ID PA24A_HUMAN Reviewed; 749 AA. AC P47712; B1AKG4; Q29R80; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Cytosolic phospholipase A2; DE Short=cPLA2; DE AltName: Full=Phospholipase A2 group IVA; DE Includes: DE RecName: Full=Phospholipase A2; DE EC=3.1.1.4 {ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:7794891}; DE AltName: Full=Phosphatidylcholine 2-acylhydrolase; DE Includes: DE RecName: Full=Lysophospholipase; DE EC=3.1.1.5 {ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:16617059}; GN Name=PLA2G4A; Synonyms=CPLA2, PLA2G4; 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], PARTIAL PROTEIN SEQUENCE, AND VARIANT LYS-651. RX PubMed=1904318; DOI=10.1016/0092-8674(91)90556-e; RA Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A., Lin A.Y., RA Milona N., Knopf J.L.; RT "A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)- RT dependent translocation domain with homology to PKC and GAP."; RL Cell 65:1043-1051(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-651. RX PubMed=1869522; DOI=10.1016/s0021-9258(18)98550-9; RA Sharp J., White D., Chiou G., Goodson T., Gamboa G., McClure D., RA Burgett S., Hoskins J., Skatrud P., Sportsman J., Becker G., Kang L., RA Roberts E., Kramer R.; RT "Molecular cloning and expression of human Ca(2+)-sensitive cytosolic RT phospholipase A2."; RL J. Biol. Chem. 266:14850-14853(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-224 AND LYS-651. RG NIEHS SNPs program; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-651. 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 [6] RP MUTAGENESIS OF SER-505, PHOSPHORYLATION AT SER-505, AND ACTIVITY RP REGULATION. RX PubMed=8381049; DOI=10.1016/0092-8674(93)90666-e; RA Lin L.-L., Wartmann M., Lin A.Y., Knopf J.L., Seth A., Davis R.J.; RT "cPLA2 is phosphorylated and activated by MAP kinase."; RL Cell 72:269-278(1993). RN [7] RP ACTIVE SITE, MUTAGENESIS OF CYS-139; CYS-141; CYS-151; SER-195; SER-215; RP CYS-220; SER-228; CYS-324; CYS-331; SER-577; CYS-620; CYS-634 AND CYS-726, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=8083230; DOI=10.1016/s0021-9258(17)31645-9; RA Sharp J.D., Pickard R.T., Chiou X.G., Manetta J.V., Kovacevic S., RA Miller J.R., Varshavsky A.D., Roberts E.F., Strifler B.A., Brems D.N., RA Kramer R.M.; RT "Serine 228 is essential for catalytic activities of 85-kDa cytosolic RT phospholipase A2."; RL J. Biol. Chem. 269:23250-23254(1994). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7794891; DOI=10.1021/bi00024a004; RA Hanel A.M., Gelb M.H.; RT "Multiple enzymatic activities of the human cytosolic 85-kDa phospholipase RT A2: hydrolytic reactions and acyl transfer to glycerol."; RL Biochemistry 34:7807-7818(1995). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF SER-228. RX PubMed=8619991; DOI=10.1021/bi952541k; RA Huang Z., Payette P., Abdullah K., Cromlish W.A., Kennedy B.P.; RT "Functional identification of the active-site nucleophile of the human 85- RT kDa cytosolic phospholipase A2."; RL Biochemistry 35:3712-3721(1996). RN [10] RP FUNCTION, ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-200; RP SER-228 AND ASP-549. RX PubMed=8702602; DOI=10.1074/jbc.271.32.19225; RA Pickard R.T., Chiou X.G., Strifler B.A., DeFelippis M.R., Hyslop P.A., RA Tebbe A.L., Yee Y.K., Reynolds L.J., Dennis E.A., Kramer R.M., Sharp J.D.; RT "Identification of essential residues for the catalytic function of 85-kDa RT cytosolic phospholipase A2. Probing the role of histidine, aspartic acid, RT cysteine, and arginine."; RL J. Biol. Chem. 271:19225-19231(1996). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=9425121; DOI=10.1042/bj3290369; RA Buckland A.G., Wilton D.C.; RT "Inhibition of human cytosolic phospholipase A2 by human annexin V."; RL Biochem. J. 329:369-372(1998). RN [12] RP PHOSPHORYLATION AT SER-505 AND SER-727. RX PubMed=9468497; DOI=10.1074/jbc.273.8.4449; RA Boersch-Haubold A.G., Bartoli F., Asselin J., Dudler T., Kramer R.M., RA Apitz-Castro R., Watson S.P., Gelb M.H.; RT "Identification of the phosphorylation sites of cytosolic phospholipase A2 RT in agonist-stimulated human platelets and HeLa cells."; RL J. Biol. Chem. 273:4449-4458(1998). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10358058; DOI=10.1074/jbc.274.24.17063; RA Song C., Chang X.J., Bean K.M., Proia M.S., Knopf J.L., Kriz R.W.; RT "Molecular characterization of cytosolic phospholipase A2-beta."; RL J. Biol. Chem. 274:17063-17067(1999). RN [14] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=11375391; DOI=10.1074/jbc.m100943200; RA Evans J.H., Spencer D.M., Zweifach A., Leslie C.C.; RT "Intracellular calcium signals regulating cytosolic phospholipase A2 RT translocation to internal membranes."; RL J. Biol. Chem. 276:30150-30160(2001). RN [15] RP INTERACTION WITH KAT5. RX PubMed=11416127; DOI=10.1128/mcb.21.14.4470-4481.2001; RA Sheridan A.M., Force T., Yoon H.J., O'Leary E., Choukroun G., Taheri M.R., RA Bonventre J.V.; RT "PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic RT phospholipase A(2), induces apoptosis, and potentiates prostaglandin RT production."; RL Mol. Cell. Biol. 21:4470-4481(2001). