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85/88 kDa calcium-independent phospholipase A2 (CaI-PLA2) (EC 3.1.1.4) (Group VI phospholipase A2) (GVI PLA2) (Intracellular membrane-associated calcium-independent phospholipase A2 beta) (iPLA2-beta) (Patatin-like phospholipase domain-containing protein 9) (PNPLA9)

 PLPL9_MOUSE             Reviewed;         807 AA.
P97819; Q99LA9; Q9JK61;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
31-OCT-2012, sequence version 3.
23-MAY-2018, entry version 154.
RecName: Full=85/88 kDa calcium-independent phospholipase A2;
Short=CaI-PLA2;
EC=3.1.1.4;
AltName: Full=Group VI phospholipase A2;
Short=GVI PLA2;
AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 beta;
Short=iPLA2-beta;
AltName: Full=Patatin-like phospholipase domain-containing protein 9;
Short=PNPLA9;
Name=Pla2g6; Synonyms=Pnpla9;
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] (ISOFORM SHORT).
STRAIN=DBA/2J;
PubMed=9079688; DOI=10.1074/jbc.272.13.8576;
Balboa M.A., Balsinde J., Jones S.S., Dennis E.A.;
"Identity between the Ca2+-independent phospholipase A2 enzymes from
P388D1 macrophages and Chinese hamster ovary cells.";
J. Biol. Chem. 272:8576-8580(1997).
[2]
SEQUENCE REVISION TO 2-3; 9; 11 AND 211.
Balboa M.A., Balsinde J., Jones S.S., Dennis E.A.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE SPLICING, AND
SUBCELLULAR LOCATION.
STRAIN=NIH Swiss;
PubMed=11563837; DOI=10.1006/bbrc.2001.5632;
Chiu C.-H., Jackowski S.;
"Role of calcium-independent phospholipases (iPLA(2)) in
phosphatidylcholine metabolism.";
Biochem. Biophys. Res. Commun. 287:600-606(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
STRAIN=C57BL/6J, FVB/N, and NMRI; 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).
[5]
PROTEIN SEQUENCE OF 479-491, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Liver, 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: Catalyzes the release of fatty acids from phospholipids.
It has been implicated in normal phospholipid remodeling, nitric
oxide-induced or vasopressin-induced arachidonic acid release and
in leukotriene and prostaglandin production. May participate in
fas mediated apoptosis and in regulating transmembrane ion flux in
glucose-stimulated B-cells. Has a role in cardiolipin (CL)
deacylation. Required for both speed and directionality of
monocyte MCP1/CCL2-induced chemotaxis through regulation of F-
actin polymerization at the pseudopods (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
-!- ENZYME REGULATION: Inhibited by calcium-activated calmodulin.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Long: Membrane; Peripheral membrane
protein. Note=Recruited to the membrane-enriched pseudopod upon
MCP1/CCL2 stimulation in monocytes. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform Short: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long; Synonyms=iPLA2-L;
IsoId=P97819-1; Sequence=Displayed;
Name=Short; Synonyms=iPLA2-S;
IsoId=P97819-2; Sequence=VSP_044364;
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U88624; AAB48511.2; -; mRNA.
EMBL; AF259401; AAF72651.1; -; mRNA.
EMBL; BC003487; AAH03487.1; -; mRNA.
EMBL; BC057209; AAH57209.1; -; mRNA.
CCDS; CCDS27637.1; -. [P97819-2]
CCDS; CCDS56991.1; -. [P97819-1]
RefSeq; NP_001185952.1; NM_001199023.1. [P97819-1]
RefSeq; NP_001185953.1; NM_001199024.1. [P97819-2]
RefSeq; NP_001185954.1; NM_001199025.1. [P97819-2]
RefSeq; NP_058611.1; NM_016915.4. [P97819-2]
RefSeq; XP_006521215.1; XM_006521152.2. [P97819-1]
RefSeq; XP_006521216.1; XM_006521153.3. [P97819-1]
RefSeq; XP_006521217.1; XM_006521154.1. [P97819-1]
RefSeq; XP_006521218.1; XM_006521155.2. [P97819-1]
RefSeq; XP_006521219.1; XM_006521156.3. [P97819-1]
RefSeq; XP_006521220.1; XM_006521157.3. [P97819-1]
RefSeq; XP_006521221.1; XM_006521158.2. [P97819-1]
RefSeq; XP_006521222.1; XM_006521159.3. [P97819-1]
RefSeq; XP_006521223.1; XM_006521160.2. [P97819-1]
RefSeq; XP_017172187.1; XM_017316698.1. [P97819-2]
UniGene; Mm.155620; -.
ProteinModelPortal; P97819; -.
SMR; P97819; -.
IntAct; P97819; 3.
STRING; 10090.ENSMUSP00000134672; -.
