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Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)]

 PA24A_MOUSE             Reviewed;         748 AA.
P47713;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 167.
RecName: Full=Cytosolic phospholipase A2;
Short=cPLA2;
AltName: Full=Phospholipase A2 group IVA;
Includes:
RecName: Full=Phospholipase A2;
EC=3.1.1.4;
AltName: Full=Phosphatidylcholine 2-acylhydrolase;
Includes:
RecName: Full=Lysophospholipase;
EC=3.1.1.5;
Name=Pla2g4a; Synonyms=Cpla2, Pla2g4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1904318; DOI=10.1016/0092-8674(91)90556-E;
Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A.,
Lin A.Y., Milona N., Knopf J.L.;
"A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-
dependent translocation domain with homology to PKC and GAP.";
Cell 65:1043-1051(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION AT SER-505 AND SER-726, AND ACTIVATION.
PubMed=10978317; DOI=10.1074/jbc.M003395200;
Hefner Y., Boersch-Haubold A.G., Murakami M., Wilde J.I., Pasquet S.,
Schieltz D., Ghomashchi F., Yates J.R. III, Armstrong C.G.,
Paterson A., Cohen P., Fukunaga R., Hunter T., Kudo I., Watson S.P.,
Gelb M.H.;
"Serine 727 phosphorylation and activation of cytosolic phospholipase
A2 by MNK1-related protein kinases.";
J. Biol. Chem. 275:37542-37551(2000).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435; SER-437; SER-505;
SER-726 AND SER-728, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the
sn-2 position releasing arachidonic acid. Together with its
lysophospholipid activity, it is implicated in the initiation of
the inflammatory response.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
-!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
glycerophosphocholine + a carboxylate.
-!- ACTIVITY REGULATION: Stimulated by agonists such as ATP, EGF,
thrombin and bradykinin as well as by cytosolic Ca(2+).
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
Note=Translocates to membrane vesicles in a calcium-dependent
fashion.
-!- DOMAIN: The N-terminal C2 domain associates with lipid membranes
upon calcium binding. It modulates enzyme activity by presenting
the active site to its substrate in response to elevations of
cytosolic Ca(2+) (By similarity). {ECO:0000250}.
-!- PTM: Activated by phosphorylation at both Ser-505 and Ser-726.
{ECO:0000269|PubMed:10978317}.
-----------------------------------------------------------------------
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EMBL; M72394; AAB00796.1; -; mRNA.
EMBL; BC003816; AAH03816.1; -; mRNA.
CCDS; CCDS15352.1; -.
PIR; B39898; B39898.
RefSeq; NP_032895.1; NM_008869.4.
UniGene; Mm.4186; -.
ProteinModelPortal; P47713; -.
SMR; P47713; -.
BioGrid; 202222; 11.
IntAct; P47713; 14.
MINT; P47713; -.
STRING; 10090.ENSMUSP00000070868; -.
BindingDB; P47713; -.
ChEMBL; CHEMBL2907; -.
iPTMnet; P47713; -.
PhosphoSitePlus; P47713; -.
SwissPalm; P47713; -.
PaxDb; P47713; -.
PeptideAtlas; P47713; -.
PRIDE; P47713; -.
Ensembl; ENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
GeneID; 18783; -.
KEGG; mmu:18783; -.
UCSC; uc007cxt.2; mouse.
CTD; 5321; -.
MGI; MGI:1195256; Pla2g4a.
eggNOG; KOG1012; Eukaryota.
eggNOG; KOG1325; Eukaryota.
eggNOG; ENOG410XR72; LUCA.
GeneTree; ENSGT00550000074489; -.
HOGENOM; HOG000115420; -.
HOVERGEN; HBG053479; -.
InParanoid; P47713; -.
KO; K16342; -.
OMA; RFSMALC; -.
OrthoDB; EOG091G0276; -.
PhylomeDB; P47713; -.
TreeFam; TF325228; -.
BRENDA; 3.1.1.4; 3474.