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF ASP-43; RP SER-437; SER-454; LYS-488; SER-505; LYS-541; LYS-543; LYS-544 AND SER-727, RP AND DOMAIN. RX PubMed=12672805; DOI=10.1074/jbc.m301386200; RA Six D.A., Dennis E.A.; RT "Essential Ca(2+)-independent role of the group IVA cytosolic phospholipase RT A(2) C2 domain for interfacial activity."; RL J. Biol. Chem. 278:23842-23850(2003). RN [17] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=14709560; DOI=10.1074/jbc.m305801200; RA Chiba H., Michibata H., Wakimoto K., Seishima M., Kawasaki S., Okubo K., RA Mitsui H., Torii H., Imai Y.; RT "Cloning of a gene for a novel epithelium-specific cytosolic phospholipase RT A2, cPLA2delta, induced in psoriatic skin."; RL J. Biol. Chem. 279:12890-12897(2004). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16617059; DOI=10.1074/jbc.m601770200; RA Ghosh M., Loper R., Gelb M.H., Leslie C.C.; RT "Identification of the expressed form of human cytosolic phospholipase RT A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria RT and early endosomes."; RL J. Biol. Chem. 281:16615-16624(2006). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF RP 57-ARG--ARG-59, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17472963; DOI=10.1074/jbc.m701396200; RA Stahelin R.V., Subramanian P., Vora M., Cho W., Chalfant C.E.; RT "Ceramide-1-phosphate binds group IVA cytosolic phospholipase a2 via a RT novel site in the C2 domain."; RL J. Biol. Chem. 282:20467-20474(2007). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437; SER-727 AND RP SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-437 AND SER-729, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-268; SER-435; SER-437; RP SER-727 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [28] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27642067; DOI=10.1016/j.chembiol.2016.08.009; RA Liu X., Moon S.H., Jenkins C.M., Sims H.F., Gross R.W.; RT "Cyclooxygenase-2 Mediated Oxidation of 2-Arachidonoyl-Lysophospholipids RT Identifies Unknown Lipid Signaling Pathways."; RL Cell Chem. Biol. 23:1217-1227(2016). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-541 AND LYS-606, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-141 IN COMPLEX WITH CALCIUM RP IONS, AND DOMAIN. RX PubMed=9430701; DOI=10.1074/jbc.273.3.1596; RA Perisic O., Fong S., Lynch D.E., Bycroft M., Williams R.L.; RT "Crystal structure of a calcium-phospholipid binding domain from cytosolic RT phospholipase A2."; RL J. Biol. Chem. 273:1596-1604(1998). RN [31] RP STRUCTURE BY NMR OF 1-138 IN COMPLEX WITH CALCIUM IONS, DOMAIN, AND RP SUBCELLULAR LOCATION. RX PubMed=9665851; DOI=10.1006/jmbi.1998.1874; RA Xu G.-Y., McDonagh T., Yu H.-A., Nalefski E.A., Clark J.D., Cumming D.A.; RT "Solution structure and membrane interactions of the C2 domain of cytosolic RT phospholipase A2."; RL J. Mol. Biol. 280:485-500(1998). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND RP ACTIVE SITE. RX PubMed=10319815; DOI=10.1016/s0092-8674(00)80744-8; RA Dessen A., Tang J., Schmidt H., Stahl M., Clark J.D., Seehra J., RA Somers W.S.; RT "Crystal structure of human cytosolic phospholipase A2 reveals a novel RT topology and catalytic mechanism."; RL Cell 97:349-360(1999). RN [33] RP VARIANT [LARGE SCALE ANALYSIS] GLN-442. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [34] RP INVOLVEMENT IN GURDP, VARIANTS GURDP PRO-111 AND HIS-485, VARIANT LYS-651, RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=18451993; DOI=10.1172/jci30473; RA Adler D.H., Cogan J.D., Phillips J.A., Schnetz-Boutaud N., Milne G.L., RA Iverson T., Stein J.A., Brenner D.A., Morrow J.D., Boutaud O., Oates J.A.; RT "Inherited human cPLA(2alpha) deficiency is associated with impaired RT eicosanoid biosynthesis, small intestinal ulceration, and platelet RT dysfunction."; RL J. Clin. Invest. 118:2121-2131(2008). RN [35] RP INVOLVEMENT IN GURDP. RX PubMed=23268370; DOI=10.1136/gutjnl-2012-303581; RA Brooke M.A., Longhurst H.J., Plagnol V., Kirkby N.S., Mitchell J.A., RA Rueschendorf F., Warner T.D., Kelsell D.P., MacDonald T.T.; RT "Cryptogenic multifocal ulcerating stenosing enteritis associated with RT homozygous deletion mutations in cytosolic phospholipase A2-alpha."; RL Gut 63:96-104(2014). RN [36] RP INVOLVEMENT IN GURDP, VARIANT GURDP HIS-575, CHARACTERIZATION OF VARIANT RP GURDP HIS-575, AND TISSUE SPECIFICITY. RX PubMed=25102815; DOI=10.1160/th14-04-0352; RA Faioni E.M., Razzari C., Zulueta A., Femia E.A., Fenu L., Trinchera M., RA Podda G.M., Pugliano M., Marongiu F., Cattaneo M.; RT "Bleeding diathesis and gastro-duodenal ulcers in inherited cytosolic RT phospholipase-A2 alpha deficiency."; RL Thromb. Haemost. 112:1182-1189(2014). CC -!