I, II, V, X, and XII
RT secreted phospholipases A(2).";
RL J. Biol. Chem. 277:5849-5857(2002).
RN [6]
RP FUNCTION, AND PATHWAY.
RX PubMed=12124392; DOI=10.1074/jbc.m205399200;
RA Kim Y.J., Kim K.P., Han S.K., Munoz N.M., Zhu X., Sano H., Leff A.R.,
RA Cho W.;
RT "Group V phospholipase A2 induces leukotriene biosynthesis in human
RT neutrophils through the activation of group IVA phospholipase A2.";
RL J. Biol. Chem. 277:36479-36488(2002).
RN [7]
RP FUNCTION, MUTAGENESIS OF TRP-50; ARG-112 AND LYS-113, AND PATHWAY.
RX PubMed=12796497; DOI=10.1074/jbc.m302476200;
RA Munoz N.M., Kim Y.J., Meliton A.Y., Kim K.P., Han S.K., Boetticher E.,
RA O'Leary E., Myou S., Zhu X., Bonventre J.V., Leff A.R., Cho W.;
RT "Human group V phospholipase A2 induces group IVA phospholipase A2-
RT independent cysteinyl leukotriene synthesis in human eosinophils.";
RL J. Biol. Chem. 278:38813-38820(2003).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14998370; DOI=10.1042/bj20040031;
RA Sun Y.X., Tsuboi K., Okamoto Y., Tonai T., Murakami M., Kudo I., Ueda N.;
RT "Biosynthesis of anandamide and N-palmitoylethanolamine by sequential
RT actions of phospholipase A2 and lysophospholipase D.";
RL Biochem. J. 380:749-756(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=23533611; DOI=10.1371/journal.pone.0059267;
RA Hsu Y.H., Dumlao D.S., Cao J., Dennis E.A.;
RT "Assessing phospholipase A2 activity toward cardiolipin by mass
RT spectrometry.";
RL PLoS ONE 8:E59267-E59267(2013).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY CYTOKINES, AND PATHWAY.
RX PubMed=25725101; DOI=10.4049/jimmunol.1401026;
RA Rubio J.M., Rodriguez J.P., Gil-de-Gomez L., Guijas C., Balboa M.A.,
RA Balsinde J.;
RT "Group V secreted phospholipase A2 is upregulated by IL-4 in human
RT macrophages and mediates phagocytosis via hydrolysis of ethanolamine
RT phospholipids.";
RL J. Immunol. 194:3327-3339(2015).
RN [11]
RP INVOLVEMENT IN FRFB, VARIANTS FRFB CYS-45 AND SER-49, AND TISSUE
RP SPECIFICITY.
RX PubMed=22137173; DOI=10.1016/j.ajhg.2011.11.004;
RA Sergouniotis P.I., Davidson A.E., Mackay D.S., Lenassi E., Li Z.,
RA Robson A.G., Yang X., Kam J.H., Isaacs T.W., Holder G.E., Jeffery G.,
RA Beck J.A., Moore A.T., Plagnol V., Webster A.R.;
RT "Biallelic mutations in PLA2G5, encoding group V phospholipase A2, cause
RT benign fleck retina.";
RL Am. J. Hum. Genet. 89:782-791(2011).
RN [12]
RP INVOLVEMENT IN FRFB, AND VARIANT FRFB CYS-45.
RX PubMed=25549071; DOI=10.1097/iae.0000000000000446;
RA Bin N.J., Heng H.M., Poh R., Noor S.M., Subrayan V.;
RT "Phospholipase A2 group v in benign familial fleck retina in a set of
RT triplets.";
RL Retina 35:1266-1272(2015).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids (PubMed:8300559). Hydrolyzes the
CC ester bond of the fatty acyl group attached at sn-2 position of
CC phospholipids (phospholipase A2 activity), preferentially releasing
CC fatty acyl groups with a low degree of unsaturation such as oleoyl
CC (C18:1) and linoleoyl (C18:2) groups (PubMed:8300559, PubMed:14998370,
CC PubMed:23533611). Hydrolyzes low-density lipoprotein (LDL)
CC phospholipids releasing unsaturated fatty acids that drive macrophage
CC polarization toward an M2 phenotype (By similarity). May act in an
CC autocrine and paracrine manner. Contributes to lipid remodeling of
CC cellular membranes at different subcellular locations and generation of
CC lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl
CC chains of cardiolipin, a major component of the inner membrane of
CC mitochondria and bacterial membranes (PubMed:23533611). Promotes
CC phagocytosis of bacteria in macrophages through production of
CC lysophosphatidylethanolamines (PubMed:25725101). Displays bactericidal
CC activity against Gram-positive bacteria by directly hydrolyzing
CC phospholipids of the bacterial membrane (PubMed:11694541). Promotes
CC phagocytosis and killing of ingested fungi likely through controlling
CC phagosome-lysosome fusion and phagosome maturation (By similarity).