ChEMBL; CHEMBL3259503; -.
iPTMnet; P97819; -.
PhosphoSitePlus; P97819; -.
MaxQB; P97819; -.
PaxDb; P97819; -.
PeptideAtlas; P97819; -.
PRIDE; P97819; -.
Ensembl; ENSMUST00000047816; ENSMUSP00000044234; ENSMUSG00000042632. [P97819-2]
Ensembl; ENSMUST00000166977; ENSMUSP00000132071; ENSMUSG00000042632. [P97819-2]
Ensembl; ENSMUST00000172403; ENSMUSP00000131081; ENSMUSG00000042632. [P97819-2]
Ensembl; ENSMUST00000173163; ENSMUSP00000134456; ENSMUSG00000042632. [P97819-2]
Ensembl; ENSMUST00000174021; ENSMUSP00000134672; ENSMUSG00000042632. [P97819-1]
GeneID; 53357; -.
KEGG; mmu:53357; -.
UCSC; uc007wtd.2; mouse. [P97819-1]
CTD; 8398; -.
MGI; MGI:1859152; Pla2g6.
eggNOG; KOG0513; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG3621; LUCA.
GeneTree; ENSGT00530000063645; -.
HOGENOM; HOG000013092; -.
HOVERGEN; HBG053482; -.
InParanoid; P97819; -.
KO; K16343; -.
OMA; RAWCEMI; -.
OrthoDB; EOG091G042U; -.
TreeFam; TF319230; -.
Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
PRO; PR:P97819; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000042632; -.
CleanEx; MM_PLA2G6; -.
ExpressionAtlas; P97819; baseline and differential.
Genevisible; P97819; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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:0017171; F:serine hydrolase activity; IDA:MGI.
GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:MGI.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IEA:Ensembl.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IEA:Ensembl.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:1901339; P:regulation of store-operated calcium channel activity; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR002641; PNPLA_dom.
Pfam; PF12796; Ank_2; 2.
Pfam; PF01734; Patatin; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 6.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF52151; SSF52151; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 4.
PROSITE; PS51635; PNPLA; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calmodulin-binding; Chemotaxis;
Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase;
Lipid degradation; Lipid metabolism; Membrane; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 807 85/88 kDa calcium-independent
phospholipase A2.
/FTId=PRO_0000067038.
REPEAT 151 181 ANK 1.
REPEAT 185 215 ANK 2.
REPEAT 219 248 ANK 3.
REPEAT 251 281 ANK 4.
REPEAT 286 312 ANK 5.
REPEAT 316 345 ANK 6.
REPEAT 349 378 ANK 7.
DOMAIN 482 666 PNPLA. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
REGION 678 697 Calmodulin-binding. {ECO:0000250}.
REGION 749 760 Calmodulin-binding. {ECO:0000250}.
MOTIF 486 491 GXGXXG. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOTIF 518 522 GXSXG. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOTIF 653 655 DGA/G. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
ACT_SITE 520 520 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
ACT_SITE 653 653 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU01161}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P97570}.
VAR_SEQ 396 451 LITRKALLTLLKTVGADHHFPIIQGVSTEQGSAAATHPLFS
LDRTQPPAISLNNLE -> Q (in isoform Short).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9079688}.
/FTId=VSP_044364.
SEQUENCE 807 AA; 89560 MW; 3838889731100294 CRC64;
MQFFGRLVNT LSSVTNLFSN PFRVKEVSLT DYVSSERVRE EGQLILLQNV SNRTWDCVLV
SPRNPQSGFR LFQLESEADA LVNFQQFSSQ LPPFYESSVQ VLHVEVLQHL TDLIRNHPSW
TVTHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD
VTDNKGETAF HYAVQGDNPQ VLQLLGKNAS AGLNQVNNQG LTPLHLACKM GKQEMVRVLL
LCNARCNIMG PGGFPIHTAM KFSQKGCAEM IISMDSNQIH SKDPRYGASP LHWAKNAEMA
RMLLKRGCDV DSTSSSGNTA LHVAVMRNRF DCVMVLLTYG ANAGARGEHG NTPLHLAMSK
DNMEMVKALI VFGAEVDTPN DFGETPALIA SKISKLITRK ALLTLLKTVG ADHHFPIIQG
VSTEQGSAAA THPLFSLDRT QPPAISLNNL ELQDLMPISR ARKPAFILSS MRDEKRSHDH
LLCLDGGGVK GLVIIQLLIA IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG
VYFRMKDEVF RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
RNYDAPEAVR EPRCNQNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR FLDGGLLANN
PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGKSP QVPVTCVDVF RPSNPWELAK
TVFGAKELGK MVVDCCTDPD GRAVDRARAW CEMVGIQYFR LNPQLGSDIM LDEVSDAVLV
NALWETEVYI YEHREEFQKL VQLLLSP


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