- FUNCTION: Has primarily calcium-dependent phospholipase and CC lysophospholipase activities, with a major role in membrane lipid CC remodeling and biosynthesis of lipid mediators of the inflammatory CC response (PubMed:7794891, PubMed:8619991, PubMed:8702602, CC PubMed:9425121, PubMed:10358058, PubMed:14709560, PubMed:16617059, CC PubMed:17472963, PubMed:27642067, PubMed:18451993). Plays an important CC role in embryo implantation and parturition through its ability to CC trigger prostanoid production (By similarity). Preferentially CC hydrolyzes the ester bond of the fatty acyl group attached at sn-2 CC position of phospholipids (phospholipase A2 activity) (PubMed:7794891, CC PubMed:8619991, PubMed:9425121, PubMed:10358058, PubMed:17472963, CC PubMed:18451993). Selectively hydrolyzes sn-2 arachidonoyl group from CC membrane phospholipids, providing the precursor for eicosanoid CC biosynthesis via the cyclooxygenase pathway (PubMed:18451993, CC PubMed:7794891, PubMed:9425121, PubMed:10358058, PubMed:17472963). In CC an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 CC fatty acyl chain of eicosanoid lysophopholipids to release free CC bioactive eicosanoids (PubMed:27642067). Hydrolyzes the ester bond of CC the fatty acyl group attached at sn-1 position of phospholipids CC (phospholipase A1 activity) only if an ether linkage rather than an CC ester linkage is present at the sn-2 position. This hydrolysis is not CC stereospecific (PubMed:7794891). Has calcium-independent phospholipase CC A2 and lysophospholipase activities in the presence of CC phosphoinositides (PubMed:12672805). Has O-acyltransferase activity. CC Catalyzes the transfer of fatty acyl chains from phospholipids to a CC primary hydroxyl group of glycerol (sn-1 or sn-3), potentially CC contributing to monoacylglycerol synthesis (PubMed:7794891). CC {ECO:0000250|UniProtKB:P47713, ECO:0000269|PubMed:10358058, CC ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:14709560, CC ECO:0000269|PubMed:16617059, ECO:0000269|PubMed:17472963, CC ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:27642067, CC ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, CC ECO:0000269|PubMed:8702602, ECO:0000269|PubMed:9425121}. 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:0000269|PubMed:10358058, ECO:0000269|PubMed:12672805, CC ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, CC ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:18451993, CC ECO:0000269|PubMed:7794891, ECO:0000269|PubMed:8619991, CC ECO:0000269|PubMed:8702602}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; CC Evidence={ECO:0000305|PubMed:18451993}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; CC Evidence={ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:16617059}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; CC Evidence={ECO:0000305|PubMed:12672805, ECO:0000305|PubMed:16617059}; 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:10358058, ECO:0000269|PubMed:12672805, CC ECO:0000269|PubMed:14709560, ECO:0000269|PubMed:16617059, CC ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; CC Evidence={ECO:0000305|PubMed:12672805, ECO:0000305|PubMed:17472963, CC ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3- CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:41075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:60657, ChEBI:CHEBI:74344; CC Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC octadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; CC Evidence={ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:7794891, CC ECO:0000269|PubMed:9425121}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; CC Evidence={ECO:0000305|PubMed:18451993}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3- CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn- CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; CC Evidence={ECO:0000269|PubMed:14709560}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; CC Evidence={ECO:0000305|PubMed:14709560}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3- CC phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1- CC octadecanoyl-sn-glycero-3-phosphocholine + H(+); CC Xref=Rhea:RHEA:41307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:32387, ChEBI:CHEBI:73858, ChEBI:CHEBI:78022; CC Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero- CC 3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn- CC glycero-3-phosphocholine + H(+) + hexadecanoate; CC Xref=Rhea:RHEA:41071, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:77694; CC Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3- CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O- CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; CC Evidence={ECO:0000269|PubMed:10358058, ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; CC Evidence={ECO:0000305|PubMed:10358058, ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) CC + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3- CC phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:41123, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:72828, ChEBI:CHEBI:75163; CC Evidence={ECO:0000269|PubMed:9425121}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124; CC Evidence={ECO:0000305|PubMed:9425121}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1- CC octadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:40451, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:74565, ChEBI:CHEBI:77091; CC Evidence={ECO:0000269|PubMed:9425121}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452; CC Evidence={ECO:0000305|PubMed:9425121}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; CC Evidence={ECO:0000269|PubMed:12672805, ECO:0000269|PubMed:16617059}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; CC Evidence={ECO:0000305|PubMed:12672805, ECO:0000305|PubMed:16617059}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O = CC H(+) + prostaglandin E2 + sn-glycero-3-phosphoethanolamine; CC Xref=Rhea:RHEA:53704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:137581, ChEBI:CHEBI:143890, ChEBI:CHEBI:606564; CC Evidence={ECO:0000269|PubMed:27642067}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705; CC Evidence={ECO:0000305|PubMed:27642067}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero- CC 3-phosphocholine + H2O = (15S)-hydroxy-(5Z,8Z,11Z,13E)- CC eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; CC Xref=Rhea:RHEA:53700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:57409, ChEBI:CHEBI:137584; CC Evidence={ECO:0000269|PubMed:27642067}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701; CC Evidence={ECO:0000305|PubMed:27642067}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero- CC 3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)- CC eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; CC Xref=Rhea:RHEA:53696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:78837, ChEBI:CHEBI:137583; CC Evidence={ECO:0000269|PubMed:27642067}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697; CC Evidence={ECO:0000305|PubMed:27642067}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H(+) CC + prostaglandin E2 + sn-glycerol 3-phosphocholine; CC Xref=Rhea:RHEA:53692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:137585, ChEBI:CHEBI:606564; CC Evidence={ECO:0000269|PubMed:27642067}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693; CC Evidence={ECO:0000305|PubMed:27642067}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero- CC 3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)- CC eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; CC Xref=Rhea:RHEA:53688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16870, ChEBI:CHEBI:78836, ChEBI:CHEBI:137582; CC Evidence={ECO:0000269|PubMed:27642067}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689; CC Evidence={ECO:0000305|PubMed:27642067}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3- CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O- CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, CC ChEBI:CHEBI:77695, ChEBI:CHEBI:77696; CC Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero- CC 3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)- CC glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; CC Xref=Rhea:RHEA:41099, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, CC ChEBI:CHEBI:74965, ChEBI:CHEBI:75612; CC Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3- CC phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol CC + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41087, CC ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:75610, CC ChEBI:CHEBI:78022; Evidence={ECO:0000269|PubMed:7794891}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088; CC Evidence={ECO:0000305|PubMed:7794891}; CC -!- ACTIVITY REGULATION: Activated by cytosolic calcium, which is necessary CC for binding to membrane lipids (PubMed:12672805). Activated by CC phosphorylation in response to mitogenic stimuli (PubMed:8381049). CC Activated by ceramide-1-phosphate. Binding (via C2 domain) to ceramide- CC 1-phosphate increases the affinity for membrane lipids CC (PubMed:17472963). Can be activated by phosphoinositides in the absence CC of calcium (PubMed:12672805). Inhibited by ANXA5 in a calcium- and CC substrate-dependent way (PubMed:9425121). {ECO:0000269|PubMed:12672805, CC ECO:0000269|PubMed:17472963, ECO:0000269|PubMed:8381049, CC ECO:0000269|PubMed:9425121}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=2.7 umol/min/mg enzyme toward CC 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine CC (phospholipase A2 activity) {ECO:0000269|PubMed:8083230}; CC Vmax=4.6 umol/min/mg enzyme toward CC 1-hexadecanoyl-sn-glycero-3-phosphocholine (lysophospholipase CC activity) {ECO:0000269|PubMed:8083230}; CC Vmax=24.5 nmol/min/mg enzyme toward CC 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine CC (phospholipase A2 activity in the absence of ceramide-1-phosphate) CC {ECO:0000269|PubMed:17472963}; CC Vmax=240.5 nmol/min/mg enzyme toward CC 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine CC (phospholipase A2 activity, in the presence of ceramide-1-phosphate) CC {ECO:0000269|PubMed:17472963}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000250|UniProtKB:P47713}. CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism. CC {ECO:0000269|PubMed:18451993}. CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC {ECO:0000269|PubMed:18451993}. CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. CC {ECO:0000269|PubMed:18451993}. CC -!