CC Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in
CC myeloid cells (PubMed:12124392, PubMed:12796497). In eosinophils,
CC triggers perinuclear arachidonate release and LTC4 synthesis in a
CC PLA2G4A-independent way (PubMed:12796497). In neutrophils, amplifies
CC CysLTs biosynthesis initiated by PLA2G4A (PubMed:12124392). Promotes
CC immune complex clearance in macrophages via stimulating synthesis of
CC CysLTs, which act through CYSLTR1 to trigger phagocytosis (By
CC similarity). May regulate antigen processing in antigen-presenting
CC cells (By similarity). In pulmonary macrophages regulates IL33
CC production required for activation of group 2 innate lymphoid cells (By
CC similarity). May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl
CC phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines,
CC which are further cleaved by a lysophospholipase D to release N-acyl
CC ethanolamines (PubMed:14998370). {ECO:0000250|UniProtKB:P97391,
CC ECO:0000269|PubMed:11694541, ECO:0000269|PubMed:12124392,
CC ECO:0000269|PubMed:12796497, ECO:0000269|PubMed:14998370,
CC ECO:0000269|PubMed:23533611, ECO:0000269|PubMed:25725101,
CC ECO:0000269|PubMed:8300559}.
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:23533611,
CC ECO:0000269|PubMed:8300559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:23533611, ECO:0000305|PubMed:8300559};
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:0000269|PubMed:23533611,
CC ECO:0000269|PubMed:8300559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:23533611, ECO:0000305|PubMed:8300559};
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:0000269|PubMed:23533611, ECO:0000269|PubMed:8300559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:23533611, ECO:0000305|PubMed:8300559};
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:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:14998370};
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:0000269|PubMed:8300559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:8300559};
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:0000269|PubMed:8300559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41216;
CC Evidence={ECO:0000305|PubMed:8300559};
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:0000269|PubMed:14998370};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000305|PubMed:14998370};
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:0000269|PubMed:23533611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468;
CC Evidence={ECO:0000305|PubMed:23533611};
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:0000269|PubMed:23533611};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464;
CC Evidence={ECO:0000305|PubMed:23533611};
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 -!- ACTIVITY REGULATION: Activated by cardiolipin.
CC {ECO:0000269|PubMed:23533611}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. Activity remains high up to pH 9.0.
CC {ECO:0000269|PubMed:8300559};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:25725101}.
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC {ECO:0000269|PubMed:12124392}.
CC -!- PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis.
CC {ECO:0000269|PubMed:12796497}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8300559}. 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 -!- TISSUE SPECIFICITY: Heart, placenta and less abundantly, in lung.
CC Detected in the outer and inner plexiform layers of the retina (at
CC protein level) (PubMed:22137173). Expressed in monocytes and
CC macrophages (PubMed:25725101). {ECO:0000269|PubMed:22137173,
CC ECO:0000269|PubMed:25725101}.
CC -!- INDUCTION: Up-regulated upon M2 macrophage polarization in response to
CC IL4, CSF1 or IL10. {ECO:0000269|PubMed:25725101}.
CC -!- PTM: This enzyme lacks one of the seven disulfide bonds found in
CC similar PLA2 proteins.
CC -!- DISEASE: Fleck retina, familial benign (FRFB) [MIM:228980]: An
CC autosomal recessive condition associated with a distinctive retinal
CC appearance and no apparent visual or electrophysiologic deficits.
CC Affected individuals are asymptomatic, but fundus examination reveals a
CC striking pattern of diffuse, yellow-white, fleck-like lesions extending
CC to the far periphery of the retina but sparing the foveal region.
CC {ECO:0000269|PubMed:22137173, ECO:0000269|PubMed:25549071}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/pla2g5/";
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DR EMBL; U03090; AAC28886.1; -; mRNA.
DR EMBL; AY524778; AAR92480.1; -; Genomic_DNA.
DR EMBL; AL158172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036792; AAH36792.2; -; mRNA.
DR CCDS; CCDS202.1; -.
DR PIR; A49959; A49959.
DR RefSeq; NP_000920.1; NM_000929.2.
DR RefSeq; XP_005245950.1; XM_005245893.4.
DR RefSeq; XP_011539889.1; XM_011541587.2.
DR RefSeq; XP_011539890.1; XM_011541588.2.
DR RefSeq; XP_011539891.1; XM_011541589.2.
DR RefSeq; XP_011539892.1; XM_011541590.2.
