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PA24A_HUMAN
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   03-AUG-2022, entry version 215.
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 = (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate
CC         + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         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 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC         eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2
CC         activity) {ECO:0000269|PubMed:8083230};
CC         Vmax=4.6 umol/min/mg enzyme toward 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine (lysophospholipase activity)
CC         {ECO:0000269|PubMed:8083230};
CC         Vmax=24.5 nmol/min/mg enzyme toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC         eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2
CC         activity in the absence of ceramide-1-phosphate)
CC         {ECO:0000269|PubMed:17472963};
CC         Vmax=240.5 nmol/min/mg enzyme toward 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC         eicosatetraenoyl)-sn-glycero-3-phosphocholine (phospholipase A2
CC         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="http://atlasgeneticsoncology.org/Genes/PLA2G4AID41733ch1q31.html";
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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; 41.
DR   DIP; DIP-40991N; -.
DR   IntAct; P47712; 16.
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; P47712; -.
DR   PeptideAtlas; P47712; -.
DR   PRIDE; P47712; -.
DR   ProteomicsDB; 55788; -.
DR   Antibodypedia; 4104; 416 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   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; KFFMGKV; -.
DR   OrthoDB; 302848at2759; -.
DR   PhylomeDB; P47712; -.
DR   TreeFam; TF325228; -.
DR   BioCyc; MetaCyc:HS04039-MON; -.
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; 9 hits in 1076 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 171 other tissues.
DR   Genevisible; P47712; HS.
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   Gene3D; 2.60.40.150; -; 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   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
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; unknown pathological 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; unknown pathological 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
 
 
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