- SUBUNIT: Interacts with KAT5. {ECO:0000269|PubMed:10319815, CC ECO:0000269|PubMed:11416127, ECO:0000269|PubMed:9430701, CC ECO:0000269|PubMed:9665851}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11375391}. Golgi CC apparatus membrane {ECO:0000269|PubMed:11375391}. Nucleus envelope. CC Note=Translocates to intracellular membranes in a calcium-dependent CC way. {ECO:0000269|PubMed:11375391}. CC -!- TISSUE SPECIFICITY: Expressed in various cells and tissues such as CC macrophages, neutrophils, fibroblasts and lung endothelium. Expressed CC in platelets (at protein level) (PubMed:25102815). CC {ECO:0000269|PubMed:25102815}. CC -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon CC calcium binding. It modulates enzyme activity by presenting the active CC site to its substrate in response to elevations of cytosolic calcium CC (PubMed:9430701, PubMed:9665851, PubMed:11375391). In the presence of CC phosphoinositides, regulates phospholipase A2 and lysophospholipase CC activities in a calcium-independent way (PubMed:12672805). CC {ECO:0000269|PubMed:11375391, ECO:0000269|PubMed:12672805, CC ECO:0000269|PubMed:9430701, ECO:0000269|PubMed:9665851}. CC -!- PTM: Phosphorylated at both Ser-505 and Ser-727 in response to CC mitogenic stimuli. {ECO:0000269|PubMed:8381049, CC ECO:0000269|PubMed:9468497}. CC -!- DISEASE: Gastrointestinal ulceration, recurrent, with dysfunctional CC platelets (GURDP) [MIM:618372]: An autosomal recessive disorder CC characterized by recurrent gastrointestinal mucosal ulcers, CC gastrointestinal bleeding, chronic anemia, iron deficiency, and CC abdominal pain. Disease features also include platelet dysfunction, and CC globally decreased eicosanoid synthesis. {ECO:0000269|PubMed:18451993, CC ECO:0000269|PubMed:23268370, ECO:0000269|PubMed:25102815}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/pla2g4a/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41733/PLA2G4A"; 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; M72393; AAB00789.1; -; mRNA. DR EMBL; M68874; AAA60105.1; -; mRNA. DR EMBL; AY552098; AAS45712.1; -; Genomic_DNA. DR EMBL; AL022147; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC114340; AAI14341.1; -; mRNA. DR CCDS; CCDS1372.1; -. DR PIR; A39329; A39329. DR RefSeq; NP_001298122.1; NM_001311193.1. DR RefSeq; NP_077734.1; NM_024420.2. DR RefSeq; XP_011507944.1; XM_011509642.2. DR PDB; 1BCI; NMR; -; A=1-138. DR PDB; 1CJY; X-ray; 2.50 A; A/B=1-749. DR PDB; 1RLW; X-ray; 2.40 A; A=17-141. DR PDBsum; 1BCI; -. DR PDBsum; 1CJY; -. DR PDBsum; 1RLW; -. DR AlphaFoldDB; P47712; -. DR BMRB; P47712; -. DR SMR; P47712; -. DR BioGRID; 111338; 60. DR DIP; DIP-40991N; -. DR IntAct; P47712; 17. DR MINT; P47712; -. DR STRING; 9606.ENSP00000356436; -. DR BindingDB; P47712; -. DR ChEMBL; CHEMBL3816; -. DR DrugBank; DB00041; Aldesleukin. DR DrugBank; DB00411; Carbamoylcholine. DR DrugBank; DB00578; Carbenicillin. DR DrugBank; DB06311; Darapladib. DR DrugBank; DB00445; Epirubicin. DR DrugBank; DB13867; Fluticasone. DR DrugBank; DB00588; Fluticasone propionate. DR DrugBank; DB05029; Lancovutide. DR DrugBank; DB04552; Niflumic acid. DR DrugBank; DB01083; Orlistat. DR DrugBank; DB00721; Procaine. DR DrugBank; DB01103; Quinacrine. DR DrugBank; DB00086; Streptokinase. DR DrugBank; DB04786; Suramin. DR DrugBank; DB04827; Urethane. DR DrugCentral; P47712; -. DR GuidetoPHARMACOLOGY; 1424; -. DR SwissLipids; SLP:000000565; -. DR iPTMnet; P47712; -. DR MetOSite; P47712; -. DR PhosphoSitePlus; P47712; -. DR BioMuta; PLA2G4A; -. DR DMDM; 317373312; -. DR EPD; P47712; -. DR jPOST; P47712; -. DR MassIVE; P47712; -. DR MaxQB; P47712; -. DR PaxDb; 9606-ENSP00000356436; -. DR PeptideAtlas; P47712; -. DR ProteomicsDB; 55788; -. DR Pumba; P47712; -. DR Antibodypedia; 4104; 460 antibodies from 38 providers. DR DNASU; 5321; -. DR Ensembl; ENST00000367466.4; ENSP00000356436.3; ENSG00000116711.10. DR GeneID; 5321; -. DR KEGG; hsa:5321; -. DR MANE-Select; ENST00000367466.4; ENSP00000356436.3; NM_024420.3; NP_077734.2. DR UCSC; uc001gsc.4; human. DR AGR; HGNC:9035; -. DR CTD; 5321; -. DR DisGeNET; 5321; -. DR GeneCards; PLA2G4A; -. DR HGNC; HGNC:9035; PLA2G4A. DR HPA; ENSG00000116711; Tissue enhanced (parathyroid