DR RefSeq; XP_011539893.1; XM_011541591.2.
DR RefSeq; XP_011539894.1; XM_011541592.2.
DR AlphaFoldDB; P39877; -.
DR SMR; P39877; -.
DR BioGRID; 111339; 29.
DR STRING; 9606.ENSP00000364249; -.
DR BindingDB; P39877; -.
DR ChEMBL; CHEMBL4323; -.
DR GuidetoPHARMACOLOGY; 1430; -.
DR SwissLipids; SLP:000000140; -.
DR BioMuta; PLA2G5; -.
DR DMDM; 730258; -.
DR MassIVE; P39877; -.
DR PaxDb; P39877; -.
DR PeptideAtlas; P39877; -.
DR PRIDE; P39877; -.
DR ProteomicsDB; 55320; -.
DR Antibodypedia; 29758; 149 antibodies from 22 providers.
DR DNASU; 5322; -.
DR Ensembl; ENST00000375108.4; ENSP00000364249.3; ENSG00000127472.11.
DR GeneID; 5322; -.
DR KEGG; hsa:5322; -.
DR MANE-Select; ENST00000375108.4; ENSP00000364249.3; NM_000929.3; NP_000920.1.
DR UCSC; uc001bcy.4; human.
DR CTD; 5322; -.
DR DisGeNET; 5322; -.
DR GeneCards; PLA2G5; -.
DR HGNC; HGNC:9038; PLA2G5.
DR HPA; ENSG00000127472; Tissue enhanced (heart muscle, ovary).
DR MalaCards; PLA2G5; -.
DR MIM; 228980; phenotype.
DR MIM; 601192; gene.
DR neXtProt; NX_P39877; -.
DR OpenTargets; ENSG00000127472; -.
DR Orphanet; 363989; Familial benign flecked retina.
DR PharmGKB; PA33366; -.
DR VEuPathDB; HostDB:ENSG00000127472; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000162222; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; P39877; -.
DR OMA; WVHDRCY; -.
DR PhylomeDB; P39877; -.
DR TreeFam; TF319283; -.
DR PathwayCommons; P39877; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SignaLink; P39877; -.
DR UniPathway; UPA00085; -.
DR UniPathway; UPA00878; -.
DR UniPathway; UPA00879; -.
DR BioGRID-ORCS; 5322; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; PLA2G5; human.
DR GeneWiki; PLA2G5; -.
DR GenomeRNAi; 5322; -.
DR Pharos; P39877; Tchem.
DR PRO; PR:P39877; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P39877; protein.
DR Bgee; ENSG00000127472; Expressed in right atrium auricular region and 128 other tissues.
DR Genevisible; P39877; HS.
DR GO; GO:0032009; C:early phagosome; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0032010; C:phagolysosome; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
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; IDA:CACAO.
DR GO; GO:0090265; P:positive regulation of immune complex clearance by monocytes and macrophages; IDA: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; IDA:CACAO.
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 Calcium; Cell membrane; Cytoplasmic vesicle; Disease variant;
KW Disulfide bond; Endosome; Fatty acid metabolism; Golgi apparatus;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Metal-binding;
KW Phagocytosis; Phospholipid degradation; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..138
FT /note="Phospholipase A2 group V"
FT /id="PRO_0000022761"
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"
FT VARIANT 45
FT /note="G -> C (in FRFB; dbSNP:rs387906795)"
FT /evidence="ECO:0000269|PubMed:22137173,
FT ECO:0000269|PubMed:25549071"
FT /id="VAR_067343"
FT VARIANT 49
FT /note="G -> S (in FRFB; dbSNP:rs387906796)"
FT /evidence="ECO:0000269|PubMed:22137173"
FT /id="VAR_067344"
FT MUTAGEN 50
FT /note="W->A: Impairs arachidonate release from cell
FT membranes."
FT /evidence="ECO:0000269|PubMed:12796497"
FT MUTAGEN 112
FT /note="R->E: Decreases arachidonate release from cell
FT membranes; when associated with E-113."
FT /evidence="ECO:0000269|PubMed:12796497"
FT MUTAGEN 113
FT /note="K->E: Decreases arachidonate release from cell
FT membranes; when associated with E-112."
FT /evidence="ECO:0000269|PubMed:12796497"
SQ SEQUENCE 138 AA; 15674 MW; 0D17DC76E55F42BC CRC64;
MKGLLPLAWF LACSVPAVQG GLLDLKSMIE KVTGKNALTN YGFYGCYCGW GGRGTPKDGT
DWCCWAHDHC YGRLEEKGCN IRTQSYKYRF AWGVVTCEPG PFCHVNLCAC DRKLVYCLKR
NLRSYNPQYQ YFPNILCS
