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 24-JAN-2024, entry version 196. 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- CC phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn- CC glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; CC 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/"; 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; 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; 30. 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; 9606-ENSP00000364249; -. DR PeptideAtlas; P39877; -. DR Antibodypedia; 29758; 171 antibodies from 23 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 AGR; HGNC:9038; -. DR CTD; 5322; -. DR DisGeNET; 5322; -. DR GeneCards; PLA2G5; -. DR HGNC; HGNC:9038; PLA2G5. DR HPA; ENSG00000127472; Tissue enhanced (choroid plexus, heart muscle). 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 OrthoDB; 638584at2759; -. 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; 15 hits in 1149 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 130 other cell types or tissues. 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:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central. 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; Phospholipase A2 domain; 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; PHOSPHOLIPASE A2 FAMILY MEMBER; 1. DR PANTHER; PTHR11716:SF10; PHOSPHOLIPASE A2 GROUP V; 1. DR Pfam; PF00068; Phospholip_A2_1; 1. DR PRINTS; PR00389; PHPHLIPASEA2. DR SMART; SM00085; PA2c; 1. DR SUPFAM; SSF48619; Phospholipase A2, PLA2; 1. DR PROSITE; PS00119; PA2_ASP; 1. DR PROSITE; PS00118; PA2_HIS; 1. DR Genevisible; P39877; HS. 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 //