gland, seminal vesicle). DR MalaCards; PLA2G4A; -. DR MIM; 600522; gene. DR MIM; 618372; phenotype. DR neXtProt; NX_P47712; -. DR OpenTargets; ENSG00000116711; -. DR Orphanet; 468635; Cryptogenic multifocal ulcerous stenosing enteritis. DR Orphanet; 477787; Cytosolic phospholipase-A2 alpha deficiency associated bleeding disorder. DR PharmGKB; PA271; -. DR VEuPathDB; HostDB:ENSG00000116711; -. DR eggNOG; KOG1012; Eukaryota. DR eggNOG; KOG1325; Eukaryota. DR GeneTree; ENSGT01030000234606; -. DR HOGENOM; CLU_011663_1_1_1; -. DR InParanoid; P47712; -. DR OMA; NFMRGLS; -. DR OrthoDB; 4250045at2759; -. DR PhylomeDB; P47712; -. DR TreeFam; TF325228; -. DR BioCyc; MetaCyc:HS04039-MONOMER; -. DR BRENDA; 3.1.1.4; 2681. DR PathwayCommons; P47712; -. DR Reactome; R-HSA-111995; phospho-PLA2 pathway. DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC. DR Reactome; R-HSA-1482798; Acyl chain remodeling of CL. 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-1483115; Hydrolysis of LPC. DR Reactome; R-HSA-1483166; Synthesis of PA. DR Reactome; R-HSA-2142753; Arachidonic acid metabolism. DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1. DR Reactome; R-HSA-432142; Platelet sensitization by LDL. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR SignaLink; P47712; -. DR SIGNOR; P47712; -. DR UniPathway; UPA00383; -. DR UniPathway; UPA00662; -. DR UniPathway; UPA00878; -. DR UniPathway; UPA00940; -. DR BioGRID-ORCS; 5321; 12 hits in 1163 CRISPR screens. DR ChiTaRS; PLA2G4A; human. DR EvolutionaryTrace; P47712; -. DR GeneWiki; PLA2G4A; -. DR GenomeRNAi; 5321; -. DR Pharos; P47712; Tchem. DR PRO; PR:P47712; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P47712; Protein. DR Bgee; ENSG00000116711; Expressed in seminal vesicle and 173 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB. DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:1902387; F:ceramide 1-phosphate binding; IDA:UniProtKB. DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB. DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB. DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB. DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:UniProtKB. DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB. DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB. DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl. DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central. DR GO; GO:0006690; P:icosanoid metabolic process; NAS:UniProtKB. DR GO; GO:0019370; P:leukotriene biosynthetic process; IMP:UniProtKB. DR GO; GO:0006640; P:monoacylglycerol biosynthetic process; IDA:UniProtKB. DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB. DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB. DR GO; GO:0034478; P:phosphatidylglycerol catabolic process; IDA:UniProtKB. DR GO; GO:0006663; P:platelet activating factor biosynthetic process; NAS:UniProtKB. DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl. DR GO; GO:0010572; P:positive regulation of platelet activation; IMP:UniProtKB. DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR CDD; cd04036; C2_cPLA2; 1. DR CDD; cd07200; cPLA2_Grp-IVA; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR041847; C2_cPLA2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR002642; LysoPLipase_cat_dom. DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1. DR PANTHER; PTHR10728:SF13; CYTOSOLIC PHOSPHOLIPASE A2; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF01735; PLA2_B; 1. DR SMART; SM00239; C2; 1. DR SMART; SM00022; PLAc; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS51210; PLA2C; 1. DR Genevisible; P47712; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cytoplasm; Direct protein sequencing; KW Disease variant; Fatty acid biosynthesis; Fatty acid metabolism; KW Glycerol metabolism; Golgi apparatus; Hydrolase; Isopeptide bond; KW Leukotriene biosynthesis; Lipid biosynthesis; Lipid degradation; KW Lipid metabolism; Lipid-binding; Membrane; Metal-binding; Nucleus; KW Phospholipid degradation; Phospholipid metabolism; Phosphoprotein; KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome; KW Ubl conjugation. FT CHAIN 1..749 FT /note="Cytosolic phospholipase A2" FT /id="PRO_0000187262" FT DOMAIN 6..122 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 140..740 FT /note="PLA2c" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555" FT REGION 1..178 FT /note="Phospholipid binding" FT /evidence="ECO:0000305" FT REGION 409..