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 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="https://atlasgeneticsoncology.org/gene/41733/PLA2G4A";
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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; 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 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 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.
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
//