Reactome; R-MMU-111995; phospho-PLA2 pathway.
Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
Reactome; R-MMU-1482798; Acyl chain remodeling of CL.
Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
Reactome; R-MMU-1483115; Hydrolysis of LPC.
Reactome; R-MMU-1483166; Synthesis of PA.
Reactome; R-MMU-2142753; Arachidonic acid metabolism.
Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-MMU-432142; Platelet sensitization by LDL.
Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
SABIO-RK; P47713; -.
PMAP-CutDB; P47713; -.
PRO; PR:P47713; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000056220; Expressed in 276 organ(s), highest expression level in indifferent gonad.
ExpressionAtlas; P47713; baseline and differential.
Genevisible; P47713; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005811; C:lipid droplet; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0042588; C:zymogen granule; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISO:MGI.
GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0019369; P:arachidonic acid metabolic process; ISO:MGI.
GO; GO:0050482; P:arachidonic acid secretion; IDA:UniProtKB.
GO; GO:0071236; P:cellular response to antibiotic; IDA:MGI.
GO; GO:0046697; P:decidualization; ISO:MGI.
GO; GO:0046456; P:icosanoid biosynthetic process; IMP:MGI.
GO; GO:0001542; P:ovulation from ovarian follicle; ISO:MGI.
GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; ISO:MGI.
GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0043129; P:surfactant homeostasis; ISO:MGI.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR002642; LysoPLipase_cat_dom.
Pfam; PF00168; C2; 1.
Pfam; PF01735; PLA2_B; 1.
SMART; SM00239; C2; 1.
SMART; SM00022; PLAc; 1.
SUPFAM; SSF52151; SSF52151; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS51210; PLA2C; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Hydrolase;
Isopeptide bond; Lipid degradation; Lipid metabolism; Metal-binding;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 748 Cytosolic phospholipase A2.
/FTId=PRO_0000187263.
DOMAIN 5 106 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 140 739 PLA2c. {ECO:0000255|PROSITE-
ProRule:PRU00555}.
REGION 1 178 Phospholipid binding. {ECO:0000305}.
ACT_SITE 228 228 Nucleophile. {ECO:0000250}.
ACT_SITE 548 548 Proton acceptor. {ECO:0000250}.
METAL 40 40 Calcium 1. {ECO:0000250}.
METAL 40 40 Calcium 2. {ECO:0000250}.
METAL 41 41 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 43 43 Calcium 1. {ECO:0000250}.
METAL 43 43 Calcium 2. {ECO:0000250}.
METAL 65 65 Calcium 1. {ECO:0000250}.
METAL 93 93 Calcium 2. {ECO:0000250}.
METAL 94 94 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 95 95 Calcium 2. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P47712}.
MOD_RES 268 268 Phosphothreonine.
{ECO:0000250|UniProtKB:P47712}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P50393}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 505 505 Phosphoserine; by MAPK.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10978317}.
MOD_RES 515 515 Phosphoserine.
{ECO:0000250|UniProtKB:P50393}.
MOD_RES 726 726 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10978317}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 540 540 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P47712}.
CROSSLNK 605 605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P47712}.
SEQUENCE 748 AA; 85222 MW; 49D12BBB2911492A CRC64;
MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI STTPDSRKRT
RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV
PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKENIKENMK KLLGPKKSEG
LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
ETLIQNRMSM TLSSLKEKVN AARCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QNKGSTMEEE
LENITAKHIV SNDSSDSDDE AQGPKGTENE EAEKEYQSDN QASWVHRMLM ALVSDSALFN
TREGRAGKVH NFMLGLNLNT SYPLSPLRDF SSQDSFDDEL DAAVADPDEF ERIYEPLDVK
SKKIHVVDSG LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK
LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPTIIHFV LANINFRKYK APGVLRETKE
EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT LNNIDVIKDA IVESIEYRRQ
NPSRCSVSLS NVEARKFFNK EFLSKPTV


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