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 420..452 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 228 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:10319815, FT ECO:0000269|PubMed:8083230, ECO:0000269|PubMed:8619991, FT ECO:0000269|PubMed:8702602" FT ACT_SITE 549 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:10319815, FT ECO:0000269|PubMed:8702602" FT BINDING 40 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 40 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 41 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 43 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 43 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 65 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT BINDING 95 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 268 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50393" FT MOD_RES 435 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 505 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000269|PubMed:8381049, FT ECO:0000269|PubMed:9468497" FT MOD_RES 515 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50393" FT MOD_RES 727 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:9468497, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 729 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 541 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 606 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 103 FT /note="G -> R (in dbSNP:rs28395828)" FT /id="VAR_029276" FT VARIANT 111 FT /note="S -> P (in GURDP; uncertain significance; FT dbSNP:rs121434634)" FT /evidence="ECO:0000269|PubMed:18451993" FT /id="VAR_070778" FT VARIANT 224 FT /note="V -> I (in dbSNP:rs12720588)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_018760" FT VARIANT 442 FT /note="H -> Q (in a breast cancer sample; somatic mutation; FT dbSNP:rs370896190)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035826" FT VARIANT 485 FT /note="R -> H (in GURDP; uncertain significance; FT dbSNP:rs121434635)" FT /evidence="ECO:0000269|PubMed:18451993" FT /id="VAR_070779" FT VARIANT 575 FT /note="D -> H (in GURDP; decreased protein expression, if FT any, in platelets from homozygous patients; FT dbSNP:rs1557895416)" FT /evidence="ECO:0000269|PubMed:25102815" FT /id="VAR_082091" FT VARIANT 637 FT /note="I -> V (in dbSNP:rs28395831)" FT /id="VAR_062128" FT VARIANT 651 FT /note="R -> K (in dbSNP:rs2307198)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18451993, ECO:0000269|PubMed:1869522, FT ECO:0000269|PubMed:1904318, ECO:0000269|Ref.3" FT /id="VAR_018424" FT MUTAGEN 43 FT /note="D->N: Impairs phospholipase A2 and lysophospholipase FT activities in the absence of phosphoinositides. Has full FT activity in the presence of phosphoinositides." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 57..59 FT /note="RKR->AAA: Impairs binding to ceramide-1-phosphate." FT /evidence="ECO:0000269|PubMed:17472963" FT MUTAGEN 139 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-141 and A-151." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 141 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-139 and A-151." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 151 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-139 and A-141." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 195 FT /note="S->A: 5-fold reduced phospholipase and FT lysophospholipase activities. 100-fold reduced FT phospholipase and lysophospholipase activities; when FT associated with A-577." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 200 FT /note="R->A,H: Abolishes phospholipase activity." FT /evidence="ECO:0000269|PubMed:8702602" FT MUTAGEN 200 FT /note="R->K: Reduces phospholipase activity 200-fold." FT /evidence="ECO:0000269|PubMed:8702602" FT MUTAGEN 215 FT /note="S->A: No effect on phospholipase or FT lysophospholipase activity." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 220 FT /note="C->A: No effect on phospholipase activity." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 228 FT /note="S->A,C,T: Abolishes both phospholipase and FT lysophospholipase activities." FT /evidence="ECO:0000269|PubMed:8083230, FT ECO:0000269|PubMed:8619991, ECO:0000269|PubMed:8702602" FT MUTAGEN 324 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-331." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 331 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-324." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 437 FT /note="S->A: Reduces phospholipase A2 activity; when FT associated with A-454; A-505 and A-727." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 454 FT /note="S->A: Reduces phospholipase A2 activity; when FT associated with A-437; A-505 and A-727." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 488 FT /note="K->E: Impairs phosphoinositide-stimulated FT phospholipase A2 activity." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 505 FT /note="S->A: Decreases agonist-stimulated release of FT arachidonic acid. Reduces phospholipase A2 activity; when FT associated with A-437; A-454 and A-727." FT /evidence="ECO:0000269|PubMed:12672805, FT ECO:0000269|PubMed:8381049" FT MUTAGEN 541 FT /note="K->A: Impairs phosphoinositide-stimulated FT phospholipase A2 activity; when associated with A-543 and FT A-544." