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Group 10 secretory phospholipase A2 (EC 3.1.1.4) (Group X secretory phospholipase A2) (GX sPLA2) (sPLA2-X) (Phosphatidylcholine 2-acylhydrolase 10)

 PA2GX_MOUSE             Reviewed;         151 AA.
Q9QXX3; Q9EQK6;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
31-JAN-2018, entry version 141.
RecName: Full=Group 10 secretory phospholipase A2;
EC=3.1.1.4;
AltName: Full=Group X secretory phospholipase A2;
Short=GX sPLA2;
Short=sPLA2-X;
AltName: Full=Phosphatidylcholine 2-acylhydrolase 10;
Flags: Precursor;
Name=Pla2g10;
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=10531313; DOI=10.1074/jbc.274.44.31195;
Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.;
"On the diversity of secreted phospholipases A2. Cloning, tissue
distribution, and functional expression of two novel mouse group II
enzymes.";
J. Biol. Chem. 274:31195-31202(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-30, AND
CHARACTERIZATION.
STRAIN=BALB/cJ;
PubMed=11019817; DOI=10.1006/abbi.2000.1977;
Morioka Y., Saiga A., Yokota Y., Suzuki N., Ikeda M., Ono T.,
Nakano K., Fujii N., Ishizaki J., Arita H., Hanasaki K.;
"Mouse group X secretory phospholipase A2 induces a potent release of
arachidonic acid from spleen cells and acts as a ligand for the
phospholipase A2 receptor.";
Arch. Biochem. Biophys. 381:31-42(2000).
-!- FUNCTION: PA2 catalyzes the calcium-dependent hydrolysis of the 2-
acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for
releasing arachidonic acid from cell membrane phospholipids.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate. {ECO:0000255|PROSITE-
ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in various tissues including the
lung, thymus, and spleen.
-!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF166097; AAF04498.2; -; mRNA.
EMBL; AF210429; AAG43522.1; -; mRNA.
CCDS; CCDS27967.1; -.
RefSeq; NP_036117.1; NM_011987.4.
UniGene; Mm.4214; -.
ProteinModelPortal; Q9QXX3; -.
SMR; Q9QXX3; -.
STRING; 10090.ENSMUSP00000023364; -.
BindingDB; Q9QXX3; -.
ChEMBL; CHEMBL4200; -.
PaxDb; Q9QXX3; -.
PRIDE; Q9QXX3; -.
Ensembl; ENSMUST00000023364; ENSMUSP00000023364; ENSMUSG00000022683.
GeneID; 26565; -.
KEGG; mmu:26565; -.
UCSC; uc007ygh.2; mouse.
CTD; 8399; -.
MGI; MGI:1347522; Pla2g10.
eggNOG; KOG4087; Eukaryota.
eggNOG; ENOG411283D; LUCA.
GeneTree; ENSGT00760000119160; -.
HOGENOM; HOG000231749; -.
HOVERGEN; HBG008137; -.
InParanoid; Q9QXX3; -.
KO; K01047; -.
OMA; ELLCKCD; -.
OrthoDB; EOG091G0UZ3; -.
PhylomeDB; Q9QXX3; -.
TreeFam; TF319283; -.
Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
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-1483166; Synthesis of PA.
PRO; PR:Q9QXX3; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022683; -.
CleanEx; MM_PLA2G10; -.
ExpressionAtlas; Q9QXX3; baseline and differential.
Genevisible; Q9QXX3; MM.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
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:0004620; F:phospholipase activity; IMP:BHF-UCL.
GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
GO; GO:0007411; P:axon guidance; ISO:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0051977; P:lysophospholipid transport; ISO:MGI.
GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:BHF-UCL.
GO; GO:0043433; P:negative regulation of DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:0010884; P:positive regulation of lipid storage; ISO:MGI.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:MGI.
GO; GO:0043030; P:regulation of macrophage activation; ISO:MGI.
CDD; cd00125; PLA2c; 1.
Gene3D; 1.20.90.10; -; 1.
InterPro; IPR001211; PLipase_A2.
InterPro; IPR033112; PLipase_A2_Asp_AS.
InterPro; IPR016090; PLipase_A2_dom.
InterPro; IPR036444; PLipase_A2_dom_sf.
InterPro; IPR033113; PLipase_A2_His_AS.
PANTHER; PTHR11716; PTHR11716; 1.
Pfam; PF00068; Phospholip_A2_1; 1.
PRINTS; PR00389; PHPHLIPASEA2.
SMART; SM00085; PA2c; 1.
SUPFAM; SSF48619; SSF48619; 1.
PROSITE; PS00119; PA2_ASP; 1.
PROSITE; PS00118; PA2_HIS; 1.
1: Evidence at protein level;
Calcium; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Hydrolase;
Lipid degradation; Lipid metabolism; Metal-binding;
Reference proteome; Secreted; Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:11019817}.
PROPEP 18 28
/FTId=PRO_0000022766.
CHAIN 29 151 Group 10 secretory phospholipase A2.
/FTId=PRO_0000022767.
ACT_SITE 74 74 {ECO:0000250}.
ACT_SITE 119 119 {ECO:0000250}.
METAL 54 54 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 56 56 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 58 58 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 75 75 Calcium. {ECO:0000250}.
DISULFID 39 97 {ECO:0000250}.
DISULFID 53 143 {ECO:0000250}.
DISULFID 55 71 {ECO:0000250}.
DISULFID 70 125 {ECO:0000250}.
DISULFID 76 150 {ECO:0000250}.
DISULFID 77 118 {ECO:0000250}.
DISULFID 86 111 {ECO:0000250}.
DISULFID 104 116 {ECO:0000250}.
CONFLICT 151 151 N -> D (in Ref. 2; AAG43522).
{ECO:0000305}.
SEQUENCE 151 AA; 17005 MW; 05D15E70BC2C9294 CRC64;
MLLLLLLLLL GPGPGFSEAT RRSHVYKRGL LELAGTLDCV GPRSPMAYMN YGCYCGLGGH
GEPRDAIDWC CYHHDCCYSR AQDAGCSPKL DRYPWKCMDH HILCGPAENK CQELLCRCDE
ELAYCLAGTE YHLKYLFFPS ILCEKDSPKC N


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