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 543 FT /note="K->A: Impairs phosphoinositide-stimulated FT phospholipase A2 activity.; when associated with A-541 and FT A-544." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 544 FT /note="K->A: Impairs phosphoinositide-stimulated FT phospholipase A2 activity.; when associated with A-541 and FT A-543." FT /evidence="ECO:0000269|PubMed:12672805" FT MUTAGEN 549 FT /note="D->A: Abolishes phospholipiase activity." FT /evidence="ECO:0000269|PubMed:8702602" FT MUTAGEN 549 FT /note="D->E: Reduces phospholipase activity 2000-fold." FT /evidence="ECO:0000269|PubMed:8702602" FT MUTAGEN 549 FT /note="D->N: Reduces phospholipase activity 300-fold." FT /evidence="ECO:0000269|PubMed:8702602" FT MUTAGEN 577 FT /note="S->A: 7-fold reduced phospholipase and FT lysophospholipase activities. 100-fold reduced FT phospholipase and lysophospholipase activities; when FT associated with A-195." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 620 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-634." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 634 FT /note="C->A: No effect on phospholipase activity; when FT associated with A-620." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 726 FT /note="C->A: No effect on phospholipase activity." FT /evidence="ECO:0000269|PubMed:8083230" FT MUTAGEN 727 FT /note="S->A: Reduces phospholipase A2 activity; when FT associated with A-437; A-455 and A-505." FT /evidence="ECO:0000269|PubMed:12672805" FT STRAND 18..29 FT /evidence="ECO:0007829|PDB:1RLW" FT HELIX 34..39 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 51..54 FT /evidence="ECO:0007829|PDB:1BCI" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:1BCI" FT STRAND 70..79 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 100..108 FT /evidence="ECO:0007829|PDB:1RLW" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:1RLW" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 128..137 FT /evidence="ECO:0007829|PDB:1RLW" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 152..177 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 198..214 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 228..239 FT /evidence="ECO:0007829|PDB:1CJY" FT TURN 241..245 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 248..260 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 269..284 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 291..304 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 313..318 FT /evidence="ECO:0007829|PDB:1CJY" FT TURN 319..321 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 326..333 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 344..349 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:1CJY" FT TURN 357..360 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 361..363 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 376..379 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 386..393 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 401..404 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 417..423 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 426..429 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 463..476 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:1CJY" FT TURN 492..495 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 543..548 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 558..561 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 570..575 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 588..599 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 611..615 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 619..623 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 636..641 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 646..648 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 650..652 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 660..666 FT /evidence="ECO:0007829|PDB:1CJY" FT STRAND 670..672 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 687..702 FT /evidence="ECO:0007829|PDB:1CJY" FT HELIX 705..718 FT /evidence="ECO:0007829|PDB:1CJY" SQ SEQUENCE 749 AA; 85239 MW; EE71CA0EBE617856 CRC64; MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGAFGDMLD TPDPYVELFI STTPDSRKRT RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFTVS SMKVGEKKEV PFIFNQVTEM VLEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKEHIRESMK KLLGPKNSEG LHSARDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYVAGLSGS TWYMSTLYSH PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG ETLIHNRMNT TLSSLKEKVN TAQCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QSRGSTMEEE LENITTKHIV SNDSSDSDDE SHEPKGTENE DAGSDYQSDN QASWIHRMIM ALVSDSALFN TREGRAGKVH NFMLGLNLNT SYPLSPLSDF ATQDSFDDDE LDAAVADPDE FERIYEPLDV KSKKIHVVDS GLTFNLPYPL ILRPQRGVDL IISFDFSARP SDSSPPFKEL LLAEKWAKMN KLPFPKIDPY VFDREGLKEC YVFKPKNPDM EKDCPTIIHF VLANINFRKY RAPGVPRETE EEKEIADFDI FDDPESPFST FNFQYPNQAF KRLHDLMHFN TLNNIDVIKE AMVESIEYRR QNPSRCSVSL SNVEARRFFN KEFLSKPKA //